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PDBsum entry 3oaa

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Hydrolase/transport protein PDB id
3oaa
Jmol
Contents
Protein chains
(+ 6 more) 488 a.a.
(+ 6 more) 458 a.a.
284 a.a.
138 a.a.
Ligands
ANP ×12
ADP ×4
SO4 ×17
Metals
_MG ×16
Waters ×64
HEADER    HYDROLASE/TRANSPORT PROTEIN             05-AUG-10   3OAA
TITLE     STRUCTURE OF THE E.COLI F1-ATP SYNTHASE INHIBITED BY SUBUNIT EPSILON
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ATP SYNTHASE SUBUNIT ALPHA;
COMPND   3 CHAIN: A, B, C, I, J, K, Q, R, S, Y, Z, a;
COMPND   4 EC: 3.6.3.14;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: ATP SYNTHASE SUBUNIT BETA;
COMPND   8 CHAIN: D, E, F, L, M, N, T, U, V, b, c, d;
COMPND   9 EC: 3.6.3.14;
COMPND  10 ENGINEERED: YES;
COMPND  11 MUTATION: YES;
COMPND  12 MOL_ID: 3;
COMPND  13 MOLECULE: ATP SYNTHASE GAMMA CHAIN;
COMPND  14 CHAIN: G, O, W, e;
COMPND  15 ENGINEERED: YES;
COMPND  16 MOL_ID: 4;
COMPND  17 MOLECULE: ATP SYNTHASE EPSILON CHAIN;
COMPND  18 CHAIN: H, P, X, f;
COMPND  19 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI DH1;
SOURCE   3 ORGANISM_TAXID: 536056;
SOURCE   4 STRAIN: ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1;
SOURCE   5 GENE: ATPA, ECDH1_4233;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 MOL_ID: 2;
SOURCE   9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI DH1;
SOURCE  10 ORGANISM_TAXID: 536056;
SOURCE  11 STRAIN: ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1;
SOURCE  12 GENE: ATPD, ECDH1_4235;
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  15 MOL_ID: 3;
SOURCE  16 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI DH1;
SOURCE  17 ORGANISM_TAXID: 536056;
SOURCE  18 STRAIN: ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1;
SOURCE  19 GENE: ECDH1_4234;
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  22 MOL_ID: 4;
SOURCE  23 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI DH1;
SOURCE  24 ORGANISM_TAXID: 536056;
SOURCE  25 STRAIN: ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1;
SOURCE  26 GENE: ATPC, ECDH1_4236;
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    ROSSMANN FOLD, HYDROLASE, SYNTHASE, HYDROLASE-TRANSPORT PROTEIN
KEYWDS   2 COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.CINGOLANI,T.M.DUNCAN
REVDAT   2   18-APR-12 3OAA    1       VERSN
REVDAT   1   25-MAY-11 3OAA    0
JRNL        AUTH   G.CINGOLANI,T.M.DUNCAN
JRNL        TITL   STRUCTURAL BASIS FOR INHIBITION OF BACTERIAL ATP SYNTHASE BY
JRNL        TITL 2 SUBUNIT EPSILON OF THE ROTOR STALK
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    3.26 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.3_473)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.26
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0
REMARK   3   NUMBER OF REFLECTIONS             : 252275
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.243
REMARK   3   R VALUE            (WORKING SET) : 0.243
REMARK   3   FREE R VALUE                     : 0.265
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 79.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 14.9999 -  7.5372    0.97    17940   144  0.1683 0.1577
REMARK   3     2  7.5372 -  6.1144    0.99    18093   144  0.2236 0.2693
REMARK   3     3  6.1144 -  5.3822    0.99    18127   146  0.2397 0.2597
REMARK   3     4  5.3822 -  4.9090    1.00    18230   145  0.2223 0.2612
REMARK   3     5  4.9090 -  4.5678    0.99    18135   144  0.1968 0.2227
REMARK   3     6  4.5678 -  4.3053    1.00    18124   145  0.2061 0.2554
REMARK   3     7  4.3053 -  4.0942    0.99    18103   145  0.2359 0.2720
REMARK   3     8  4.0942 -  3.9193    1.00    18158   146  0.2609 0.3059
REMARK   3     9  3.9193 -  3.7709    1.00    18112   144  0.2826 0.3117
REMARK   3    10  3.7709 -  3.6427    1.00    18063   144  0.3069 0.3246
REMARK   3    11  3.6427 -  3.5303    1.00    18091   145  0.3247 0.3263
REMARK   3    12  3.5303 -  3.4307    0.99    18097   145  0.3410 0.3763
REMARK   3    13  3.4307 -  3.3414    0.99    17989   143  0.3637 0.3402
REMARK   3    14  3.3414 -  3.2600    0.83    15013   120  0.3855 0.4051
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.10
REMARK   3   SHRINKAGE RADIUS   : 0.83
REMARK   3   K_SOL              : 0.26
REMARK   3   B_SOL              : 37.47
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.470
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 79.38
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 118.36
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -4.29640
REMARK   3    B22 (A**2) : -5.48240
REMARK   3    B33 (A**2) : -2.60160
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : 1.48460
REMARK   3    B23 (A**2) : -0.00000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.004         101060
REMARK   3   ANGLE     :  0.821         136804
REMARK   3   CHIRALITY :  0.058          15664
REMARK   3   PLANARITY :  0.003          17872
REMARK   3   DIHEDRAL  : 22.888          64092
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 96
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: (CHAIN A AND RESID 24:94 )
REMARK   3    ORIGIN FOR THE GROUP (A): -85.2629 -60.3585  21.9190
REMARK   3    T TENSOR
REMARK   3      T11:   0.8514 T22:   0.3387
REMARK   3      T33:   1.1253 T12:  -0.1656
REMARK   3      T13:  -0.1208 T23:  -0.1871
REMARK   3    L TENSOR
REMARK   3      L11:   0.4592 L22:   0.6199
REMARK   3      L33:   0.6221 L12:  -0.2173
REMARK   3      L13:  -0.0148 L23:   0.2207
REMARK   3    S TENSOR
REMARK   3      S11:   0.2086 S12:  -0.1475 S13:  -0.6333
REMARK   3      S21:  -0.0541 S22:  -0.3312 S23:   0.2033
REMARK   3      S31:   0.2222 S32:  -0.2756 S33:  -0.0002
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: (CHAIN A AND RESID 95:382 )
REMARK   3    ORIGIN FOR THE GROUP (A): -71.2239 -38.3181  36.2691
REMARK   3    T TENSOR
REMARK   3      T11:   0.3639 T22:   0.3470
REMARK   3      T33:   0.4873 T12:  -0.2053
REMARK   3      T13:   0.0272 T23:  -0.0233
REMARK   3    L TENSOR
REMARK   3      L11:   2.1729 L22:   4.0759
REMARK   3      L33:   2.5022 L12:   0.5226
REMARK   3      L13:  -0.0799 L23:   0.2609
REMARK   3    S TENSOR
REMARK   3      S11:   0.4007 S12:  -0.5845 S13:  -0.0426
REMARK   3      S21:   0.6370 S22:  -0.2929 S23:   0.3179
REMARK   3      S31:   0.1183 S32:   0.0181 S33:   0.0000
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: (CHAIN A AND RESID 383:511 )
REMARK   3    ORIGIN FOR THE GROUP (A): -51.6032 -17.4065  47.9917
REMARK   3    T TENSOR
REMARK   3      T11:   1.0004 T22:   0.9048
REMARK   3      T33:   0.4972 T12:  -0.4419
REMARK   3      T13:  -0.0502 T23:  -0.0691
REMARK   3    L TENSOR
REMARK   3      L11:   0.7299 L22:   1.2842
REMARK   3      L33:   0.9416 L12:   0.0627
REMARK   3      L13:  -0.4806 L23:   0.7109
REMARK   3    S TENSOR
REMARK   3      S11:   0.2118 S12:  -0.5516 S13:   0.0272
REMARK   3      S21:   0.6413 S22:  -0.3511 S23:  -0.4954
REMARK   3      S31:  -0.2807 S32:   0.5897 S33:  -0.0001
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: (CHAIN A AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -54.4512 -36.4997  32.1082
REMARK   3    T TENSOR
REMARK   3      T11:   0.6130 T22:   1.0782
REMARK   3      T33:   0.7684 T12:  -0.1199
REMARK   3      T13:  -0.2518 T23:  -0.2522
REMARK   3    L TENSOR
REMARK   3      L11:   0.0251 L22:   0.0305
REMARK   3      L33:   0.0538 L12:   0.0268
REMARK   3      L13:   0.0175 L23:   0.0100
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2241 S12:  -0.0013 S13:   0.1522
REMARK   3      S21:   0.4274 S22:  -0.1967 S23:  -0.3820
REMARK   3      S31:  -0.0686 S32:   0.3333 S33:   0.0011
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: (CHAIN B AND RESID 26:94 )
REMARK   3    ORIGIN FOR THE GROUP (A):-109.8609 -35.8632  -2.2778
REMARK   3    T TENSOR
REMARK   3      T11:   0.5595 T22:   0.6060
REMARK   3      T33:   1.7646 T12:  -0.2988
REMARK   3      T13:  -0.5610 T23:  -0.0878
REMARK   3    L TENSOR
REMARK   3      L11:   0.1853 L22:   0.1583
REMARK   3      L33:   0.5318 L12:  -0.0119
REMARK   3      L13:  -0.0872 L23:  -0.0341
REMARK   3    S TENSOR
REMARK   3      S11:   0.0070 S12:   0.1298 S13:  -0.1527
REMARK   3      S21:  -0.4382 S22:   0.2218 S23:   1.2414
REMARK   3      S31:   0.3664 S32:  -0.1953 S33:   0.0001
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: (CHAIN B AND RESID 95:382 )
REMARK   3    ORIGIN FOR THE GROUP (A): -97.8769  -9.3330  -7.2418
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1232 T22:   0.0497
REMARK   3      T33:   1.3018 T12:  -0.4372
REMARK   3      T13:  -0.6939 T23:  -0.1207
REMARK   3    L TENSOR
REMARK   3      L11:   2.4584 L22:   3.0307
REMARK   3      L33:   2.0433 L12:   0.5383
REMARK   3      L13:  -0.6650 L23:  -0.2215
REMARK   3    S TENSOR
REMARK   3      S11:   0.3522 S12:   0.5186 S13:   0.7446
REMARK   3      S21:  -0.7991 S22:   0.0432 S23:   1.3073
REMARK   3      S31:  -0.6643 S32:  -0.5216 S33:   0.0356
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: (CHAIN B AND RESID 383:511 )
REMARK   3    ORIGIN FOR THE GROUP (A): -85.2758  18.9967  -7.9716
REMARK   3    T TENSOR
REMARK   3      T11:   1.2174 T22:   0.7300
REMARK   3      T33:   1.5074 T12:  -0.1991
REMARK   3      T13:  -0.2754 T23:   0.1515
REMARK   3    L TENSOR
REMARK   3      L11:   0.1614 L22:   0.6061
REMARK   3      L33:   1.1238 L12:  -0.1277
REMARK   3      L13:  -0.1187 L23:   0.0172
REMARK   3    S TENSOR
REMARK   3      S11:   0.0050 S12:   0.1576 S13:   0.6464
REMARK   3      S21:  -0.6003 S22:   0.1612 S23:  -0.2192
REMARK   3      S31:  -0.8199 S32:   0.6970 S33:  -0.0000
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: (CHAIN B AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -91.6285  -0.9179   6.6411
REMARK   3    T TENSOR
REMARK   3      T11:   1.1635 T22:   0.4451
REMARK   3      T33:   2.1700 T12:  -0.0121
REMARK   3      T13:  -0.2725 T23:  -0.0796
REMARK   3    L TENSOR
REMARK   3      L11:   0.0237 L22:   0.0097
REMARK   3      L33:   0.0320 L12:  -0.0021
REMARK   3      L13:  -0.0066 L23:   0.0172
REMARK   3    S TENSOR
REMARK   3      S11:   0.2613 S12:  -0.2147 S13:   0.1513
REMARK   3      S21:   0.3005 S22:   0.1775 S23:   0.1095
REMARK   3      S31:  -0.3813 S32:  -0.0566 S33:   0.0019
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: (CHAIN C AND RESID 25:94 )
REMARK   3    ORIGIN FOR THE GROUP (A): -79.2923 -58.4176 -20.3854
REMARK   3    T TENSOR
REMARK   3      T11:   1.1914 T22:   0.6624
REMARK   3      T33:   1.0501 T12:  -0.2029
REMARK   3      T13:  -0.2934 T23:  -0.4114
REMARK   3    L TENSOR
REMARK   3      L11:   0.3395 L22:   0.2314
REMARK   3      L33:   0.3587 L12:  -0.2732
REMARK   3      L13:   0.1850 L23:  -0.2163
REMARK   3    S TENSOR
REMARK   3      S11:   0.0028 S12:   0.7242 S13:  -0.8046
REMARK   3      S21:  -0.5582 S22:   0.0552 S23:   0.3943
REMARK   3      S31:   0.3038 S32:   0.2627 S33:   0.0000
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: (CHAIN C AND RESID 95:382 )
REMARK   3    ORIGIN FOR THE GROUP (A): -53.8688 -42.8962 -17.2502
REMARK   3    T TENSOR
REMARK   3      T11:   1.0307 T22:   0.4633
REMARK   3      T33:   0.6280 T12:  -0.0678
REMARK   3      T13:   0.1321 T23:  -0.4527
REMARK   3    L TENSOR
REMARK   3      L11:   2.0013 L22:   1.7918
REMARK   3      L33:   1.4326 L12:   0.7566
REMARK   3      L13:   0.2343 L23:   0.6131
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2476 S12:   0.4728 S13:  -0.6047
REMARK   3      S21:  -0.8435 S22:   0.3361 S23:  -0.2119
REMARK   3      S31:   0.4188 S32:   0.3829 S33:  -0.0002
REMARK   3   TLS GROUP : 11
REMARK   3    SELECTION: (CHAIN C AND RESID 383:511 )
REMARK   3    ORIGIN FOR THE GROUP (A): -30.6419 -22.1721 -12.3245
REMARK   3    T TENSOR
REMARK   3      T11:   0.5469 T22:   0.7260
REMARK   3      T33:   0.7405 T12:  -0.0793
REMARK   3      T13:   0.3311 T23:  -0.2753
REMARK   3    L TENSOR
REMARK   3      L11:   1.1657 L22:   0.5774
REMARK   3      L33:   0.8307 L12:   0.3993
REMARK   3      L13:   0.6253 L23:  -0.2553
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1069 S12:   0.5521 S13:  -0.1345
REMARK   3      S21:  -0.7801 S22:  -0.0340 S23:  -0.4764
REMARK   3      S31:  -0.0311 S32:   0.7722 S33:  -0.0072
REMARK   3   TLS GROUP : 12
REMARK   3    SELECTION: (CHAIN C AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -54.7301 -25.9359 -19.9032
REMARK   3    T TENSOR
REMARK   3      T11:   0.9136 T22:   0.8508
REMARK   3      T33:   0.5801 T12:  -0.1276
REMARK   3      T13:   0.4132 T23:  -0.2776
REMARK   3    L TENSOR
REMARK   3      L11:   0.0243 L22:   0.0198
REMARK   3      L33:   0.0457 L12:  -0.0200
REMARK   3      L13:  -0.0235 L23:   0.0117
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0163 S12:  -0.0524 S13:  -0.3579
REMARK   3      S21:  -0.0307 S22:   0.1903 S23:   0.7318
REMARK   3      S31:  -0.2708 S32:   0.1578 S33:  -0.0046
REMARK   3   TLS GROUP : 13
REMARK   3    SELECTION: (CHAIN D AND RESID 2:74 )
REMARK   3    ORIGIN FOR THE GROUP (A): -72.0015 -67.2413   0.9493
REMARK   3    T TENSOR
REMARK   3      T11:   1.1366 T22:   0.4000
REMARK   3      T33:   1.1842 T12:  -0.1626
REMARK   3      T13:  -0.0793 T23:  -0.2938
REMARK   3    L TENSOR
REMARK   3      L11:   0.5361 L22:   0.4511
REMARK   3      L33:   0.4244 L12:   0.0157
REMARK   3      L13:   0.4190 L23:  -0.0837
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2449 S12:  -0.1728 S13:  -0.5472
REMARK   3      S21:  -0.3601 S22:   0.3460 S23:   0.0439
REMARK   3      S31:   0.5628 S32:   0.2989 S33:  -0.0013
REMARK   3   TLS GROUP : 14
REMARK   3    SELECTION: (CHAIN D AND RESID 75:344 )
REMARK   3    ORIGIN FOR THE GROUP (A): -49.5236 -51.8184  12.7020
REMARK   3    T TENSOR
REMARK   3      T11:   0.5294 T22:   0.2376
REMARK   3      T33:   0.8337 T12:   0.1903
REMARK   3      T13:  -0.0000 T23:  -0.1435
REMARK   3    L TENSOR
REMARK   3      L11:   2.7791 L22:   2.0949
REMARK   3      L33:   1.0159 L12:   1.2000
REMARK   3      L13:   0.1544 L23:   0.1833
REMARK   3    S TENSOR
REMARK   3      S11:   0.0954 S12:  -0.1024 S13:  -1.0447
REMARK   3      S21:  -0.0678 S22:  -0.0578 S23:  -0.4544
REMARK   3      S31:   0.7910 S32:   0.2039 S33:   0.0050
REMARK   3   TLS GROUP : 15
REMARK   3    SELECTION: (CHAIN D AND RESID 345:459 )
REMARK   3    ORIGIN FOR THE GROUP (A): -28.6178 -30.4743  18.5542
REMARK   3    T TENSOR
REMARK   3      T11:   0.3233 T22:   0.5849
REMARK   3      T33:   0.9318 T12:   0.1370
REMARK   3      T13:  -0.0207 T23:  -0.0760
REMARK   3    L TENSOR
REMARK   3      L11:   0.4282 L22:   0.6272
REMARK   3      L33:   0.8382 L12:   0.3657
REMARK   3      L13:   0.3216 L23:   0.7250
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2022 S12:  -0.1760 S13:  -0.5156
REMARK   3      S21:   0.0519 S22:  -0.0467 S23:  -0.6467
REMARK   3      S31:   0.3922 S32:   0.3747 S33:  -0.0003
REMARK   3   TLS GROUP : 16
REMARK   3    SELECTION: (CHAIN D AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -40.5050 -41.8555   2.6496
REMARK   3    T TENSOR
REMARK   3      T11:   0.4497 T22:   0.4856
REMARK   3      T33:   1.1612 T12:   0.3039
REMARK   3      T13:  -0.0608 T23:  -0.1724
REMARK   3    L TENSOR
REMARK   3      L11:   0.3116 L22:   0.0540
REMARK   3      L33:   0.4703 L12:   0.1293
REMARK   3      L13:  -0.0080 L23:  -0.0008
REMARK   3    S TENSOR
REMARK   3      S11:   0.0296 S12:   0.3015 S13:   0.1090
REMARK   3      S21:  -0.0898 S22:   0.2472 S23:  -0.3669
REMARK   3      S31:  -0.3992 S32:   0.1264 S33:  -0.0016
REMARK   3   TLS GROUP : 17
REMARK   3    SELECTION: (CHAIN E AND RESID 2:74 )
REMARK   3    ORIGIN FOR THE GROUP (A):-103.2194 -44.1958  21.2552
REMARK   3    T TENSOR
REMARK   3      T11:   0.6037 T22:   0.4027
REMARK   3      T33:   1.4108 T12:  -0.3699
REMARK   3      T13:  -0.0682 T23:  -0.1439
REMARK   3    L TENSOR
REMARK   3      L11:   1.0787 L22:   0.9310
REMARK   3      L33:   0.6710 L12:  -0.6230
REMARK   3      L13:   0.2118 L23:  -0.4127
REMARK   3    S TENSOR
REMARK   3      S11:   0.1887 S12:  -0.5461 S13:   0.2010
REMARK   3      S21:   0.3174 S22:  -0.2324 S23:   1.1381
REMARK   3      S31:   0.2908 S32:  -0.4569 S33:   0.0133
REMARK   3   TLS GROUP : 18
REMARK   3    SELECTION: (CHAIN E AND RESID 75:344 )
REMARK   3    ORIGIN FOR THE GROUP (A): -94.2707 -16.4625  26.8278
REMARK   3    T TENSOR
REMARK   3      T11:   0.1167 T22:   0.4261
REMARK   3      T33:   1.3219 T12:  -0.2433
REMARK   3      T13:   0.1905 T23:  -0.3107
REMARK   3    L TENSOR
REMARK   3      L11:   2.0022 L22:   2.2978
REMARK   3      L33:   2.0784 L12:  -0.0559
REMARK   3      L13:  -0.6689 L23:   1.0644
REMARK   3    S TENSOR
REMARK   3      S11:   0.1946 S12:  -0.2817 S13:   0.2955
REMARK   3      S21:   0.3585 S22:  -0.1706 S23:   0.9106
REMARK   3      S31:   0.0404 S32:  -0.0707 S33:   0.0186
REMARK   3   TLS GROUP : 19
REMARK   3    SELECTION: (CHAIN E AND RESID 345:459 )
REMARK   3    ORIGIN FOR THE GROUP (A): -81.2089  10.7905  30.8105
REMARK   3    T TENSOR
REMARK   3      T11:   0.6384 T22:   0.6199
REMARK   3      T33:   1.6281 T12:  -0.3906
REMARK   3      T13:   0.4282 T23:  -0.4166
REMARK   3    L TENSOR
REMARK   3      L11:   0.7835 L22:   0.9044
REMARK   3      L33:   1.3090 L12:  -0.3635
REMARK   3      L13:   0.0589 L23:   0.2237
REMARK   3    S TENSOR
REMARK   3      S11:   0.2630 S12:  -0.2039 S13:   0.0895
REMARK   3      S21:  -0.3566 S22:   0.1466 S23:  -0.0886
REMARK   3      S31:  -0.6784 S32:   0.4436 S33:   0.0000
REMARK   3   TLS GROUP : 20
REMARK   3    SELECTION: (CHAIN F AND RESID 2:74 )
REMARK   3    ORIGIN FOR THE GROUP (A): -99.1143 -41.5466 -23.0536
REMARK   3    T TENSOR
REMARK   3      T11:   1.0900 T22:   0.7667
REMARK   3      T33:   1.2985 T12:  -0.4759
REMARK   3      T13:  -0.6096 T23:  -0.2327
REMARK   3    L TENSOR
REMARK   3      L11:   0.4088 L22:   0.4865
REMARK   3      L33:   0.4862 L12:   0.0368
REMARK   3      L13:  -0.3471 L23:  -0.3312
REMARK   3    S TENSOR
REMARK   3      S11:  -0.6406 S12:   0.9425 S13:   0.2132
REMARK   3      S21:  -1.1452 S22:   0.5826 S23:   0.6875
REMARK   3      S31:   0.2759 S32:  -0.0377 S33:  -0.0003
REMARK   3   TLS GROUP : 21
REMARK   3    SELECTION: (CHAIN F AND RESID 75:344 )
REMARK   3    ORIGIN FOR THE GROUP (A): -78.2229 -21.7228 -27.2999
REMARK   3    T TENSOR
REMARK   3      T11:   1.0607 T22:   0.4285
REMARK   3      T33:   0.6531 T12:  -0.3397
REMARK   3      T13:  -0.5845 T23:  -0.1376
REMARK   3    L TENSOR
REMARK   3      L11:   2.0505 L22:   1.5346
REMARK   3      L33:   0.8274 L12:   0.8666
REMARK   3      L13:  -0.2920 L23:   0.1360
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3125 S12:   0.8491 S13:   0.0487
REMARK   3      S21:  -1.3188 S22:   0.4031 S23:   0.5057
REMARK   3      S31:   0.1317 S32:  -0.1037 S33:   0.1033
REMARK   3   TLS GROUP : 22
REMARK   3    SELECTION: (CHAIN F AND RESID 345:459 )
REMARK   3    ORIGIN FOR THE GROUP (A): -57.7411  -1.1205 -17.7030
REMARK   3    T TENSOR
REMARK   3      T11:   0.7800 T22:   0.4752
REMARK   3      T33:   0.3939 T12:  -0.2551
REMARK   3      T13:  -0.0832 T23:  -0.2416
REMARK   3    L TENSOR
REMARK   3      L11:   1.0377 L22:   1.4037
REMARK   3      L33:   1.0961 L12:   0.2198
REMARK   3      L13:  -0.2215 L23:  -0.5469
REMARK   3    S TENSOR
REMARK   3      S11:   0.0052 S12:   0.3763 S13:   0.1032
REMARK   3      S21:  -1.0919 S22:   0.1862 S23:   0.2644
REMARK   3      S31:  -0.2317 S32:   0.1363 S33:   0.0057
REMARK   3   TLS GROUP : 23
REMARK   3    SELECTION: (CHAIN G AND (RESID 1:284 OR RESID 300:300 OR RESID
REMARK   3               287:296 ) )
REMARK   3    ORIGIN FOR THE GROUP (A): -40.1426  13.0232  10.3380
REMARK   3    T TENSOR
REMARK   3      T11:  -0.8589 T22:   0.2032
REMARK   3      T33:  -0.9813 T12:   0.0891
REMARK   3      T13:   0.9703 T23:  -0.4401
REMARK   3    L TENSOR
REMARK   3      L11:   2.2738 L22:   1.0701
REMARK   3      L33:   0.6786 L12:   0.7619
REMARK   3      L13:  -0.4932 L23:  -0.5474
REMARK   3    S TENSOR
REMARK   3      S11:   0.6687 S12:  -0.1765 S13:  -0.4968
REMARK   3      S21:   0.1028 S22:  -0.1266 S23:   0.2880
REMARK   3      S31:   0.0924 S32:  -0.0588 S33:   0.9982
REMARK   3   TLS GROUP : 24
REMARK   3    SELECTION: (CHAIN H AND (RESID 1:138 OR RESID 200:200 OR RESID
REMARK   3               139:142 ) )
REMARK   3    ORIGIN FOR THE GROUP (A): -27.0451  15.2656  23.8301
REMARK   3    T TENSOR
REMARK   3      T11:   0.1742 T22:   0.5824
REMARK   3      T33:   0.1783 T12:  -0.1781
REMARK   3      T13:   0.0685 T23:  -0.0729
REMARK   3    L TENSOR
REMARK   3      L11:   1.3760 L22:   1.7326
REMARK   3      L33:   0.9850 L12:   0.6324
REMARK   3      L13:  -0.4790 L23:  -0.3225
REMARK   3    S TENSOR
REMARK   3      S11:   0.1964 S12:  -0.2549 S13:  -0.1674
REMARK   3      S21:   0.2209 S22:  -0.2591 S23:  -0.1860
REMARK   3      S31:   0.0345 S32:   0.4636 S33:   0.0505
REMARK   3   TLS GROUP : 25
REMARK   3    SELECTION: (CHAIN I AND RESID 24:94 )
REMARK   3    ORIGIN FOR THE GROUP (A): -52.9151  98.6830 -68.3920
REMARK   3    T TENSOR
REMARK   3      T11:   1.0899 T22:   0.8571
REMARK   3      T33:   1.4713 T12:   0.4450
REMARK   3      T13:   0.4242 T23:   0.5103
REMARK   3    L TENSOR
REMARK   3      L11:   0.0165 L22:   0.3731
REMARK   3      L33:   0.3401 L12:   0.0829
REMARK   3      L13:   0.0766 L23:   0.3575
REMARK   3    S TENSOR
REMARK   3      S11:   0.2696 S12:   0.6717 S13:   0.7952
REMARK   3      S21:  -0.3242 S22:  -0.0799 S23:  -0.2190
REMARK   3      S31:  -0.5295 S32:  -0.3239 S33:  -0.0000
REMARK   3   TLS GROUP : 26
REMARK   3    SELECTION: (CHAIN I AND RESID 95:382 )
REMARK   3    ORIGIN FOR THE GROUP (A): -33.9232  75.9772 -71.9352
REMARK   3    T TENSOR
REMARK   3      T11:   0.9434 T22:   0.8651
REMARK   3      T33:   0.7329 T12:   0.3690
REMARK   3      T13:   0.3440 T23:   0.3465
REMARK   3    L TENSOR
REMARK   3      L11:   2.4267 L22:   2.9121
REMARK   3      L33:   1.3027 L12:   0.1031
REMARK   3      L13:  -0.0823 L23:   0.0154
REMARK   3    S TENSOR
REMARK   3      S11:   0.2141 S12:   0.5663 S13:   0.4749
REMARK   3      S21:  -0.7736 S22:  -0.2286 S23:  -0.1819
REMARK   3      S31:   0.0534 S32:   0.2953 S33:   0.0001
REMARK   3   TLS GROUP : 27
REMARK   3    SELECTION: (CHAIN I AND RESID 383:511 )
REMARK   3    ORIGIN FOR THE GROUP (A): -11.8561  54.3114 -70.1122
REMARK   3    T TENSOR
REMARK   3      T11:   1.1500 T22:   1.2143
REMARK   3      T33:   0.8327 T12:   0.4399
REMARK   3      T13:   0.4299 T23:   0.1503
REMARK   3    L TENSOR
REMARK   3      L11:   0.1255 L22:   0.7557
REMARK   3      L33:   0.9377 L12:  -0.0511
REMARK   3      L13:   0.2569 L23:   0.4391
REMARK   3    S TENSOR
REMARK   3      S11:   0.2002 S12:   0.0554 S13:   0.2341
REMARK   3      S21:  -0.2270 S22:  -0.1945 S23:  -0.6738
REMARK   3      S31:   0.1105 S32:   0.9375 S33:  -0.0001
REMARK   3   TLS GROUP : 28
REMARK   3    SELECTION: (CHAIN I AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -22.7029  73.8251 -58.8859
REMARK   3    T TENSOR
REMARK   3      T11:   1.2045 T22:   1.1292
REMARK   3      T33:   1.2670 T12:   0.2284
REMARK   3      T13:   0.1725 T23:  -0.1374
REMARK   3    L TENSOR
REMARK   3      L11:   0.3208 L22:   0.0561
REMARK   3      L33:   0.0094 L12:  -0.1194
REMARK   3      L13:  -0.0502 L23:   0.0221
REMARK   3    S TENSOR
REMARK   3      S11:   0.2824 S12:   0.0233 S13:  -0.1506
REMARK   3      S21:   0.2010 S22:   0.1623 S23:  -0.2393
REMARK   3      S31:   0.2752 S32:   0.1504 S33:   0.0040
REMARK   3   TLS GROUP : 29
REMARK   3    SELECTION: (CHAIN J AND RESID 26:94 )
REMARK   3    ORIGIN FOR THE GROUP (A): -87.5197  75.4226 -62.7560
REMARK   3    T TENSOR
REMARK   3      T11:   0.8085 T22:   0.9147
REMARK   3      T33:   0.7894 T12:   0.5714
REMARK   3      T13:  -0.1675 T23:   0.2901
REMARK   3    L TENSOR
REMARK   3      L11:   0.4925 L22:   0.4219
REMARK   3      L33:   0.3813 L12:   0.0397
REMARK   3      L13:  -0.1299 L23:   0.0817
REMARK   3    S TENSOR
REMARK   3      S11:   0.3944 S12:   0.5086 S13:   0.2973
REMARK   3      S21:  -0.4933 S22:  -0.0943 S23:   0.4703
REMARK   3      S31:  -0.1824 S32:  -0.2260 S33:  -0.0000
REMARK   3   TLS GROUP : 30
REMARK   3    SELECTION: (CHAIN J AND RESID 95:382 )
REMARK   3    ORIGIN FOR THE GROUP (A): -81.5734  48.6405 -51.8258
REMARK   3    T TENSOR
REMARK   3      T11:   0.2203 T22:   0.5700
REMARK   3      T33:   0.5231 T12:   0.3410
REMARK   3      T13:  -0.3247 T23:  -0.1543
REMARK   3    L TENSOR
REMARK   3      L11:   2.6868 L22:   2.7997
REMARK   3      L33:   2.3511 L12:  -0.1732
REMARK   3      L13:  -0.0366 L23:  -0.4432
REMARK   3    S TENSOR
REMARK   3      S11:   0.3262 S12:   0.4801 S13:  -0.3580
REMARK   3      S21:  -0.5122 S22:  -0.2552 S23:   0.7452
REMARK   3      S31:   0.1967 S32:  -0.4360 S33:  -0.0665
REMARK   3   TLS GROUP : 31
REMARK   3    SELECTION: (CHAIN J AND RESID 383:511 )
REMARK   3    ORIGIN FOR THE GROUP (A): -72.7438  19.9585 -43.9981
REMARK   3    T TENSOR
REMARK   3      T11:   0.9607 T22:   0.8325
REMARK   3      T33:   1.4557 T12:   0.2016
REMARK   3      T13:   0.0022 T23:  -0.0916
REMARK   3    L TENSOR
REMARK   3      L11:   0.5098 L22:   0.8158
REMARK   3      L33:   1.2091 L12:   0.0573
REMARK   3      L13:  -0.5410 L23:  -0.1541
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3937 S12:  -0.3137 S13:  -1.0728
REMARK   3      S21:   0.6623 S22:   0.0489 S23:  -0.1220
REMARK   3      S31:   0.9438 S32:   0.4785 S33:  -0.0001
REMARK   3   TLS GROUP : 32
REMARK   3    SELECTION: (CHAIN J AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -68.7620  39.7633 -59.5515
REMARK   3    T TENSOR
REMARK   3      T11:   1.2782 T22:   1.0210
REMARK   3      T33:   0.9250 T12:   0.3253
REMARK   3      T13:  -0.0452 T23:  -0.1734
REMARK   3    L TENSOR
REMARK   3      L11:   0.0192 L22:   0.0036
REMARK   3      L33:   0.0117 L12:  -0.0023
REMARK   3      L13:   0.0113 L23:   0.0027
REMARK   3    S TENSOR
REMARK   3      S11:   0.3066 S12:   0.0006 S13:  -0.1405
REMARK   3      S21:  -0.1615 S22:   0.1524 S23:  -0.0253
REMARK   3      S31:   0.1312 S32:  -0.0498 S33:   0.0011
REMARK   3   TLS GROUP : 33
REMARK   3    SELECTION: (CHAIN K AND RESID 25:94 )
REMARK   3    ORIGIN FOR THE GROUP (A): -72.3254  97.4218 -30.2573
REMARK   3    T TENSOR
REMARK   3      T11:   0.7865 T22:   0.5359
REMARK   3      T33:   1.4332 T12:   0.4077
REMARK   3      T13:   0.1573 T23:  -0.1421
REMARK   3    L TENSOR
REMARK   3      L11:   0.5274 L22:   0.3016
REMARK   3      L33:   0.1839 L12:   0.1505
REMARK   3      L13:  -0.0354 L23:   0.1458
REMARK   3    S TENSOR
REMARK   3      S11:   0.2525 S12:  -0.0557 S13:   1.2235
REMARK   3      S21:   0.0753 S22:   0.0442 S23:   0.2156
REMARK   3      S31:  -0.6673 S32:  -0.1307 S33:   0.0001
REMARK   3   TLS GROUP : 34
REMARK   3    SELECTION: (CHAIN K AND RESID 95:382 )
REMARK   3    ORIGIN FOR THE GROUP (A): -50.3398  81.1511 -18.0512
REMARK   3    T TENSOR
REMARK   3      T11:   0.4842 T22:   0.3479
REMARK   3      T33:   0.7587 T12:   0.1273
REMARK   3      T13:   0.0286 T23:  -0.4211
REMARK   3    L TENSOR
REMARK   3      L11:   2.9087 L22:   2.0030
REMARK   3      L33:   1.8128 L12:  -1.3399
REMARK   3      L13:   0.5619 L23:  -0.2423
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0735 S12:  -0.4948 S13:   0.9660
REMARK   3      S21:   0.4389 S22:   0.2420 S23:   0.0253
REMARK   3      S31:  -0.5605 S32:   0.1247 S33:  -0.0141
REMARK   3   TLS GROUP : 35
REMARK   3    SELECTION: (CHAIN K AND RESID 383:511 )
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2807  59.7045  -8.5748
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0509 T22:   0.3720
REMARK   3      T33:  -0.0908 T12:   0.1760
REMARK   3      T13:  -0.3046 T23:  -0.4765
REMARK   3    L TENSOR
REMARK   3      L11:   2.0528 L22:   1.7484
REMARK   3      L33:   0.8595 L12:   0.0911
REMARK   3      L13:  -0.6954 L23:   0.0263
REMARK   3    S TENSOR
REMARK   3      S11:   0.0939 S12:  -0.9614 S13:   0.2456
REMARK   3      S21:   0.8015 S22:  -0.0547 S23:  -0.4309
REMARK   3      S31:   0.0307 S32:   0.5241 S33:  -0.0550
REMARK   3   TLS GROUP : 36
REMARK   3    SELECTION: (CHAIN K AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -53.1286  64.2817 -16.4054
REMARK   3    T TENSOR
REMARK   3      T11:   0.5201 T22:   0.4589
REMARK   3      T33:   0.3803 T12:   0.0808
REMARK   3      T13:  -0.2138 T23:  -0.4782
REMARK   3    L TENSOR
REMARK   3      L11:   0.0735 L22:   0.0132
REMARK   3      L33:   0.1699 L12:  -0.0043
REMARK   3      L13:  -0.0397 L23:  -0.0141
REMARK   3    S TENSOR
REMARK   3      S11:  -0.4872 S12:   0.4599 S13:   0.1744
REMARK   3      S21:  -0.3090 S22:   0.1280 S23:   0.5095
REMARK   3      S31:   0.2423 S32:  -0.0695 S33:  -0.0080
REMARK   3   TLS GROUP : 37
REMARK   3    SELECTION: (CHAIN L AND RESID 2:74 )
REMARK   3    ORIGIN FOR THE GROUP (A): -53.8709 105.6067 -43.4690
REMARK   3    T TENSOR
REMARK   3      T11:   1.1025 T22:   0.5873
REMARK   3      T33:   1.6252 T12:   0.2339
REMARK   3      T13:   0.2459 T23:   0.0792
REMARK   3    L TENSOR
REMARK   3      L11:   0.4980 L22:   0.2768
REMARK   3      L33:   0.0429 L12:   0.2567
REMARK   3      L13:  -0.0712 L23:  -0.0976
REMARK   3    S TENSOR
REMARK   3      S11:   0.1651 S12:   0.2173 S13:   1.0721
REMARK   3      S21:  -0.1178 S22:  -0.0155 S23:  -0.1776
REMARK   3      S31:  -0.9625 S32:   0.0059 S33:   0.0001
REMARK   3   TLS GROUP : 38
REMARK   3    SELECTION: (CHAIN L AND RESID 75:344 )
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2670  89.3484 -40.0576
REMARK   3    T TENSOR
REMARK   3      T11:   0.7241 T22:   0.4456
REMARK   3      T33:   1.3841 T12:  -0.0261
REMARK   3      T13:   0.2285 T23:  -0.0986
REMARK   3    L TENSOR
REMARK   3      L11:   1.8208 L22:   1.8551
REMARK   3      L33:   1.6634 L12:  -0.8474
REMARK   3      L13:   0.8326 L23:  -0.1250
REMARK   3    S TENSOR
REMARK   3      S11:   0.2197 S12:   0.1869 S13:   1.2739
REMARK   3      S21:  -0.0036 S22:  -0.0680 S23:  -0.5200
REMARK   3      S31:  -0.6731 S32:   0.4046 S33:  -0.0000
REMARK   3   TLS GROUP : 39
REMARK   3    SELECTION: (CHAIN L AND RESID 345:459 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.5452  67.3635 -32.6774
REMARK   3    T TENSOR
REMARK   3      T11:   0.4692 T22:   0.7577
REMARK   3      T33:   1.2134 T12:  -0.0571
REMARK   3      T13:   0.0463 T23:  -0.1960
REMARK   3    L TENSOR
REMARK   3      L11:   0.8229 L22:   0.8475
REMARK   3      L33:   0.7655 L12:  -0.6122
REMARK   3      L13:  -0.5340 L23:   0.0917
REMARK   3    S TENSOR
REMARK   3      S11:   0.1281 S12:  -0.0465 S13:   0.8624
REMARK   3      S21:   0.1743 S22:  -0.1378 S23:  -0.8381
REMARK   3      S31:  -0.5577 S32:   0.6804 S33:  -0.0093
REMARK   3   TLS GROUP : 40
REMARK   3    SELECTION: (CHAIN L AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -28.0046  79.3431 -26.5940
REMARK   3    T TENSOR
REMARK   3      T11:   0.5407 T22:   0.8232
REMARK   3      T33:   1.3264 T12:  -0.1361
REMARK   3      T13:  -0.0806 T23:  -0.4081
REMARK   3    L TENSOR
REMARK   3      L11:   0.0071 L22:   0.0169
REMARK   3      L33:   0.0548 L12:  -0.0099
REMARK   3      L13:   0.0176 L23:  -0.0217
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1330 S12:  -0.3397 S13:  -0.1953
REMARK   3      S21:   0.2670 S22:  -0.1948 S23:  -0.1610
REMARK   3      S31:   0.0574 S32:   0.1808 S33:  -0.0032
REMARK   3   TLS GROUP : 41
REMARK   3    SELECTION: (CHAIN M AND RESID 2:74 )
REMARK   3    ORIGIN FOR THE GROUP (A): -68.4584  83.1445 -78.1077
REMARK   3    T TENSOR
REMARK   3      T11:   1.2818 T22:   1.1416
REMARK   3      T33:   0.9654 T12:   0.7300
REMARK   3      T13:   0.1393 T23:   0.5478
REMARK   3    L TENSOR
REMARK   3      L11:   0.2978 L22:   0.4165
REMARK   3      L33:   0.3180 L12:   0.1579
REMARK   3      L13:   0.3081 L23:   0.1274
REMARK   3    S TENSOR
REMARK   3      S11:   0.5199 S12:   1.0018 S13:   0.3025
REMARK   3      S21:  -1.1594 S22:  -0.3188 S23:   0.4388
REMARK   3      S31:   0.1020 S32:   0.0897 S33:   0.0008
REMARK   3   TLS GROUP : 42
REMARK   3    SELECTION: (CHAIN M AND RESID 75:344 )
REMARK   3    ORIGIN FOR THE GROUP (A): -58.8583  55.0731 -77.6622
REMARK   3    T TENSOR
REMARK   3      T11:   0.9137 T22:   1.1551
REMARK   3      T33:   0.2216 T12:   0.5101
REMARK   3      T13:  -0.1717 T23:   0.0175
REMARK   3    L TENSOR
REMARK   3      L11:   1.4746 L22:   2.7492
REMARK   3      L33:   1.6457 L12:  -1.1395
REMARK   3      L13:   0.2626 L23:   1.0190
REMARK   3    S TENSOR
REMARK   3      S11:   0.3668 S12:   1.0377 S13:   0.2113
REMARK   3      S21:  -0.8192 S22:  -0.1760 S23:   0.2691
REMARK   3      S31:   0.0672 S32:  -0.0911 S33:   0.0004
REMARK   3   TLS GROUP : 43
REMARK   3    SELECTION: (CHAIN M AND RESID 345:459 )
REMARK   3    ORIGIN FOR THE GROUP (A): -46.7805  27.3975 -73.5229
REMARK   3    T TENSOR
REMARK   3      T11:   1.1919 T22:   1.0187
REMARK   3      T33:   0.4851 T12:   0.4419
REMARK   3      T13:  -0.2981 T23:  -0.3363
REMARK   3    L TENSOR
REMARK   3      L11:   0.8919 L22:   1.0909
REMARK   3      L33:   0.7413 L12:   0.0719
REMARK   3      L13:  -0.4810 L23:   0.2608
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0763 S12:   0.4124 S13:  -0.5439
REMARK   3      S21:  -0.0203 S22:   0.2914 S23:   0.0162
REMARK   3      S31:   0.3630 S32:  -0.0610 S33:  -0.0002
REMARK   3   TLS GROUP : 44
REMARK   3    SELECTION: (CHAIN N AND RESID 2:74 )
REMARK   3    ORIGIN FOR THE GROUP (A): -90.5568  81.1504 -39.5157
REMARK   3    T TENSOR
REMARK   3      T11:   0.5772 T22:   0.6843
REMARK   3      T33:   0.8754 T12:   0.4940
REMARK   3      T13:   0.0212 T23:   0.1941
REMARK   3    L TENSOR
REMARK   3      L11:   0.7885 L22:   1.6940
REMARK   3      L33:   0.6290 L12:   0.4031
REMARK   3      L13:   0.2871 L23:  -0.0107
REMARK   3    S TENSOR
REMARK   3      S11:   0.0228 S12:  -0.0098 S13:   0.1314
REMARK   3      S21:   0.2736 S22:   0.3312 S23:   1.2292
REMARK   3      S31:  -0.0959 S32:  -0.3861 S33:  -0.0324
REMARK   3   TLS GROUP : 45
REMARK   3    SELECTION: (CHAIN N AND RESID 75:344 )
REMARK   3    ORIGIN FOR THE GROUP (A): -76.6449  60.8505 -23.9784
REMARK   3    T TENSOR
REMARK   3      T11:   0.2202 T22:   0.3848
REMARK   3      T33:   0.4925 T12:   0.2384
REMARK   3      T13:  -0.0017 T23:  -0.0724
REMARK   3    L TENSOR
REMARK   3      L11:   2.4355 L22:   2.6109
REMARK   3      L33:   0.9213 L12:  -1.4838
REMARK   3      L13:   0.3463 L23:  -0.5723
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0453 S12:  -0.3257 S13:   0.1033
REMARK   3      S21:   0.2031 S22:   0.2515 S23:   0.4297
REMARK   3      S31:  -0.1786 S32:  -0.3190 S33:   0.1133
REMARK   3   TLS GROUP : 46
REMARK   3    SELECTION: (CHAIN N AND RESID 345:459 )
REMARK   3    ORIGIN FOR THE GROUP (A): -55.1080  39.5558 -19.9803
REMARK   3    T TENSOR
REMARK   3      T11:   0.1852 T22:   0.4535
REMARK   3      T33:   0.3259 T12:   0.2670
REMARK   3      T13:   0.0283 T23:  -0.1324
REMARK   3    L TENSOR
REMARK   3      L11:   1.7170 L22:   2.3711
REMARK   3      L33:   1.3841 L12:  -0.6113
REMARK   3      L13:  -0.2428 L23:  -0.7254
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1287 S12:  -0.5474 S13:  -0.3804
REMARK   3      S21:   0.1440 S22:   0.0850 S23:   0.3167
REMARK   3      S31:   0.2446 S32:  -0.0592 S33:   0.0304
REMARK   3   TLS GROUP : 47
REMARK   3    SELECTION: (CHAIN O AND (RESID 1:284 OR RESID 300:300 OR RESID
REMARK   3               287:291 ) )
REMARK   3    ORIGIN FOR THE GROUP (A): -25.3424  24.4145 -32.6433
REMARK   3    T TENSOR
REMARK   3      T11:   0.1629 T22:   0.4488
REMARK   3      T33:   0.0731 T12:   0.1300
REMARK   3      T13:  -0.0059 T23:  -0.1379
REMARK   3    L TENSOR
REMARK   3      L11:   1.0086 L22:   1.4322
REMARK   3      L33:   1.7355 L12:  -0.5364
REMARK   3      L13:   0.3628 L23:  -0.9077
REMARK   3    S TENSOR
REMARK   3      S11:   0.1378 S12:   0.1691 S13:   0.0215
REMARK   3      S21:  -0.3495 S22:  -0.2594 S23:  -0.1787
REMARK   3      S31:   0.2858 S32:   0.1404 S33:  -0.1618
REMARK   3   TLS GROUP : 48
REMARK   3    SELECTION: (CHAIN P AND (RESID 1:138 OR RESID 200:200 OR RESID
REMARK   3               139:140 ) )
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.8116  21.7490 -35.3912
REMARK   3    T TENSOR
REMARK   3      T11:   0.1683 T22:   0.5956
REMARK   3      T33:   0.2752 T12:   0.1746
REMARK   3      T13:   0.1026 T23:  -0.0384
REMARK   3    L TENSOR
REMARK   3      L11:   0.5496 L22:   2.0799
REMARK   3      L33:   1.3098 L12:  -0.0526
REMARK   3      L13:   0.3137 L23:  -0.6300
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0328 S12:  -0.1321 S13:   0.0220
REMARK   3      S21:  -0.2443 S22:  -0.0859 S23:  -0.3373
REMARK   3      S31:   0.1350 S32:   0.4275 S33:  -0.0007
REMARK   3   TLS GROUP : 49
REMARK   3    SELECTION: (CHAIN Q AND RESID 24:94 )
REMARK   3    ORIGIN FOR THE GROUP (A): -29.5786  79.1293  83.7740
REMARK   3    T TENSOR
REMARK   3      T11:   1.3519 T22:   0.7655
REMARK   3      T33:   0.5939 T12:  -0.1925
REMARK   3      T13:  -0.4939 T23:  -0.4140
REMARK   3    L TENSOR
REMARK   3      L11:   0.6831 L22:   0.6851
REMARK   3      L33:   0.3431 L12:  -0.5298
REMARK   3      L13:  -0.1260 L23:   0.1268
REMARK   3    S TENSOR
REMARK   3      S11:   0.0932 S12:  -0.5780 S13:   0.6625
REMARK   3      S21:   0.0952 S22:   0.2274 S23:  -0.3951
REMARK   3      S31:  -0.6587 S32:   0.7845 S33:   0.0054
REMARK   3   TLS GROUP : 50
REMARK   3    SELECTION: (CHAIN Q AND RESID 95:382 )
REMARK   3    ORIGIN FOR THE GROUP (A): -38.8926  51.4412  77.8225
REMARK   3    T TENSOR
REMARK   3      T11:   0.7086 T22:   0.4572
REMARK   3      T33:   0.0625 T12:   0.0786
REMARK   3      T13:  -0.2318 T23:  -0.0915
REMARK   3    L TENSOR
REMARK   3      L11:   2.3239 L22:   2.5270
REMARK   3      L33:   3.2400 L12:   0.8550
REMARK   3      L13:   0.5578 L23:   0.7009
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0748 S12:  -0.1976 S13:  -0.2871
REMARK   3      S21:   0.4408 S22:   0.1333 S23:  -0.3152
REMARK   3      S31:  -0.1091 S32:   0.3865 S33:  -0.1147
REMARK   3   TLS GROUP : 51
REMARK   3    SELECTION: (CHAIN Q AND RESID 383:511 )
REMARK   3    ORIGIN FOR THE GROUP (A): -53.1437  24.0147  75.7299
REMARK   3    T TENSOR
REMARK   3      T11:   0.9976 T22:   0.5982
REMARK   3      T33:   0.9920 T12:   0.1208
REMARK   3      T13:  -0.1605 T23:   0.0445
REMARK   3    L TENSOR
REMARK   3      L11:   0.7617 L22:   1.2978
REMARK   3      L33:   0.7323 L12:   0.2499
REMARK   3      L13:  -0.1764 L23:   0.6254
REMARK   3    S TENSOR
REMARK   3      S11:   0.1910 S12:  -0.3328 S13:  -1.1458
REMARK   3      S21:   1.0655 S22:  -0.2158 S23:   0.4063
REMARK   3      S31:   0.7238 S32:  -0.1744 S33:   0.0001
REMARK   3   TLS GROUP : 52
REMARK   3    SELECTION: (CHAIN Q AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -53.4722  46.8333  86.0719
REMARK   3    T TENSOR
REMARK   3      T11:   1.4058 T22:   0.6943
REMARK   3      T33:   0.8749 T12:  -0.0052
REMARK   3      T13:  -0.1406 T23:   0.0575
REMARK   3    L TENSOR
REMARK   3      L11:   0.0333 L22:   0.2703
REMARK   3      L33:   0.0187 L12:   0.0364
REMARK   3      L13:   0.0065 L23:  -0.0526
REMARK   3    S TENSOR
REMARK   3      S11:   0.1048 S12:  -0.1187 S13:  -0.3189
REMARK   3      S21:   0.2141 S22:   0.0332 S23:   0.1751
REMARK   3      S31:   0.5149 S32:  -0.3262 S33:  -0.0011
REMARK   3   TLS GROUP : 53
REMARK   3    SELECTION: (CHAIN R AND RESID 26:94 )
REMARK   3    ORIGIN FOR THE GROUP (A): -38.8824  95.3218  45.7890
REMARK   3    T TENSOR
REMARK   3      T11:   1.2707 T22:   0.5537
REMARK   3      T33:   0.6634 T12:  -0.5003
REMARK   3      T13:  -0.2864 T23:  -0.0053
REMARK   3    L TENSOR
REMARK   3      L11:   0.7322 L22:   0.1853
REMARK   3      L33:   0.1228 L12:  -0.1877
REMARK   3      L13:  -0.1654 L23:  -0.0439
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0620 S12:   0.1925 S13:   0.9533
REMARK   3      S21:  -0.3588 S22:   0.3232 S23:   0.0011
REMARK   3      S31:  -0.6093 S32:   0.6388 S33:   0.0148
REMARK   3   TLS GROUP : 54
REMARK   3    SELECTION: (CHAIN R AND RESID 95:382 )
REMARK   3    ORIGIN FOR THE GROUP (A): -60.6811  80.6932  32.2639
REMARK   3    T TENSOR
REMARK   3      T11:   1.3171 T22:   0.2603
REMARK   3      T33:   0.0785 T12:  -0.1072
REMARK   3      T13:  -0.3120 T23:  -0.0180
REMARK   3    L TENSOR
REMARK   3      L11:   2.9411 L22:   1.3458
REMARK   3      L33:   1.6914 L12:  -0.0002
REMARK   3      L13:  -0.1174 L23:  -0.1992
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2090 S12:   0.8023 S13:   0.3439
REMARK   3      S21:  -0.3397 S22:   0.0168 S23:  -0.1082
REMARK   3      S31:  -0.7999 S32:  -0.0589 S33:   0.0043
REMARK   3   TLS GROUP : 55
REMARK   3    SELECTION: (CHAIN R AND RESID 383:511 )
REMARK   3    ORIGIN FOR THE GROUP (A): -80.9311  61.6987  18.4420
REMARK   3    T TENSOR
REMARK   3      T11:   1.2714 T22:   1.0845
REMARK   3      T33:   0.8466 T12:   0.1585
REMARK   3      T13:  -0.5478 T23:  -0.1659
REMARK   3    L TENSOR
REMARK   3      L11:   1.0679 L22:   1.1615
REMARK   3      L33:   0.5757 L12:  -0.4228
REMARK   3      L13:   0.2505 L23:   0.1564
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0057 S12:  -0.0583 S13:  -0.3759
REMARK   3      S21:  -0.0215 S22:  -0.1322 S23:   1.2969
REMARK   3      S31:  -0.1807 S32:  -0.7455 S33:   0.0028
REMARK   3   TLS GROUP : 56
REMARK   3    SELECTION: (CHAIN R AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -59.3769  63.3702  31.9728
REMARK   3    T TENSOR
REMARK   3      T11:   1.7518 T22:   1.1704
REMARK   3      T33:   0.5937 T12:   0.0684
REMARK   3      T13:  -0.4729 T23:  -0.0896
REMARK   3    L TENSOR
REMARK   3      L11:   0.0120 L22:   0.0050
REMARK   3      L33:   0.0139 L12:   0.0061
REMARK   3      L13:  -0.0127 L23:  -0.0063
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0460 S12:   0.0938 S13:  -0.0979
REMARK   3      S21:  -0.1967 S22:   0.1127 S23:  -0.2627
REMARK   3      S31:   0.1022 S32:  -0.2228 S33:  -0.0015
REMARK   3   TLS GROUP : 57
REMARK   3    SELECTION: (CHAIN S AND RESID 25:94 )
REMARK   3    ORIGIN FOR THE GROUP (A): -61.3245 107.7731  79.1529
REMARK   3    T TENSOR
REMARK   3      T11:   1.8146 T22:   0.3918
REMARK   3      T33:   0.9965 T12:   0.1885
REMARK   3      T13:  -0.4788 T23:  -0.4061
REMARK   3    L TENSOR
REMARK   3      L11:   0.2136 L22:   0.2908
REMARK   3      L33:   0.3907 L12:  -0.0855
REMARK   3      L13:  -0.1559 L23:  -0.2092
REMARK   3    S TENSOR
REMARK   3      S11:   0.0492 S12:  -0.4101 S13:   0.7118
REMARK   3      S21:   0.4201 S22:   0.1348 S23:  -0.0823
REMARK   3      S31:  -0.3532 S32:   0.3881 S33:   0.0001
REMARK   3   TLS GROUP : 58
REMARK   3    SELECTION: (CHAIN S AND RESID 95:382 )
REMARK   3    ORIGIN FOR THE GROUP (A): -82.4852  87.0570  83.6427
REMARK   3    T TENSOR
REMARK   3      T11:   1.3634 T22:   0.8277
REMARK   3      T33:   0.7758 T12:   0.3837
REMARK   3      T13:  -0.2563 T23:  -0.7653
REMARK   3    L TENSOR
REMARK   3      L11:   1.1915 L22:   1.1636
REMARK   3      L33:   0.6743 L12:   0.1834
REMARK   3      L13:  -0.3498 L23:  -0.6332
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2299 S12:  -0.4532 S13:   0.2997
REMARK   3      S21:   0.4150 S22:  -0.3277 S23:   0.6951
REMARK   3      S31:  -0.4712 S32:  -0.5018 S33:   0.0250
REMARK   3   TLS GROUP : 59
REMARK   3    SELECTION: (CHAIN S AND RESID 383:511 )
REMARK   3    ORIGIN FOR THE GROUP (A):-103.1702  63.2862  83.0787
REMARK   3    T TENSOR
REMARK   3      T11:   0.9293 T22:   1.1646
REMARK   3      T33:   1.0144 T12:   0.1681
REMARK   3      T13:   0.3692 T23:  -0.6280
REMARK   3    L TENSOR
REMARK   3      L11:   0.4410 L22:   0.4780
REMARK   3      L33:   0.0928 L12:   0.2923
REMARK   3      L13:  -0.2049 L23:  -0.1687
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2191 S12:  -0.1664 S13:  -0.0561
REMARK   3      S21:   0.3140 S22:  -0.2167 S23:   0.5350
REMARK   3      S31:  -0.1985 S32:  -0.9208 S33:  -0.0005
REMARK   3   TLS GROUP : 60
REMARK   3    SELECTION: (CHAIN S AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -90.4558  80.9320  69.7038
REMARK   3    T TENSOR
REMARK   3      T11:   0.5624 T22:   1.1936
REMARK   3      T33:   0.5736 T12:   0.2110
REMARK   3      T13:   0.0103 T23:  -0.4442
REMARK   3    L TENSOR
REMARK   3      L11:   0.0552 L22:   0.0253
REMARK   3      L33:   0.0501 L12:  -0.0373
REMARK   3      L13:  -0.0206 L23:   0.0117
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0856 S12:   0.0166 S13:  -0.2009
REMARK   3      S21:  -0.0653 S22:  -0.0940 S23:   0.2021
REMARK   3      S31:  -0.0729 S32:   0.2542 S33:  -0.0020
REMARK   3   TLS GROUP : 61
REMARK   3    SELECTION: (CHAIN T AND RESID 2:74 )
REMARK   3    ORIGIN FOR THE GROUP (A): -49.0454  93.2117  93.7752
REMARK   3    T TENSOR
REMARK   3      T11:   1.6531 T22:   0.8142
REMARK   3      T33:   0.6058 T12:  -0.0034
REMARK   3      T13:  -0.4754 T23:  -0.4679
REMARK   3    L TENSOR
REMARK   3      L11:   0.8669 L22:   0.8614
REMARK   3      L33:   0.3133 L12:  -0.2948
REMARK   3      L13:   0.0444 L23:  -0.3359
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0763 S12:  -1.3046 S13:   0.5302
REMARK   3      S21:  -0.1219 S22:   0.2598 S23:   0.3177
REMARK   3      S31:  -0.8904 S32:   0.6439 S33:   0.0086
REMARK   3   TLS GROUP : 62
REMARK   3    SELECTION: (CHAIN T AND RESID 75:344 )
REMARK   3    ORIGIN FOR THE GROUP (A): -62.7367  67.2036  97.9302
REMARK   3    T TENSOR
REMARK   3      T11:   1.5458 T22:   0.8961
REMARK   3      T33:   0.1935 T12:   0.1780
REMARK   3      T13:  -0.0242 T23:  -0.3744
REMARK   3    L TENSOR
REMARK   3      L11:   1.2547 L22:   1.4025
REMARK   3      L33:   1.8523 L12:   0.5020
REMARK   3      L13:  -0.1637 L23:   0.0668
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2190 S12:  -0.6845 S13:   0.2651
REMARK   3      S21:   0.6975 S22:  -0.3048 S23:   0.2760
REMARK   3      S31:  -0.0676 S32:  -0.1709 S33:  -0.2185
REMARK   3   TLS GROUP : 63
REMARK   3    SELECTION: (CHAIN T AND RESID 345:459 )
REMARK   3    ORIGIN FOR THE GROUP (A): -81.4803  43.3402  95.6138
REMARK   3    T TENSOR
REMARK   3      T11:   1.5512 T22:   1.3841
REMARK   3      T33:   0.6990 T12:  -0.0831
REMARK   3      T13:   0.5025 T23:  -0.2946
REMARK   3    L TENSOR
REMARK   3      L11:   0.1441 L22:   0.5605
REMARK   3      L33:   0.1937 L12:  -0.0486
REMARK   3      L13:  -0.0883 L23:  -0.2177
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3040 S12:  -0.5994 S13:   0.0531
REMARK   3      S21:   0.6045 S22:   0.0217 S23:   0.4125
REMARK   3      S31:   0.2669 S32:  -0.4982 S33:   0.0000
REMARK   3   TLS GROUP : 64
REMARK   3    SELECTION: (CHAIN T AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -79.0760  66.0424  94.2986
REMARK   3    T TENSOR
REMARK   3      T11:   1.7962 T22:   0.8810
REMARK   3      T33:   0.5057 T12:   0.0574
REMARK   3      T13:   0.0348 T23:  -0.2230
REMARK   3    L TENSOR
REMARK   3      L11:   0.0096 L22:   0.0015
REMARK   3      L33:   0.0009 L12:  -0.0019
REMARK   3      L13:   0.0015 L23:  -0.0014
REMARK   3    S TENSOR
REMARK   3      S11:   0.2357 S12:  -0.0015 S13:  -0.0027
REMARK   3      S21:  -0.0154 S22:   0.1346 S23:   0.3077
REMARK   3      S31:   0.0992 S32:  -0.2436 S33:   0.0016
REMARK   3   TLS GROUP : 65
REMARK   3    SELECTION: (CHAIN U AND RESID 2:74 )
REMARK   3    ORIGIN FOR THE GROUP (A): -24.7428  78.8834  60.0985
REMARK   3    T TENSOR
REMARK   3      T11:   1.3672 T22:   0.7658
REMARK   3      T33:   0.8387 T12:  -0.4647
REMARK   3      T13:  -0.2640 T23:  -0.3328
REMARK   3    L TENSOR
REMARK   3      L11:   0.4301 L22:   0.9502
REMARK   3      L33:   1.0984 L12:   0.0848
REMARK   3      L13:  -0.1259 L23:  -0.6891
REMARK   3    S TENSOR
REMARK   3      S11:  -0.6608 S12:  -0.1799 S13:   0.4925
REMARK   3      S21:  -0.7187 S22:   0.4319 S23:  -1.2002
REMARK   3      S31:  -0.3308 S32:   0.6298 S33:  -0.0859
REMARK   3   TLS GROUP : 66
REMARK   3    SELECTION: (CHAIN U AND RESID 75:344 )
REMARK   3    ORIGIN FOR THE GROUP (A): -38.2837  56.8943  45.5049
REMARK   3    T TENSOR
REMARK   3      T11:   0.7241 T22:   0.4492
REMARK   3      T33:   0.1718 T12:  -0.3990
REMARK   3      T13:  -0.0184 T23:  -0.1527
REMARK   3    L TENSOR
REMARK   3      L11:   1.8508 L22:   2.8230
REMARK   3      L33:   2.3228 L12:  -1.4956
REMARK   3      L13:  -1.0723 L23:   1.0089
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2758 S12:   0.2784 S13:   0.0406
REMARK   3      S21:  -0.2534 S22:   0.2761 S23:  -0.3351
REMARK   3      S31:  -0.6644 S32:   0.4838 S33:  -0.0009
REMARK   3   TLS GROUP : 67
REMARK   3    SELECTION: (CHAIN U AND RESID 345:459 )
REMARK   3    ORIGIN FOR THE GROUP (A): -55.3644  34.6288  33.6093
REMARK   3    T TENSOR
REMARK   3      T11:   0.8337 T22:   0.8709
REMARK   3      T33:   1.1593 T12:  -0.3490
REMARK   3      T13:  -0.0582 T23:  -0.3973
REMARK   3    L TENSOR
REMARK   3      L11:   0.8544 L22:   1.4266
REMARK   3      L33:   1.0618 L12:  -0.6592
REMARK   3      L13:   0.5407 L23:   0.3564
REMARK   3    S TENSOR
REMARK   3      S11:   0.0721 S12:  -0.0627 S13:  -0.7667
REMARK   3      S21:  -0.5405 S22:  -0.3143 S23:   1.5603
REMARK   3      S31:  -0.1024 S32:  -0.3793 S33:  -0.0001
REMARK   3   TLS GROUP : 68
REMARK   3    SELECTION: (CHAIN V AND RESID 2:74 )
REMARK   3    ORIGIN FOR THE GROUP (A): -56.8461 109.4790  53.5354
REMARK   3    T TENSOR
REMARK   3      T11:   2.0338 T22:   0.3891
REMARK   3      T33:   0.9972 T12:   0.0184
REMARK   3      T13:  -0.3918 T23:  -0.1191
REMARK   3    L TENSOR
REMARK   3      L11:   0.5251 L22:   0.2673
REMARK   3      L33:   0.0383 L12:  -0.0409
REMARK   3      L13:   0.0929 L23:   0.0297
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2317 S12:   0.3330 S13:   1.3698
REMARK   3      S21:  -0.5090 S22:   0.0804 S23:   0.3847
REMARK   3      S31:  -1.4146 S32:   0.2987 S33:  -0.0003
REMARK   3   TLS GROUP : 69
REMARK   3    SELECTION: (CHAIN V AND RESID 75:344 )
REMARK   3    ORIGIN FOR THE GROUP (A): -81.4289  94.1402  50.7626
REMARK   3    T TENSOR
REMARK   3      T11:   1.4350 T22:   0.3399
REMARK   3      T33:   0.6471 T12:   0.3546
REMARK   3      T13:  -0.5517 T23:  -0.3418
REMARK   3    L TENSOR
REMARK   3      L11:   1.3931 L22:   1.7477
REMARK   3      L33:   0.5160 L12:   0.1716
REMARK   3      L13:  -0.2987 L23:  -0.2712
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2315 S12:   0.2375 S13:   0.8212
REMARK   3      S21:  -0.3691 S22:  -0.0431 S23:   0.6021
REMARK   3      S31:  -0.8030 S32:  -0.5835 S33:   0.0244
REMARK   3   TLS GROUP : 70
REMARK   3    SELECTION: (CHAIN V AND RESID 345:459 )
REMARK   3    ORIGIN FOR THE GROUP (A): -97.3520  68.0883  49.3562
REMARK   3    T TENSOR
REMARK   3      T11:   0.9980 T22:   0.8566
REMARK   3      T33:   1.1550 T12:   0.2716
REMARK   3      T13:  -0.2750 T23:  -0.5107
REMARK   3    L TENSOR
REMARK   3      L11:   0.5681 L22:   0.3621
REMARK   3      L33:   0.3583 L12:  -0.2548
REMARK   3      L13:  -0.0255 L23:   0.0310
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0392 S12:   0.2553 S13:  -0.0523
REMARK   3      S21:  -0.1188 S22:  -0.2520 S23:   0.8493
REMARK   3      S31:  -0.0979 S32:  -0.5682 S33:  -0.0002
REMARK   3   TLS GROUP : 71
REMARK   3    SELECTION: (CHAIN W AND (RESID 1:284 OR RESID 300:300 ) )
REMARK   3    ORIGIN FOR THE GROUP (A): -97.2533  32.8391  54.1781
REMARK   3    T TENSOR
REMARK   3      T11:   0.4688 T22:   0.7765
REMARK   3      T33:   0.9879 T12:  -0.0359
REMARK   3      T13:   0.0762 T23:  -0.6188
REMARK   3    L TENSOR
REMARK   3      L11:   0.8996 L22:   2.1885
REMARK   3      L33:   0.6964 L12:   0.3815
REMARK   3      L13:  -0.3969 L23:   0.0469
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3539 S12:   0.0899 S13:  -0.0689
REMARK   3      S21:  -0.3073 S22:  -0.2801 S23:   1.1550
REMARK   3      S31:  -0.1041 S32:  -0.6756 S33:  -0.0000
REMARK   3   TLS GROUP : 72
REMARK   3    SELECTION: (CHAIN X AND (RESID 1:138 OR RESID 139:139 ) )
REMARK   3    ORIGIN FOR THE GROUP (A): -98.0161  15.9359  62.2378
REMARK   3    T TENSOR
REMARK   3      T11:   0.5530 T22:   0.8348
REMARK   3      T33:   0.8772 T12:  -0.2991
REMARK   3      T13:   0.4028 T23:  -0.4582
REMARK   3    L TENSOR
REMARK   3      L11:   2.1510 L22:   0.6081
REMARK   3      L33:   1.9279 L12:   0.1941
REMARK   3      L13:   0.0344 L23:   1.0683
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2024 S12:  -0.1821 S13:  -0.4897
REMARK   3      S21:   1.0702 S22:  -0.3223 S23:   0.9013
REMARK   3      S31:   0.6904 S32:  -0.8905 S33:   0.0002
REMARK   3   TLS GROUP : 73
REMARK   3    SELECTION: (CHAIN Y AND RESID 24:94 )
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1074 -38.9622 -87.0962
REMARK   3    T TENSOR
REMARK   3      T11:   0.6085 T22:   1.1120
REMARK   3      T33:   1.6592 T12:   0.4215
REMARK   3      T13:   0.5131 T23:  -0.8772
REMARK   3    L TENSOR
REMARK   3      L11:   0.3996 L22:   0.6281
REMARK   3      L33:   0.2521 L12:   0.3909
REMARK   3      L13:   0.0597 L23:   0.2560
REMARK   3    S TENSOR
REMARK   3      S11:   0.1854 S12:   0.3375 S13:  -0.3973
REMARK   3      S21:  -0.0007 S22:  -0.1343 S23:  -0.4820
REMARK   3      S31:   0.3502 S32:   0.3408 S33:  -0.0020
REMARK   3   TLS GROUP : 74
REMARK   3    SELECTION: (CHAIN Y AND RESID 95:382 )
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0777 -11.6891 -86.5842
REMARK   3    T TENSOR
REMARK   3      T11:   0.3817 T22:   1.2989
REMARK   3      T33:   0.9868 T12:  -0.1871
REMARK   3      T13:   0.5864 T23:  -0.7743
REMARK   3    L TENSOR
REMARK   3      L11:   1.5042 L22:   2.1889
REMARK   3      L33:   2.4610 L12:  -0.3717
REMARK   3      L13:   1.2020 L23:   0.1270
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2260 S12:   0.7258 S13:  -0.3660
REMARK   3      S21:  -0.4678 S22:   0.1717 S23:  -0.3580
REMARK   3      S31:  -0.2848 S32:   0.6807 S33:  -0.0465
REMARK   3   TLS GROUP : 75
REMARK   3    SELECTION: (CHAIN Y AND RESID 383:511 )
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4698  15.5803 -92.1422
REMARK   3    T TENSOR
REMARK   3      T11:   1.3604 T22:   1.1980
REMARK   3      T33:   1.2738 T12:  -0.1251
REMARK   3      T13:   0.0495 T23:  -0.2178
REMARK   3    L TENSOR
REMARK   3      L11:   0.4448 L22:   0.7771
REMARK   3      L33:   0.1810 L12:  -0.4092
REMARK   3      L13:   0.1292 L23:   0.1332
REMARK   3    S TENSOR
REMARK   3      S11:  -0.5029 S12:   0.5258 S13:   0.7966
REMARK   3      S21:  -0.6996 S22:  -0.1819 S23:  -0.1111
REMARK   3      S31:  -0.4406 S32:   0.1662 S33:  -0.0005
REMARK   3   TLS GROUP : 76
REMARK   3    SELECTION: (CHAIN Y AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A):   9.3126  -6.5264-101.7069
REMARK   3    T TENSOR
REMARK   3      T11:   1.3379 T22:   1.6747
REMARK   3      T33:   1.8868 T12:  -0.7082
REMARK   3      T13:   0.9377 T23:  -1.0641
REMARK   3    L TENSOR
REMARK   3      L11:   0.0055 L22:   0.0118
REMARK   3      L33:   0.0013 L12:   0.0041
REMARK   3      L13:   0.0025 L23:   0.0003
REMARK   3    S TENSOR
REMARK   3      S11:   0.0977 S12:   0.1983 S13:  -0.0037
REMARK   3      S21:  -0.0474 S22:   0.0554 S23:   0.0282
REMARK   3      S31:  -0.0382 S32:  -0.0956 S33:   0.0002
REMARK   3   TLS GROUP : 77
REMARK   3    SELECTION: (CHAIN Z AND RESID 26:94 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.5237 -57.2012 -63.3618
REMARK   3    T TENSOR
REMARK   3      T11:   1.4965 T22:   1.1096
REMARK   3      T33:   1.9253 T12:   0.1399
REMARK   3      T13:   0.1851 T23:  -0.0266
REMARK   3    L TENSOR
REMARK   3      L11:   0.0230 L22:   0.0448
REMARK   3      L33:   0.0079 L12:   0.0143
REMARK   3      L13:  -0.0054 L23:  -0.0064
REMARK   3    S TENSOR
REMARK   3      S11:   0.1970 S12:  -0.3095 S13:  -0.4051
REMARK   3      S21:   0.2731 S22:  -0.2160 S23:  -0.2400
REMARK   3      S31:   0.5922 S32:  -0.1362 S33:   0.0000
REMARK   3   TLS GROUP : 78
REMARK   3    SELECTION: (CHAIN Z AND RESID 95:382 )
REMARK   3    ORIGIN FOR THE GROUP (A): -27.6487 -43.5332 -65.0295
REMARK   3    T TENSOR
REMARK   3      T11:   0.9924 T22:   0.8862
REMARK   3      T33:   1.0895 T12:  -0.1216
REMARK   3      T13:   0.4343 T23:  -0.0382
REMARK   3    L TENSOR
REMARK   3      L11:   1.4565 L22:   1.3119
REMARK   3      L33:   1.6006 L12:  -0.4579
REMARK   3      L13:   0.3881 L23:  -0.2216
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0581 S12:  -0.3115 S13:  -0.5458
REMARK   3      S21:   0.3436 S22:   0.1552 S23:  -0.0554
REMARK   3      S31:   0.5997 S32:  -0.7078 S33:   0.0000
REMARK   3   TLS GROUP : 79
REMARK   3    SELECTION: (CHAIN Z AND RESID 383:511 )
REMARK   3    ORIGIN FOR THE GROUP (A): -52.8985 -25.5258 -65.3011
REMARK   3    T TENSOR
REMARK   3      T11:   0.8824 T22:   2.0299
REMARK   3      T33:   2.1857 T12:  -0.1485
REMARK   3      T13:   0.3296 T23:  -0.2101
REMARK   3    L TENSOR
REMARK   3      L11:   0.2609 L22:   0.8896
REMARK   3      L33:   0.3661 L12:   0.2263
REMARK   3      L13:   0.0647 L23:   0.5353
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0465 S12:   0.3387 S13:  -0.0795
REMARK   3      S21:  -0.1214 S22:  -0.0902 S23:   1.3509
REMARK   3      S31:  -0.6671 S32:  -1.1793 S33:   0.0001
REMARK   3   TLS GROUP : 80
REMARK   3    SELECTION: (CHAIN Z AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -27.4891 -26.2129 -63.1447
REMARK   3    T TENSOR
REMARK   3      T11:   1.8266 T22:   2.1648
REMARK   3      T33:   1.6452 T12:  -0.1545
REMARK   3      T13:  -0.1167 T23:  -0.5949
REMARK   3    L TENSOR
REMARK   3      L11:   0.1475 L22:   0.0405
REMARK   3      L33:   0.0441 L12:  -0.0601
REMARK   3      L13:  -0.0709 L23:   0.0196
REMARK   3    S TENSOR
REMARK   3      S11:   0.1006 S12:   0.0135 S13:   0.0292
REMARK   3      S21:   0.1819 S22:   0.1999 S23:   0.0066
REMARK   3      S31:  -0.0946 S32:  -0.1700 S33:   0.0010
REMARK   3   TLS GROUP : 81
REMARK   3    SELECTION: (CHAIN a AND RESID 25:94 )
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0069 -67.6017-104.0990
REMARK   3    T TENSOR
REMARK   3      T11:   1.6927 T22:   1.0238
REMARK   3      T33:   1.7914 T12:   0.3005
REMARK   3      T13:   0.1818 T23:  -0.5743
REMARK   3    L TENSOR
REMARK   3      L11:   0.0839 L22:   0.2195
REMARK   3      L33:   0.2434 L12:  -0.0064
REMARK   3      L13:  -0.0997 L23:  -0.1553
REMARK   3    S TENSOR
REMARK   3      S11:   0.5609 S12:   0.5444 S13:  -0.7630
REMARK   3      S21:   0.1059 S22:   0.0956 S23:  -0.3325
REMARK   3      S31:   0.7482 S32:   0.6262 S33:   0.0002
REMARK   3   TLS GROUP : 82
REMARK   3    SELECTION: (CHAIN a AND RESID 95:382 )
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8663 -46.6173-119.4463
REMARK   3    T TENSOR
REMARK   3      T11:   1.2873 T22:   0.8955
REMARK   3      T33:   0.8171 T12:   0.0074
REMARK   3      T13:   0.4806 T23:  -0.7141
REMARK   3    L TENSOR
REMARK   3      L11:   0.8190 L22:   1.2505
REMARK   3      L33:   0.9958 L12:  -0.1416
REMARK   3      L13:   0.8946 L23:  -0.1693
REMARK   3    S TENSOR
REMARK   3      S11:   0.1015 S12:   0.3688 S13:  -0.3014
REMARK   3      S21:  -0.5661 S22:  -0.0159 S23:  -0.0101
REMARK   3      S31:   0.1629 S32:   0.1938 S33:   0.0034
REMARK   3   TLS GROUP : 83
REMARK   3    SELECTION: (CHAIN a AND RESID 383:511 )
REMARK   3    ORIGIN FOR THE GROUP (A): -31.5392 -22.9062-130.3409
REMARK   3    T TENSOR
REMARK   3      T11:   1.6008 T22:   1.5084
REMARK   3      T33:   0.6196 T12:   0.0113
REMARK   3      T13:   0.1117 T23:  -0.5955
REMARK   3    L TENSOR
REMARK   3      L11:   0.3091 L22:   0.5668
REMARK   3      L33:   0.3980 L12:   0.1384
REMARK   3      L13:   0.0685 L23:  -0.4063
REMARK   3    S TENSOR
REMARK   3      S11:   0.0931 S12:   0.5639 S13:  -0.0692
REMARK   3      S21:  -0.5038 S22:  -0.0467 S23:   0.2082
REMARK   3      S31:  -0.4596 S32:  -0.5786 S33:  -0.0000
REMARK   3   TLS GROUP : 84
REMARK   3    SELECTION: (CHAIN a AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A): -28.9396 -41.4105-112.9144
REMARK   3    T TENSOR
REMARK   3      T11:   1.1760 T22:   1.5042
REMARK   3      T33:   0.5235 T12:  -0.0471
REMARK   3      T13:  -0.0975 T23:  -0.5779
REMARK   3    L TENSOR
REMARK   3      L11:   0.0071 L22:   0.0181
REMARK   3      L33:   0.0165 L12:   0.0114
REMARK   3      L13:   0.0110 L23:   0.0175
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0921 S12:   0.0129 S13:   0.0781
REMARK   3      S21:  -0.0937 S22:  -0.0242 S23:   0.1034
REMARK   3      S31:  -0.0857 S32:  -0.0326 S33:   0.0009
REMARK   3   TLS GROUP : 85
REMARK   3    SELECTION: (CHAIN b AND RESID 2:74 )
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1548 -51.9888-107.7860
REMARK   3    T TENSOR
REMARK   3      T11:   1.3066 T22:   1.4489
REMARK   3      T33:   1.7232 T12:   0.3607
REMARK   3      T13:   0.3781 T23:  -0.7473
REMARK   3    L TENSOR
REMARK   3      L11:   0.0139 L22:   0.2480
REMARK   3      L33:   0.0160 L12:   0.0575
REMARK   3      L13:  -0.0151 L23:  -0.0660
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0562 S12:   0.1199 S13:   0.5205
REMARK   3      S21:  -0.1538 S22:  -0.0139 S23:  -0.1510
REMARK   3      S31:   0.3803 S32:   0.6204 S33:  -0.0002
REMARK   3   TLS GROUP : 86
REMARK   3    SELECTION: (CHAIN b AND RESID 75:344 )
REMARK   3    ORIGIN FOR THE GROUP (A):   9.7552 -25.7387-117.9724
REMARK   3    T TENSOR
REMARK   3      T11:   1.3107 T22:   1.4134
REMARK   3      T33:   0.7217 T12:  -0.1328
REMARK   3      T13:   0.8741 T23:  -0.7537
REMARK   3    L TENSOR
REMARK   3      L11:   0.7534 L22:   1.1488
REMARK   3      L33:   1.3272 L12:   0.0668
REMARK   3      L13:   0.4897 L23:  -0.9810
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2926 S12:   0.7105 S13:  -0.1343
REMARK   3      S21:  -0.5796 S22:   0.0530 S23:  -0.8605
REMARK   3      S31:  -0.3854 S32:   0.5866 S33:  -0.0409
REMARK   3   TLS GROUP : 87
REMARK   3    SELECTION: (CHAIN b AND RESID 345:459 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.5041  -2.0516-126.1929
REMARK   3    T TENSOR
REMARK   3      T11:   1.5865 T22:   1.4021
REMARK   3      T33:   0.6478 T12:  -0.1169
REMARK   3      T13:   0.3678 T23:  -0.2425
REMARK   3    L TENSOR
REMARK   3      L11:   0.4160 L22:   0.2673
REMARK   3      L33:   0.1961 L12:   0.3273
REMARK   3      L13:   0.0311 L23:   0.0085
REMARK   3    S TENSOR
REMARK   3      S11:   0.1412 S12:   0.7941 S13:   0.3155
REMARK   3      S21:   0.0424 S22:  -0.1762 S23:  -0.2100
REMARK   3      S31:  -0.0862 S32:  -0.1441 S33:   0.0000
REMARK   3   TLS GROUP : 88
REMARK   3    SELECTION: (CHAIN b AND RESID 600:601 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.4864 -24.8496-124.9108
REMARK   3    T TENSOR
REMARK   3      T11:   2.7207 T22:   1.9385
REMARK   3      T33:   0.2854 T12:   0.0240
REMARK   3      T13:   0.6947 T23:  -0.1540
REMARK   3    L TENSOR
REMARK   3      L11:   0.0414 L22:   0.0851
REMARK   3      L33:   0.1935 L12:  -0.0598
REMARK   3      L13:   0.0800 L23:  -0.1159
REMARK   3    S TENSOR
REMARK   3      S11:   0.0232 S12:   0.0533 S13:   0.1085
REMARK   3      S21:  -0.1621 S22:  -0.0437 S23:   0.2187
REMARK   3      S31:  -0.0895 S32:  -0.0730 S33:   0.0005
REMARK   3   TLS GROUP : 89
REMARK   3    SELECTION: (CHAIN c AND RESID 2:74 )
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5355 -40.2511 -65.3043
REMARK   3    T TENSOR
REMARK   3      T11:   0.8459 T22:   0.8554
REMARK   3      T33:   2.1732 T12:   0.3547
REMARK   3      T13:   0.3054 T23:  -0.5129
REMARK   3    L TENSOR
REMARK   3      L11:   0.1327 L22:   0.0045
REMARK   3      L33:   0.3099 L12:  -0.0258
REMARK   3      L13:   0.0548 L23:  -0.0248
REMARK   3    S TENSOR
REMARK   3      S11:   0.2457 S12:  -0.2571 S13:  -0.7413
REMARK   3      S21:   0.6488 S22:   0.4064 S23:   0.0717
REMARK   3      S31:   0.5989 S32:   1.1651 S33:   0.0008
REMARK   3   TLS GROUP : 90
REMARK   3    SELECTION: (CHAIN c AND RESID 75:344 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.7419 -19.0766 -60.7717
REMARK   3    T TENSOR
REMARK   3      T11:   0.5413 T22:   0.6779
REMARK   3      T33:   1.0803 T12:   0.2161
REMARK   3      T13:   0.4255 T23:  -0.1998
REMARK   3    L TENSOR
REMARK   3      L11:   1.4179 L22:   2.1057
REMARK   3      L33:   2.3099 L12:   0.6530
REMARK   3      L13:   0.5453 L23:   1.2966
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3418 S12:  -0.1925 S13:  -0.9497
REMARK   3      S21:   0.0561 S22:   0.3530 S23:  -0.2532
REMARK   3      S31:   0.2521 S32:  -0.0316 S33:   0.0002
REMARK   3   TLS GROUP : 91
REMARK   3    SELECTION: (CHAIN c AND RESID 345:459 )
REMARK   3    ORIGIN FOR THE GROUP (A): -24.2011   2.5528 -60.5449
REMARK   3    T TENSOR
REMARK   3      T11:   0.7488 T22:   1.2443
REMARK   3      T33:   0.8341 T12:   0.4811
REMARK   3      T13:   0.1434 T23:  -0.2828
REMARK   3    L TENSOR
REMARK   3      L11:   0.9377 L22:   1.5608
REMARK   3      L33:   0.6612 L12:   0.4294
REMARK   3      L13:  -0.3068 L23:  -0.3929
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3723 S12:  -0.0918 S13:  -0.4140
REMARK   3      S21:  -0.3381 S22:   0.0766 S23:   0.9137
REMARK   3      S31:  -0.0230 S32:  -0.4184 S33:   0.0203
REMARK   3   TLS GROUP : 92
REMARK   3    SELECTION: (CHAIN d AND RESID 2:74 )
REMARK   3    ORIGIN FOR THE GROUP (A): -10.6757 -70.8601 -81.1132
REMARK   3    T TENSOR
REMARK   3      T11:   1.6489 T22:   1.0165
REMARK   3      T33:   1.8996 T12:   0.0743
REMARK   3      T13:  -0.0349 T23:  -0.3677
REMARK   3    L TENSOR
REMARK   3      L11:   0.0600 L22:   0.1848
REMARK   3      L33:   0.0682 L12:  -0.0560
REMARK   3      L13:   0.0342 L23:  -0.1151
REMARK   3    S TENSOR
REMARK   3      S11:   0.3713 S12:  -0.6703 S13:  -1.1819
REMARK   3      S21:  -0.0565 S22:   0.0624 S23:   0.6984
REMARK   3      S31:   0.8035 S32:  -0.1198 S33:   0.0005
REMARK   3   TLS GROUP : 93
REMARK   3    SELECTION: (CHAIN d AND RESID 75:344 )
REMARK   3    ORIGIN FOR THE GROUP (A): -32.5456 -55.7355 -92.9594
REMARK   3    T TENSOR
REMARK   3      T11:   1.2232 T22:   0.7905
REMARK   3      T33:   1.2493 T12:  -0.3710
REMARK   3      T13:   0.3184 T23:  -0.5688
REMARK   3    L TENSOR
REMARK   3      L11:   0.4907 L22:   1.1290
REMARK   3      L33:   0.5355 L12:  -0.0494
REMARK   3      L13:  -0.0520 L23:  -0.3315
REMARK   3    S TENSOR
REMARK   3      S11:   0.2588 S12:  -0.0787 S13:  -0.8060
REMARK   3      S21:  -0.2434 S22:  -0.3000 S23:   0.4876
REMARK   3      S31:   0.8481 S32:  -0.6943 S33:   0.0030
REMARK   3   TLS GROUP : 94
REMARK   3    SELECTION: (CHAIN d AND RESID 345:459 )
REMARK   3    ORIGIN FOR THE GROUP (A): -47.0779 -29.8138-100.1660
REMARK   3    T TENSOR
REMARK   3      T11:   1.2153 T22:   1.3237
REMARK   3      T33:   1.2714 T12:  -0.1326
REMARK   3      T13:   0.1340 T23:  -0.7077
REMARK   3    L TENSOR
REMARK   3      L11:   0.7031 L22:   0.4848
REMARK   3      L33:   0.5870 L12:  -0.0588
REMARK   3      L13:   0.5595 L23:  -0.3108
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1404 S12:  -0.1488 S13:  -0.3541
REMARK   3      S21:  -0.3385 S22:   0.0103 S23:  -0.0183
REMARK   3      S31:   0.1937 S32:  -0.7740 S33:   0.0000
REMARK   3   TLS GROUP : 95
REMARK   3    SELECTION: (CHAIN e AND RESID 1:284 )
REMARK   3    ORIGIN FOR THE GROUP (A): -45.3208   5.8603-102.3741
REMARK   3    T TENSOR
REMARK   3      T11:   1.1589 T22:   1.4300
REMARK   3      T33:   0.6484 T12:   0.0827
REMARK   3      T13:  -0.0949 T23:  -0.8230
REMARK   3    L TENSOR
REMARK   3      L11:   0.2993 L22:   2.3880
REMARK   3      L33:   1.0187 L12:   0.0390
REMARK   3      L13:   0.1780 L23:  -0.6663
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1381 S12:   0.3499 S13:  -0.4311
REMARK   3      S21:  -0.7259 S22:   0.0660 S23:   0.9394
REMARK   3      S31:  -0.2154 S32:  -0.6333 S33:   0.0228
REMARK   3   TLS GROUP : 96
REMARK   3    SELECTION: (CHAIN f AND RESID 1:138 )
REMARK   3    ORIGIN FOR THE GROUP (A): -41.5229  23.0782-108.9905
REMARK   3    T TENSOR
REMARK   3      T11:   1.2565 T22:   1.5086
REMARK   3      T33:   0.2450 T12:   0.1758
REMARK   3      T13:  -0.0252 T23:  -0.3938
REMARK   3    L TENSOR
REMARK   3      L11:   1.4767 L22:   0.3673
REMARK   3      L33:   0.9556 L12:  -0.3448
REMARK   3      L13:   0.0250 L23:  -0.0645
REMARK   3    S TENSOR
REMARK   3      S11:   0.0228 S12:   0.7812 S13:  -0.0122
REMARK   3      S21:  -0.9478 S22:   0.0855 S23:   0.0291
REMARK   3      S31:  -0.5080 S32:  -0.5401 S33:   0.0019
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : 12
REMARK   3   NCS GROUP : 1
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain A resid 24:511
REMARK   3     SELECTION          : chain I and resid 24:511
REMARK   3     ATOM PAIRS NUMBER  : 3667
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain A resid 24:511
REMARK   3     SELECTION          : chain Q and resid 24:511
REMARK   3     ATOM PAIRS NUMBER  : 3667
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain A resid 24:511
REMARK   3     SELECTION          : chain Y and resid 24:511
REMARK   3     ATOM PAIRS NUMBER  : 3667
REMARK   3     RMSD               : NULL
REMARK   3   NCS GROUP : 2
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain A resid 600:601
REMARK   3     SELECTION          : chain I and resid 600:601
REMARK   3     ATOM PAIRS NUMBER  : 32
REMARK   3     RMSD               : 0.006
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain A resid 600:601
REMARK   3     SELECTION          : chain Q and resid 600:601
REMARK   3     ATOM PAIRS NUMBER  : 32
REMARK   3     RMSD               : 0.008
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain A resid 600:601
REMARK   3     SELECTION          : chain Y and resid 600:601
REMARK   3     ATOM PAIRS NUMBER  : 32
REMARK   3     RMSD               : 0.007
REMARK   3   NCS GROUP : 3
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain B resid 26:511
REMARK   3     SELECTION          : chain J and resid 26:511
REMARK   3     ATOM PAIRS NUMBER  : 3627
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain B resid 26:511
REMARK   3     SELECTION          : chain R and resid 26:511
REMARK   3     ATOM PAIRS NUMBER  : 3627
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain B resid 26:511
REMARK   3     SELECTION          : chain Z and resid 26:511
REMARK   3     ATOM PAIRS NUMBER  : 3627
REMARK   3     RMSD               : NULL
REMARK   3   NCS GROUP : 4
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain B resid 600:601
REMARK   3     SELECTION          : chain J and resid 600:601
REMARK   3     ATOM PAIRS NUMBER  : 32
REMARK   3     RMSD               : 0.006
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain B resid 600:601
REMARK   3     SELECTION          : chain R and resid 600:601
REMARK   3     ATOM PAIRS NUMBER  : 32
REMARK   3     RMSD               : 0.007
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain B resid 600:601
REMARK   3     SELECTION          : chain Z and resid 600:601
REMARK   3     ATOM PAIRS NUMBER  : 32
REMARK   3     RMSD               : 0.006
REMARK   3   NCS GROUP : 5
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain C resid 25:511
REMARK   3     SELECTION          : chain K and resid 25:511
REMARK   3     ATOM PAIRS NUMBER  : 3646
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain C resid 25:511
REMARK   3     SELECTION          : chain S and resid 25:511
REMARK   3     ATOM PAIRS NUMBER  : 3646
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain C resid 25:511
REMARK   3     SELECTION          : chain a and resid 25:511
REMARK   3     ATOM PAIRS NUMBER  : 3646
REMARK   3     RMSD               : NULL
REMARK   3   NCS GROUP : 6
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain C resid 600:601
REMARK   3     SELECTION          : chain K and resid 600:601
REMARK   3     ATOM PAIRS NUMBER  : 32
REMARK   3     RMSD               : 0.006
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain C resid 600:601
REMARK   3     SELECTION          : chain S and resid 600:601
REMARK   3     ATOM PAIRS NUMBER  : 32
REMARK   3     RMSD               : 0.008
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain C resid 600:601
REMARK   3     SELECTION          : chain a and resid 600:601
REMARK   3     ATOM PAIRS NUMBER  : 32
REMARK   3     RMSD               : 0.008
REMARK   3   NCS GROUP : 7
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain D resid 2:259
REMARK   3     SELECTION          : chain L and resid 2:259
REMARK   3     ATOM PAIRS NUMBER  : 1970
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain D resid 2:259
REMARK   3     SELECTION          : chain T and resid 2:259
REMARK   3     ATOM PAIRS NUMBER  : 1970
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain D resid 2:259
REMARK   3     SELECTION          : chain b and resid 2:259
REMARK   3     ATOM PAIRS NUMBER  : 1970
REMARK   3     RMSD               : NULL
REMARK   3   NCS GROUP : 8
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain D resid 600:601
REMARK   3     SELECTION          : chain L and resid 600:601
REMARK   3     ATOM PAIRS NUMBER  : 28
REMARK   3     RMSD               : 0.008
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain D resid 600:601
REMARK   3     SELECTION          : chain T and resid 600:601
REMARK   3     ATOM PAIRS NUMBER  : 28
REMARK   3     RMSD               : 0.008
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain D resid 600:601
REMARK   3     SELECTION          : chain b and resid 600:601
REMARK   3     ATOM PAIRS NUMBER  : 28
REMARK   3     RMSD               : 0.006
REMARK   3   NCS GROUP : 9
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain E resid 2:259
REMARK   3     SELECTION          : chain M and resid 2:259
REMARK   3     ATOM PAIRS NUMBER  : 1970
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain E resid 2:259
REMARK   3     SELECTION          : chain U and resid 2:259
REMARK   3     ATOM PAIRS NUMBER  : 1970
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain E resid 2:259
REMARK   3     SELECTION          : chain c and resid 2:259
REMARK   3     ATOM PAIRS NUMBER  : 1970
REMARK   3     RMSD               : NULL
REMARK   3   NCS GROUP : 10
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain F resid 2:259
REMARK   3     SELECTION          : chain N and resid 2:259
REMARK   3     ATOM PAIRS NUMBER  : 1970
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain F resid 2:259
REMARK   3     SELECTION          : chain V and resid 2:259
REMARK   3     ATOM PAIRS NUMBER  : 1970
REMARK   3     RMSD               : NULL
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain F resid 2:259
REMARK   3     SELECTION          : chain d and resid 2:259
REMARK   3     ATOM PAIRS NUMBER  : 1970
REMARK   3     RMSD               : NULL
REMARK   3   NCS GROUP : 11
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain G resid 1:284
REMARK   3     SELECTION          : chain O and resid 1:284
REMARK   3     ATOM PAIRS NUMBER  : 2182
REMARK   3     RMSD               : 0.001
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain G resid 1:284
REMARK   3     SELECTION          : chain W and resid 1:284
REMARK   3     ATOM PAIRS NUMBER  : 2182
REMARK   3     RMSD               : 0.001
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain G resid 1:284
REMARK   3     SELECTION          : chain e and resid 1:284
REMARK   3     ATOM PAIRS NUMBER  : 2182
REMARK   3     RMSD               : 0.001
REMARK   3   NCS GROUP : 12
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: chain H resid 1:138
REMARK   3     SELECTION          : chain P and resid 1:138
REMARK   3     ATOM PAIRS NUMBER  : 1047
REMARK   3     RMSD               : 0.001
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: chain H resid 1:138
REMARK   3     SELECTION          : chain X and resid 1:138
REMARK   3     ATOM PAIRS NUMBER  : 1047
REMARK   3     RMSD               : 0.001
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: chain H resid 1:138
REMARK   3     SELECTION          : chain f and resid 1:138
REMARK   3     ATOM PAIRS NUMBER  : 1047
REMARK   3     RMSD               : 0.001
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3OAA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB060862.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-08; NULL; NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL; NULL
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; Y
REMARK 200  RADIATION SOURCE               : NSLS; NSLS; CHESS
REMARK 200  BEAMLINE                       : X25; X6A; F1
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL; NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL; NULL; NULL
REMARK 200  MONOCHROMATOR                  : NULL; NULL; NULL
REMARK 200  OPTICS                         : NULL; NULL; NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD; NULL; NULL
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R; NULL; NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 252390
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.260
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5
REMARK 200  DATA REDUNDANCY                : 2.500
REMARK 200  R MERGE                    (I) : 0.09200
REMARK 200  R SYM                      (I) : 0.09200
REMARK 200   FOR THE DATA SET  : 15.4400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.26
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.36
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.62600
REMARK 200  R SYM FOR SHELL            (I) : 0.62600
REMARK 200   FOR SHELL         : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2CK3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MOPS-NAOH, 75-150 MM MGSO4, 7-9%
REMARK 280  PEG8000, 5 MM BETA-MERCAPTOETHANOL, PH 7.0, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
REMARK 290       4555   -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      217.98500
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       91.50000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      217.98500
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       91.50000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L, M, N, O, P
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, R, S, T, U, V, W, X
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Y, Z, a, b, c, d, e, f
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     GLN A     2
REMARK 465     LEU A     3
REMARK 465     ASN A     4
REMARK 465     SER A     5
REMARK 465     THR A     6
REMARK 465     GLU A     7
REMARK 465     ILE A     8
REMARK 465     SER A     9
REMARK 465     GLU A    10
REMARK 465     LEU A    11
REMARK 465     ILE A    12
REMARK 465     LYS A    13
REMARK 465     GLN A    14
REMARK 465     ARG A    15
REMARK 465     ILE A    16
REMARK 465     ALA A    17
REMARK 465     GLN A    18
REMARK 465     PHE A    19
REMARK 465     ASN A    20
REMARK 465     VAL A    21
REMARK 465     VAL A    22
REMARK 465     SER A    23
REMARK 465     SER A   512
REMARK 465     TRP A   513
REMARK 465     MET B     1
REMARK 465     GLN B     2
REMARK 465     LEU B     3
REMARK 465     ASN B     4
REMARK 465     SER B     5
REMARK 465     THR B     6
REMARK 465     GLU B     7
REMARK 465     ILE B     8
REMARK 465     SER B     9
REMARK 465     GLU B    10
REMARK 465     LEU B    11
REMARK 465     ILE B    12
REMARK 465     LYS B    13
REMARK 465     GLN B    14
REMARK 465     ARG B    15
REMARK 465     ILE B    16
REMARK 465     ALA B    17
REMARK 465     GLN B    18
REMARK 465     PHE B    19
REMARK 465     ASN B    20
REMARK 465     VAL B    21
REMARK 465     VAL B    22
REMARK 465     SER B    23
REMARK 465     GLU B    24
REMARK 465     ALA B    25
REMARK 465     SER B   512
REMARK 465     TRP B   513
REMARK 465     MET C     1
REMARK 465     GLN C     2
REMARK 465     LEU C     3
REMARK 465     ASN C     4
REMARK 465     SER C     5
REMARK 465     THR C     6
REMARK 465     GLU C     7
REMARK 465     ILE C     8
REMARK 465     SER C     9
REMARK 465     GLU C    10
REMARK 465     LEU C    11
REMARK 465     ILE C    12
REMARK 465     LYS C    13
REMARK 465     GLN C    14
REMARK 465     ARG C    15
REMARK 465     ILE C    16
REMARK 465     ALA C    17
REMARK 465     GLN C    18
REMARK 465     PHE C    19
REMARK 465     ASN C    20
REMARK 465     VAL C    21
REMARK 465     VAL C    22
REMARK 465     SER C    23
REMARK 465     GLU C    24
REMARK 465     SER C   512
REMARK 465     TRP C   513
REMARK 465     ALA D     1
REMARK 465     ALA E     1
REMARK 465     ALA F     1
REMARK 465     ALA G   285
REMARK 465     VAL G   286
REMARK 465     MET I     1
REMARK 465     GLN I     2
REMARK 465     LEU I     3
REMARK 465     ASN I     4
REMARK 465     SER I     5
REMARK 465     THR I     6
REMARK 465     GLU I     7
REMARK 465     ILE I     8
REMARK 465     SER I     9
REMARK 465     GLU I    10
REMARK 465     LEU I    11
REMARK 465     ILE I    12
REMARK 465     LYS I    13
REMARK 465     GLN I    14
REMARK 465     ARG I    15
REMARK 465     ILE I    16
REMARK 465     ALA I    17
REMARK 465     GLN I    18
REMARK 465     PHE I    19
REMARK 465     ASN I    20
REMARK 465     VAL I    21
REMARK 465     VAL I    22
REMARK 465     SER I    23
REMARK 465     SER I   512
REMARK 465     TRP I   513
REMARK 465     MET J     1
REMARK 465     GLN J     2
REMARK 465     LEU J     3
REMARK 465     ASN J     4
REMARK 465     SER J     5
REMARK 465     THR J     6
REMARK 465     GLU J     7
REMARK 465     ILE J     8
REMARK 465     SER J     9
REMARK 465     GLU J    10
REMARK 465     LEU J    11
REMARK 465     ILE J    12
REMARK 465     LYS J    13
REMARK 465     GLN J    14
REMARK 465     ARG J    15
REMARK 465     ILE J    16
REMARK 465     ALA J    17
REMARK 465     GLN J    18
REMARK 465     PHE J    19
REMARK 465     ASN J    20
REMARK 465     VAL J    21
REMARK 465     VAL J    22
REMARK 465     SER J    23
REMARK 465     GLU J    24
REMARK 465     ALA J    25
REMARK 465     SER J   512
REMARK 465     TRP J   513
REMARK 465     MET K     1
REMARK 465     GLN K     2
REMARK 465     LEU K     3
REMARK 465     ASN K     4
REMARK 465     SER K     5
REMARK 465     THR K     6
REMARK 465     GLU K     7
REMARK 465     ILE K     8
REMARK 465     SER K     9
REMARK 465     GLU K    10
REMARK 465     LEU K    11
REMARK 465     ILE K    12
REMARK 465     LYS K    13
REMARK 465     GLN K    14
REMARK 465     ARG K    15
REMARK 465     ILE K    16
REMARK 465     ALA K    17
REMARK 465     GLN K    18
REMARK 465     PHE K    19
REMARK 465     ASN K    20
REMARK 465     VAL K    21
REMARK 465     VAL K    22
REMARK 465     SER K    23
REMARK 465     GLU K    24
REMARK 465     SER K   512
REMARK 465     TRP K   513
REMARK 465     ALA L     1
REMARK 465     ALA M     1
REMARK 465     ALA N     1
REMARK 465     ALA O   285
REMARK 465     VAL O   286
REMARK 465     MET Q     1
REMARK 465     GLN Q     2
REMARK 465     LEU Q     3
REMARK 465     ASN Q     4
REMARK 465     SER Q     5
REMARK 465     THR Q     6
REMARK 465     GLU Q     7
REMARK 465     ILE Q     8
REMARK 465     SER Q     9
REMARK 465     GLU Q    10
REMARK 465     LEU Q    11
REMARK 465     ILE Q    12
REMARK 465     LYS Q    13
REMARK 465     GLN Q    14
REMARK 465     ARG Q    15
REMARK 465     ILE Q    16
REMARK 465     ALA Q    17
REMARK 465     GLN Q    18
REMARK 465     PHE Q    19
REMARK 465     ASN Q    20
REMARK 465     VAL Q    21
REMARK 465     VAL Q    22
REMARK 465     SER Q    23
REMARK 465     SER Q   512
REMARK 465     TRP Q   513
REMARK 465     MET R     1
REMARK 465     GLN R     2
REMARK 465     LEU R     3
REMARK 465     ASN R     4
REMARK 465     SER R     5
REMARK 465     THR R     6
REMARK 465     GLU R     7
REMARK 465     ILE R     8
REMARK 465     SER R     9
REMARK 465     GLU R    10
REMARK 465     LEU R    11
REMARK 465     ILE R    12
REMARK 465     LYS R    13
REMARK 465     GLN R    14
REMARK 465     ARG R    15
REMARK 465     ILE R    16
REMARK 465     ALA R    17
REMARK 465     GLN R    18
REMARK 465     PHE R    19
REMARK 465     ASN R    20
REMARK 465     VAL R    21
REMARK 465     VAL R    22
REMARK 465     SER R    23
REMARK 465     GLU R    24
REMARK 465     ALA R    25
REMARK 465     SER R   512
REMARK 465     TRP R   513
REMARK 465     MET S     1
REMARK 465     GLN S     2
REMARK 465     LEU S     3
REMARK 465     ASN S     4
REMARK 465     SER S     5
REMARK 465     THR S     6
REMARK 465     GLU S     7
REMARK 465     ILE S     8
REMARK 465     SER S     9
REMARK 465     GLU S    10
REMARK 465     LEU S    11
REMARK 465     ILE S    12
REMARK 465     LYS S    13
REMARK 465     GLN S    14
REMARK 465     ARG S    15
REMARK 465     ILE S    16
REMARK 465     ALA S    17
REMARK 465     GLN S    18
REMARK 465     PHE S    19
REMARK 465     ASN S    20
REMARK 465     VAL S    21
REMARK 465     VAL S    22
REMARK 465     SER S    23
REMARK 465     GLU S    24
REMARK 465     SER S   512
REMARK 465     TRP S   513
REMARK 465     ALA T     1
REMARK 465     ALA U     1
REMARK 465     ALA V     1
REMARK 465     ALA W   285
REMARK 465     VAL W   286
REMARK 465     MET Y     1
REMARK 465     GLN Y     2
REMARK 465     LEU Y     3
REMARK 465     ASN Y     4
REMARK 465     SER Y     5
REMARK 465     THR Y     6
REMARK 465     GLU Y     7
REMARK 465     ILE Y     8
REMARK 465     SER Y     9
REMARK 465     GLU Y    10
REMARK 465     LEU Y    11
REMARK 465     ILE Y    12
REMARK 465     LYS Y    13
REMARK 465     GLN Y    14
REMARK 465     ARG Y    15
REMARK 465     ILE Y    16
REMARK 465     ALA Y    17
REMARK 465     GLN Y    18
REMARK 465     PHE Y    19
REMARK 465     ASN Y    20
REMARK 465     VAL Y    21
REMARK 465     VAL Y    22
REMARK 465     SER Y    23
REMARK 465     SER Y   512
REMARK 465     TRP Y   513
REMARK 465     MET Z     1
REMARK 465     GLN Z     2
REMARK 465     LEU Z     3
REMARK 465     ASN Z     4
REMARK 465     SER Z     5
REMARK 465     THR Z     6
REMARK 465     GLU Z     7
REMARK 465     ILE Z     8
REMARK 465     SER Z     9
REMARK 465     GLU Z    10
REMARK 465     LEU Z    11
REMARK 465     ILE Z    12
REMARK 465     LYS Z    13
REMARK 465     GLN Z    14
REMARK 465     ARG Z    15
REMARK 465     ILE Z    16
REMARK 465     ALA Z    17
REMARK 465     GLN Z    18
REMARK 465     PHE Z    19
REMARK 465     ASN Z    20
REMARK 465     VAL Z    21
REMARK 465     VAL Z    22
REMARK 465     SER Z    23
REMARK 465     GLU Z    24
REMARK 465     ALA Z    25
REMARK 465     SER Z   512
REMARK 465     TRP Z   513
REMARK 465     MET a     1
REMARK 465     GLN a     2
REMARK 465     LEU a     3
REMARK 465     ASN a     4
REMARK 465     SER a     5
REMARK 465     THR a     6
REMARK 465     GLU a     7
REMARK 465     ILE a     8
REMARK 465     SER a     9
REMARK 465     GLU a    10
REMARK 465     LEU a    11
REMARK 465     ILE a    12
REMARK 465     LYS a    13
REMARK 465     GLN a    14
REMARK 465     ARG a    15
REMARK 465     ILE a    16
REMARK 465     ALA a    17
REMARK 465     GLN a    18
REMARK 465     PHE a    19
REMARK 465     ASN a    20
REMARK 465     VAL a    21
REMARK 465     VAL a    22
REMARK 465     SER a    23
REMARK 465     GLU a    24
REMARK 465     SER a   512
REMARK 465     TRP a   513
REMARK 465     ALA b     1
REMARK 465     ALA c     1
REMARK 465     ALA d     1
REMARK 465     ALA e   285
REMARK 465     VAL e   286
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLU A  24    CG   CD   OE1  OE2
REMARK 470     LEU A 448    CG   CD1  CD2
REMARK 470     ILE A 464    CG1  CG2  CD1
REMARK 470     PHE B 406    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     SER B 407    OG
REMARK 470     GLN B 408    CG   CD   OE1  NE2
REMARK 470     SER B 411    OG
REMARK 470     ASP B 412    CG   OD1  OD2
REMARK 470     LEU B 413    CG   CD1  CD2
REMARK 470     ASP B 414    CG   OD1  OD2
REMARK 470     ASP B 415    CG   OD1  OD2
REMARK 470     ARG B 418    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU B 448    CG   CD1  CD2
REMARK 470     ILE B 464    CG1  CG2  CD1
REMARK 470     GLU C 310    CG   CD   OE1  OE2
REMARK 470     THR C 313    OG1  CG2
REMARK 470     LYS C 314    CG   CD   CE   NZ
REMARK 470     GLU C 316    CG   CD   OE1  OE2
REMARK 470     VAL C 317    CG1  CG2
REMARK 470     LEU C 448    CG   CD1  CD2
REMARK 470     ILE C 464    CG1  CG2  CD1
REMARK 470     LEU G  60    CG   CD1  CD2
REMARK 470     GLU G  61    CG   CD   OE1  OE2
REMARK 470     GLU I  24    CG   CD   OE1  OE2
REMARK 470     LEU I 448    CG   CD1  CD2
REMARK 470     ILE I 464    CG1  CG2  CD1
REMARK 470     PHE J 406    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     SER J 407    OG
REMARK 470     GLN J 408    CG   CD   OE1  NE2
REMARK 470     SER J 411    OG
REMARK 470     ASP J 412    CG   OD1  OD2
REMARK 470     LEU J 413    CG   CD1  CD2
REMARK 470     ASP J 414    CG   OD1  OD2
REMARK 470     ASP J 415    CG   OD1  OD2
REMARK 470     ARG J 418    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU J 448    CG   CD1  CD2
REMARK 470     ILE J 464    CG1  CG2  CD1
REMARK 470     GLU K 310    CG   CD   OE1  OE2
REMARK 470     THR K 313    OG1  CG2
REMARK 470     LYS K 314    CG   CD   CE   NZ
REMARK 470     GLU K 316    CG   CD   OE1  OE2
REMARK 470     VAL K 317    CG1  CG2
REMARK 470     LEU K 448    CG   CD1  CD2
REMARK 470     ILE K 464    CG1  CG2  CD1
REMARK 470     LEU O  60    CG   CD1  CD2
REMARK 470     GLU O  61    CG   CD   OE1  OE2
REMARK 470     GLU Q  24    CG   CD   OE1  OE2
REMARK 470     LEU Q 448    CG   CD1  CD2
REMARK 470     ILE Q 464    CG1  CG2  CD1
REMARK 470     PHE R 406    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     SER R 407    OG
REMARK 470     GLN R 408    CG   CD   OE1  NE2
REMARK 470     SER R 411    OG
REMARK 470     ASP R 412    CG   OD1  OD2
REMARK 470     LEU R 413    CG   CD1  CD2
REMARK 470     ASP R 414    CG   OD1  OD2
REMARK 470     ASP R 415    CG   OD1  OD2
REMARK 470     ARG R 418    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU R 448    CG   CD1  CD2
REMARK 470     ILE R 464    CG1  CG2  CD1
REMARK 470     GLU S 310    CG   CD   OE1  OE2
REMARK 470     THR S 313    OG1  CG2
REMARK 470     LYS S 314    CG   CD   CE   NZ
REMARK 470     GLU S 316    CG   CD   OE1  OE2
REMARK 470     VAL S 317    CG1  CG2
REMARK 470     LEU S 448    CG   CD1  CD2
REMARK 470     ILE S 464    CG1  CG2  CD1
REMARK 470     LEU W  60    CG   CD1  CD2
REMARK 470     GLU W  61    CG   CD   OE1  OE2
REMARK 470     GLU Y  24    CG   CD   OE1  OE2
REMARK 470     LEU Y 448    CG   CD1  CD2
REMARK 470     ILE Y 464    CG1  CG2  CD1
REMARK 470     PHE Z 406    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     SER Z 407    OG
REMARK 470     GLN Z 408    CG   CD   OE1  NE2
REMARK 470     SER Z 411    OG
REMARK 470     ASP Z 412    CG   OD1  OD2
REMARK 470     LEU Z 413    CG   CD1  CD2
REMARK 470     ASP Z 414    CG   OD1  OD2
REMARK 470     ASP Z 415    CG   OD1  OD2
REMARK 470     ARG Z 418    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU Z 448    CG   CD1  CD2
REMARK 470     ILE Z 464    CG1  CG2  CD1
REMARK 470     GLU a 310    CG   CD   OE1  OE2
REMARK 470     THR a 313    OG1  CG2
REMARK 470     LYS a 314    CG   CD   CE   NZ
REMARK 470     GLU a 316    CG   CD   OE1  OE2
REMARK 470     VAL a 317    CG1  CG2
REMARK 470     LEU a 448    CG   CD1  CD2
REMARK 470     ILE a 464    CG1  CG2  CD1
REMARK 470     LEU e  60    CG   CD1  CD2
REMARK 470     GLU e  61    CG   CD   OE1  OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    GLY R    50     CG2  ILE R    94              1.63
REMARK 500   C    ILE Y   137     CA   GLU Y   138              1.79
REMARK 500   C    GLY R    50     CG2  ILE R    94              2.05
REMARK 500   O    LEU J   413     N    ASP J   415              2.07
REMARK 500   O    LEU Z   413     N    ASP Z   415              2.07
REMARK 500   O    LEU R   413     N    ASP R   415              2.07
REMARK 500   CD2  LEU R    95     CG2  VAL R   129              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    GLN B 408   N   -  CA  -  C   ANGL. DEV. =  16.5 DEGREES
REMARK 500    PRO E 332   C   -  N   -  CA  ANGL. DEV. =  -9.0 DEGREES
REMARK 500    PRO G  65   C   -  N   -  CA  ANGL. DEV. =  -9.3 DEGREES
REMARK 500    ALA H   1   CB  -  CA  -  C   ANGL. DEV. =  41.2 DEGREES
REMARK 500    ALA H   1   N   -  CA  -  C   ANGL. DEV. = -20.8 DEGREES
REMARK 500    GLU I 138   N   -  CA  -  C   ANGL. DEV. =  18.3 DEGREES
REMARK 500    GLN J 408   N   -  CA  -  C   ANGL. DEV. =  16.5 DEGREES
REMARK 500    ALA L 112   CB  -  CA  -  C   ANGL. DEV. =  12.0 DEGREES
REMARK 500    PRO M 332   C   -  N   -  CA  ANGL. DEV. =  -9.4 DEGREES
REMARK 500    PRO O  65   C   -  N   -  CA  ANGL. DEV. =  -9.4 DEGREES
REMARK 500    PRO O 191   C   -  N   -  CD  ANGL. DEV. = -14.3 DEGREES
REMARK 500    GLN R 408   N   -  CA  -  C   ANGL. DEV. =  19.8 DEGREES
REMARK 500    ALA T 112   CB  -  CA  -  C   ANGL. DEV. =  16.0 DEGREES
REMARK 500    ALA T 112   N   -  CA  -  C   ANGL. DEV. = -17.4 DEGREES
REMARK 500    PRO U 332   C   -  N   -  CA  ANGL. DEV. = -10.5 DEGREES
REMARK 500    PRO W  65   C   -  N   -  CA  ANGL. DEV. =  -9.3 DEGREES
REMARK 500    PRO W 191   C   -  N   -  CD  ANGL. DEV. = -21.9 DEGREES
REMARK 500    ILE Y 137   N   -  CA  -  C   ANGL. DEV. =  32.1 DEGREES
REMARK 500    GLU Y 138   C   -  N   -  CA  ANGL. DEV. = -41.6 DEGREES
REMARK 500    GLN Z 408   N   -  CA  -  C   ANGL. DEV. =  16.5 DEGREES
REMARK 500    PRO b 114   C   -  N   -  CD  ANGL. DEV. = -18.1 DEGREES
REMARK 500    PRO e  65   C   -  N   -  CA  ANGL. DEV. =  -9.3 DEGREES
REMARK 500    PRO e 191   C   -  N   -  CD  ANGL. DEV. = -41.9 DEGREES
REMARK 500    ALA f   1   CB  -  CA  -  C   ANGL. DEV. =  41.2 DEGREES
REMARK 500    ALA f   1   N   -  CA  -  C   ANGL. DEV. = -20.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  35      127.23   -171.65
REMARK 500    ASN A  58       77.27     57.09
REMARK 500    ARG A  59      147.89   -173.71
REMARK 500    LEU A  95       58.91     34.34
REMARK 500    ASP A 143        6.00   -156.52
REMARK 500    GLN A 172       76.54     53.78
REMARK 500    GLU A 214      -71.11    -63.44
REMARK 500    ASP A 262       55.92     70.09
REMARK 500    GLU A 284       47.48   -106.30
REMARK 500    ALA A 285      -10.88     69.42
REMARK 500    GLU A 316      -75.37    -54.84
REMARK 500    LYS A 318      -48.55   -131.13
REMARK 500    LEU A 327       57.69   -146.68
REMARK 500    ASN A 361       21.68    -75.72
REMARK 500    ILE A 364       91.48    -62.57
REMARK 500    PRO A 366       75.16    -61.87
REMARK 500    VAL A 374      134.24   -174.32
REMARK 500    GLN A 435      -80.89    -72.75
REMARK 500    TYR A 436        4.92    -66.52
REMARK 500    PRO A 438     -174.59    -67.37
REMARK 500    ASP A 458      -88.79    -65.79
REMARK 500    VAL A 459       53.20    -69.41
REMARK 500    HIS A 479       69.69   -150.79
REMARK 500    LYS A 508       39.83    -75.40
REMARK 500    ALA A 509       23.94   -159.28
REMARK 500    ASP B  46       32.05    -82.61
REMARK 500    TYR B  60     -168.44   -120.50
REMARK 500    PRO B  98       99.13    -41.13
REMARK 500    PRO B 114      109.72    -27.22
REMARK 500    ASP B 116      114.41   -160.48
REMARK 500    PRO B 134      151.38    -47.36
REMARK 500    ASP B 188       52.90   -160.05
REMARK 500    ASP B 262       81.63     57.49
REMARK 500    ARG B 278       11.51     80.44
REMARK 500    ASP B 336       87.54    -68.56
REMARK 500    ASP B 350       49.44    -92.41
REMARK 500    ALA B 362       38.49    -87.52
REMARK 500    ILE B 364       83.36    -64.80
REMARK 500    PRO B 366       77.91    -64.95
REMARK 500    ALA B 367       11.19    -66.50
REMARK 500    ILE B 372      -33.58   -130.44
REMARK 500    LEU B 403       48.02    -97.04
REMARK 500    ALA B 410       96.98    -49.57
REMARK 500    ALA B 416      -80.06    -82.69
REMARK 500    GLN B 443        3.56    -63.39
REMARK 500    LEU B 448      -71.82    -43.35
REMARK 500    PHE B 449      -73.80    -81.78
REMARK 500    ALA B 451      -85.35    -80.42
REMARK 500    TYR B 455      -84.74    -43.27
REMARK 500    VAL B 459      -61.28    -94.77
REMARK 500
REMARK 500 THIS ENTRY HAS     625 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLY A  135     VAL A  136                 -148.48
REMARK 500 GLU C  460     LEU C  461                 -140.11
REMARK 500 ASN C  493     ASP C  494                 -106.15
REMARK 500 ASP D   20     ALA D   21                   61.63
REMARK 500 LEU D  119     SER D  120                  145.27
REMARK 500 TYR E  331     PRO E  332                  144.37
REMARK 500 PRO E  346     LEU E  347                  139.69
REMARK 500 VAL E  348     VAL E  349                  146.22
REMARK 500 TYR E  444     MET E  445                  144.35
REMARK 500 TYR F  331     PRO F  332                  143.56
REMARK 500 LEU G  188     PRO G  189                   65.81
REMARK 500 PRO G  191     ALA G  192                  102.90
REMARK 500 ILE I  137     GLU I  138                  117.50
REMARK 500 GLU K  460     LEU K  461                 -140.09
REMARK 500 ASP L   20     ALA L   21                  139.19
REMARK 500 LEU L  119     SER L  120                  145.25
REMARK 500 TYR M  331     PRO M  332                  145.01
REMARK 500 TYR N  331     PRO N  332                  143.52
REMARK 500 LEU O  188     PRO O  189                   69.46
REMARK 500 PRO O  191     ALA O  192                  106.05
REMARK 500 GLU Q  138     ARG Q  139                 -121.35
REMARK 500 ILE R   94     LEU R   95                  118.98
REMARK 500 GLU S  460     LEU S  461                 -140.06
REMARK 500 ASN S  493     ASP S  494                 -118.72
REMARK 500 LEU T  119     SER T  120                  145.21
REMARK 500 TYR U  331     PRO U  332                  146.71
REMARK 500 TYR V  331     PRO V  332                  144.22
REMARK 500 LEU W  188     PRO W  189                   89.36
REMARK 500 PRO W  189     LEU W  190                 -132.05
REMARK 500 LEU W  190     PRO W  191                 -145.39
REMARK 500 PRO W  191     ALA W  192                   87.97
REMARK 500 ILE Y  137     GLU Y  138                   94.14
REMARK 500 ILE Z   94     LEU Z   95                 -145.87
REMARK 500 LEU Z   95     GLU Z   96                 -145.04
REMARK 500 GLU a  460     LEU a  461                 -140.07
REMARK 500 HIS b  110     ARG b  111                  118.90
REMARK 500 ALA b  113     PRO b  114                 -132.87
REMARK 500 SER b  115     TYR b  116                 -110.03
REMARK 500 GLU b  118     LEU b  119                 -145.40
REMARK 500 LEU b  119     SER b  120                  145.23
REMARK 500 TYR c  331     PRO c  332                  144.32
REMARK 500 TYR d  331     PRO d  332                  143.93
REMARK 500 LEU e  187     LEU e  188                  127.14
REMARK 500 LEU e  188     PRO e  189                   65.08
REMARK 500 PRO e  191     ALA e  192                   63.06
REMARK 500 SER e  193     ASP e  194                  148.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    ILE J  94        -11.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    GLN B 408        21.8      L          L   OUTSIDE RANGE
REMARK 500    TYR D 331        23.8      L          L   OUTSIDE RANGE
REMARK 500    TYR E 331        22.9      L          L   OUTSIDE RANGE
REMARK 500    TYR F 331        23.8      L          L   OUTSIDE RANGE
REMARK 500    GLU I 138         6.1      L          L   EXPECTING SP3
REMARK 500    ASP I 458        24.5      L          L   OUTSIDE RANGE
REMARK 500    GLN J 408        21.8      L          L   OUTSIDE RANGE
REMARK 500    TYR L 331        24.0      L          L   OUTSIDE RANGE
REMARK 500    TYR M 331        22.1      L          L   OUTSIDE RANGE
REMARK 500    TYR N 331        23.9      L          L   OUTSIDE RANGE
REMARK 500    GLN R 408        19.4      L          L   OUTSIDE RANGE
REMARK 500    TYR T 331        23.8      L          L   OUTSIDE RANGE
REMARK 500    TYR U 331        23.0      L          L   OUTSIDE RANGE
REMARK 500    TYR V 331        24.3      L          L   OUTSIDE RANGE
REMARK 500    ILE Y 137         4.6      L          L   EXPECTING SP3
REMARK 500    GLN Z 408        21.8      L          L   OUTSIDE RANGE
REMARK 500    TYR b 331        24.2      L          L   OUTSIDE RANGE
REMARK 500    TYR c 331        23.0      L          L   OUTSIDE RANGE
REMARK 500    TYR d 331        24.6      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG S 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP S 600   O2G
REMARK 620 2 THR S 176   OG1 155.7
REMARK 620 3 ANP S 600   O2B  77.8  81.6
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG a 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP a 600   O2G
REMARK 620 2 THR a 176   OG1 144.9
REMARK 620 3 ANP a 600   O2B  74.4  76.1
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG K 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR K 176   OG1
REMARK 620 2 ANP K 600   O2G 155.6
REMARK 620 3 ANP K 600   O2B  84.7  76.9
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG L 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SO4 L 630   O3
REMARK 620 2 THR L 156   OG1 157.1
REMARK 620 3 ADP L 600   O2B  64.6 104.3
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG Y 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP Y 600   O2G
REMARK 620 2 THR Y 176   OG1 118.4
REMARK 620 3 ANP Y 600   O2B  67.6  62.0
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG I 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR I 176   OG1
REMARK 620 2 ANP I 600   O2G 161.4
REMARK 620 3 ANP I 600   O2B  93.1  72.8
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP C 600   O2G
REMARK 620 2 THR C 176   OG1 153.5
REMARK 620 3 ANP C 600   O2B  73.0  80.7
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP A 600   O2G
REMARK 620 2 THR A 176   OG1 137.4
REMARK 620 3 ANP A 600   O2B  67.7  78.2
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG Q 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP Q 600   O2G
REMARK 620 2 THR Q 176   OG1 147.1
REMARK 620 3 ANP Q 600   O2B  71.5  78.8
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 176   OG1
REMARK 620 2 ANP B 600   O2G 164.2
REMARK 620 3 ANP B 600   O2B  64.1 100.2
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG T 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR T 156   OG1
REMARK 620 2 SO4 T 630   O3  152.8
REMARK 620 3 ADP T 600   O2B 102.2  66.9
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG J 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP J 600   O2G
REMARK 620 2 THR J 176   OG1 169.3
REMARK 620 3 ANP J 600   O2B 103.6  67.1
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG R 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP R 600   O2G
REMARK 620 2 THR R 176   OG1 169.0
REMARK 620 3 ANP R 600   O2B 103.6  66.9
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG D 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SO4 D 630   O3
REMARK 620 2 THR D 156   OG1 156.5
REMARK 620 3 ADP D 600   O2B  65.2 102.8
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG b 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR b 156   OG1
REMARK 620 2 SO4 b 630   O3  153.0
REMARK 620 3 ADP b 600   O2B 101.4  65.7
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG Z 601  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP Z 600   O2G
REMARK 620 2 ANP Z 600   O2B 103.4
REMARK 620 3 THR Z 176   OG1 169.4  66.8
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 630
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP I 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP J 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP K 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP L 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 630
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 M 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 N 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 O 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 P 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP Q 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP R 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP S 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG S 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP T 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 T 630
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 U 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 V 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 W 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP Y 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP Z 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP a 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG a 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP b 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG b 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 b 630
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 c 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 d 530
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CK3   RELATED DB: PDB
REMARK 900 BOVINE F1-ATPASE
REMARK 900 RELATED ID: 2HLD   RELATED DB: PDB
REMARK 900 YEAST F1-ATPASE
DBREF  3OAA A    1   513  UNP    C9QXA2   C9QXA2_ECOD1     1    513
DBREF  3OAA B    1   513  UNP    C9QXA2   C9QXA2_ECOD1     1    513
DBREF  3OAA C    1   513  UNP    C9QXA2   C9QXA2_ECOD1     1    513
DBREF  3OAA D    1   459  UNP    C9QXA4   C9QXA4_ECOD1     2    460
DBREF  3OAA E    1   459  UNP    C9QXA4   C9QXA4_ECOD1     2    460
DBREF  3OAA F    1   459  UNP    C9QXA4   C9QXA4_ECOD1     2    460
DBREF  3OAA G    1   286  UNP    C9QXA3   C9QXA3_ECOD1     2    287
DBREF  3OAA H    1   138  UNP    C9QXA5   C9QXA5_ECOD1     2    139
DBREF  3OAA I    1   513  UNP    C9QXA2   C9QXA2_ECOD1     1    513
DBREF  3OAA J    1   513  UNP    C9QXA2   C9QXA2_ECOD1     1    513
DBREF  3OAA K    1   513  UNP    C9QXA2   C9QXA2_ECOD1     1    513
DBREF  3OAA L    1   459  UNP    C9QXA4   C9QXA4_ECOD1     2    460
DBREF  3OAA M    1   459  UNP    C9QXA4   C9QXA4_ECOD1     2    460
DBREF  3OAA N    1   459  UNP    C9QXA4   C9QXA4_ECOD1     2    460
DBREF  3OAA O    1   286  UNP    C9QXA3   C9QXA3_ECOD1     2    287
DBREF  3OAA P    1   138  UNP    C9QXA5   C9QXA5_ECOD1     2    139
DBREF  3OAA Q    1   513  UNP    C9QXA2   C9QXA2_ECOD1     1    513
DBREF  3OAA R    1   513  UNP    C9QXA2   C9QXA2_ECOD1     1    513
DBREF  3OAA S    1   513  UNP    C9QXA2   C9QXA2_ECOD1     1    513
DBREF  3OAA T    1   459  UNP    C9QXA4   C9QXA4_ECOD1     2    460
DBREF  3OAA U    1   459  UNP    C9QXA4   C9QXA4_ECOD1     2    460
DBREF  3OAA V    1   459  UNP    C9QXA4   C9QXA4_ECOD1     2    460
DBREF  3OAA W    1   286  UNP    C9QXA3   C9QXA3_ECOD1     2    287
DBREF  3OAA X    1   138  UNP    C9QXA5   C9QXA5_ECOD1     2    139
DBREF  3OAA Y    1   513  UNP    C9QXA2   C9QXA2_ECOD1     1    513
DBREF  3OAA Z    1   513  UNP    C9QXA2   C9QXA2_ECOD1     1    513
DBREF  3OAA a    1   513  UNP    C9QXA2   C9QXA2_ECOD1     1    513
DBREF  3OAA b    1   459  UNP    C9QXA4   C9QXA4_ECOD1     2    460
DBREF  3OAA c    1   459  UNP    C9QXA4   C9QXA4_ECOD1     2    460
DBREF  3OAA d    1   459  UNP    C9QXA4   C9QXA4_ECOD1     2    460
DBREF  3OAA e    1   286  UNP    C9QXA3   C9QXA3_ECOD1     2    287
DBREF  3OAA f    1   138  UNP    C9QXA5   C9QXA5_ECOD1     2    139
SEQADV 3OAA GLU D   81  UNP  C9QXA4    LYS    82 ENGINEERED MUTATION
SEQADV 3OAA GLU E   81  UNP  C9QXA4    LYS    82 ENGINEERED MUTATION
SEQADV 3OAA GLU F   81  UNP  C9QXA4    LYS    82 ENGINEERED MUTATION
SEQADV 3OAA GLU L   81  UNP  C9QXA4    LYS    82 ENGINEERED MUTATION
SEQADV 3OAA GLU M   81  UNP  C9QXA4    LYS    82 ENGINEERED MUTATION
SEQADV 3OAA GLU N   81  UNP  C9QXA4    LYS    82 ENGINEERED MUTATION
SEQADV 3OAA GLU T   81  UNP  C9QXA4    LYS    82 ENGINEERED MUTATION
SEQADV 3OAA GLU U   81  UNP  C9QXA4    LYS    82 ENGINEERED MUTATION
SEQADV 3OAA GLU V   81  UNP  C9QXA4    LYS    82 ENGINEERED MUTATION
SEQADV 3OAA GLU b   81  UNP  C9QXA4    LYS    82 ENGINEERED MUTATION
SEQADV 3OAA GLU c   81  UNP  C9QXA4    LYS    82 ENGINEERED MUTATION
SEQADV 3OAA GLU d   81  UNP  C9QXA4    LYS    82 ENGINEERED MUTATION
SEQRES   1 A  513  MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES   2 A  513  GLN ARG ILE ALA GLN PHE ASN VAL VAL SER GLU ALA HIS
SEQRES   3 A  513  ASN GLU GLY THR ILE VAL SER VAL SER ASP GLY VAL ILE
SEQRES   4 A  513  ARG ILE HIS GLY LEU ALA ASP CYS MET GLN GLY GLU MET
SEQRES   5 A  513  ILE SER LEU PRO GLY ASN ARG TYR ALA ILE ALA LEU ASN
SEQRES   6 A  513  LEU GLU ARG ASP SER VAL GLY ALA VAL VAL MET GLY PRO
SEQRES   7 A  513  TYR ALA ASP LEU ALA GLU GLY MET LYS VAL LYS CYS THR
SEQRES   8 A  513  GLY ARG ILE LEU GLU VAL PRO VAL GLY ARG GLY LEU LEU
SEQRES   9 A  513  GLY ARG VAL VAL ASN THR LEU GLY ALA PRO ILE ASP GLY
SEQRES  10 A  513  LYS GLY PRO LEU ASP HIS ASP GLY PHE SER ALA VAL GLU
SEQRES  11 A  513  ALA ILE ALA PRO GLY VAL ILE GLU ARG GLN SER VAL ASP
SEQRES  12 A  513  GLN PRO VAL GLN THR GLY TYR LYS ALA VAL ASP SER MET
SEQRES  13 A  513  ILE PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES  14 A  513  ASP ARG GLN THR GLY LYS THR ALA LEU ALA ILE ASP ALA
SEQRES  15 A  513  ILE ILE ASN GLN ARG ASP SER GLY ILE LYS CYS ILE TYR
SEQRES  16 A  513  VAL ALA ILE GLY GLN LYS ALA SER THR ILE SER ASN VAL
SEQRES  17 A  513  VAL ARG LYS LEU GLU GLU HIS GLY ALA LEU ALA ASN THR
SEQRES  18 A  513  ILE VAL VAL VAL ALA THR ALA SER GLU SER ALA ALA LEU
SEQRES  19 A  513  GLN TYR LEU ALA PRO TYR ALA GLY CYS ALA MET GLY GLU
SEQRES  20 A  513  TYR PHE ARG ASP ARG GLY GLU ASP ALA LEU ILE ILE TYR
SEQRES  21 A  513  ASP ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN ILE
SEQRES  22 A  513  SER LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA PHE
SEQRES  23 A  513  PRO GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU
SEQRES  24 A  513  ARG ALA ALA ARG VAL ASN ALA GLU TYR VAL GLU ALA PHE
SEQRES  25 A  513  THR LYS GLY GLU VAL LYS GLY LYS THR GLY SER LEU THR
SEQRES  26 A  513  ALA LEU PRO ILE ILE GLU THR GLN ALA GLY ASP VAL SER
SEQRES  27 A  513  ALA PHE VAL PRO THR ASN VAL ILE SER ILE THR ASP GLY
SEQRES  28 A  513  GLN ILE PHE LEU GLU THR ASN LEU PHE ASN ALA GLY ILE
SEQRES  29 A  513  ARG PRO ALA VAL ASN PRO GLY ILE SER VAL SER ARG VAL
SEQRES  30 A  513  GLY GLY ALA ALA GLN THR LYS ILE MET LYS LYS LEU SER
SEQRES  31 A  513  GLY GLY ILE ARG THR ALA LEU ALA GLN TYR ARG GLU LEU
SEQRES  32 A  513  ALA ALA PHE SER GLN PHE ALA SER ASP LEU ASP ASP ALA
SEQRES  33 A  513  THR ARG LYS GLN LEU ASP HIS GLY GLN LYS VAL THR GLU
SEQRES  34 A  513  LEU LEU LYS GLN LYS GLN TYR ALA PRO MET SER VAL ALA
SEQRES  35 A  513  GLN GLN SER LEU VAL LEU PHE ALA ALA GLU ARG GLY TYR
SEQRES  36 A  513  LEU ALA ASP VAL GLU LEU SER LYS ILE GLY SER PHE GLU
SEQRES  37 A  513  ALA ALA LEU LEU ALA TYR VAL ASP ARG ASP HIS ALA PRO
SEQRES  38 A  513  LEU MET GLN GLU ILE ASN GLN THR GLY GLY TYR ASN ASP
SEQRES  39 A  513  GLU ILE GLU GLY LYS LEU LYS GLY ILE LEU ASP SER PHE
SEQRES  40 A  513  LYS ALA THR GLN SER TRP
SEQRES   1 B  513  MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES   2 B  513  GLN ARG ILE ALA GLN PHE ASN VAL VAL SER GLU ALA HIS
SEQRES   3 B  513  ASN GLU GLY THR ILE VAL SER VAL SER ASP GLY VAL ILE
SEQRES   4 B  513  ARG ILE HIS GLY LEU ALA ASP CYS MET GLN GLY GLU MET
SEQRES   5 B  513  ILE SER LEU PRO GLY ASN ARG TYR ALA ILE ALA LEU ASN
SEQRES   6 B  513  LEU GLU ARG ASP SER VAL GLY ALA VAL VAL MET GLY PRO
SEQRES   7 B  513  TYR ALA ASP LEU ALA GLU GLY MET LYS VAL LYS CYS THR
SEQRES   8 B  513  GLY ARG ILE LEU GLU VAL PRO VAL GLY ARG GLY LEU LEU
SEQRES   9 B  513  GLY ARG VAL VAL ASN THR LEU GLY ALA PRO ILE ASP GLY
SEQRES  10 B  513  LYS GLY PRO LEU ASP HIS ASP GLY PHE SER ALA VAL GLU
SEQRES  11 B  513  ALA ILE ALA PRO GLY VAL ILE GLU ARG GLN SER VAL ASP
SEQRES  12 B  513  GLN PRO VAL GLN THR GLY TYR LYS ALA VAL ASP SER MET
SEQRES  13 B  513  ILE PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES  14 B  513  ASP ARG GLN THR GLY LYS THR ALA LEU ALA ILE ASP ALA
SEQRES  15 B  513  ILE ILE ASN GLN ARG ASP SER GLY ILE LYS CYS ILE TYR
SEQRES  16 B  513  VAL ALA ILE GLY GLN LYS ALA SER THR ILE SER ASN VAL
SEQRES  17 B  513  VAL ARG LYS LEU GLU GLU HIS GLY ALA LEU ALA ASN THR
SEQRES  18 B  513  ILE VAL VAL VAL ALA THR ALA SER GLU SER ALA ALA LEU
SEQRES  19 B  513  GLN TYR LEU ALA PRO TYR ALA GLY CYS ALA MET GLY GLU
SEQRES  20 B  513  TYR PHE ARG ASP ARG GLY GLU ASP ALA LEU ILE ILE TYR
SEQRES  21 B  513  ASP ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN ILE
SEQRES  22 B  513  SER LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA PHE
SEQRES  23 B  513  PRO GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU
SEQRES  24 B  513  ARG ALA ALA ARG VAL ASN ALA GLU TYR VAL GLU ALA PHE
SEQRES  25 B  513  THR LYS GLY GLU VAL LYS GLY LYS THR GLY SER LEU THR
SEQRES  26 B  513  ALA LEU PRO ILE ILE GLU THR GLN ALA GLY ASP VAL SER
SEQRES  27 B  513  ALA PHE VAL PRO THR ASN VAL ILE SER ILE THR ASP GLY
SEQRES  28 B  513  GLN ILE PHE LEU GLU THR ASN LEU PHE ASN ALA GLY ILE
SEQRES  29 B  513  ARG PRO ALA VAL ASN PRO GLY ILE SER VAL SER ARG VAL
SEQRES  30 B  513  GLY GLY ALA ALA GLN THR LYS ILE MET LYS LYS LEU SER
SEQRES  31 B  513  GLY GLY ILE ARG THR ALA LEU ALA GLN TYR ARG GLU LEU
SEQRES  32 B  513  ALA ALA PHE SER GLN PHE ALA SER ASP LEU ASP ASP ALA
SEQRES  33 B  513  THR ARG LYS GLN LEU ASP HIS GLY GLN LYS VAL THR GLU
SEQRES  34 B  513  LEU LEU LYS GLN LYS GLN TYR ALA PRO MET SER VAL ALA
SEQRES  35 B  513  GLN GLN SER LEU VAL LEU PHE ALA ALA GLU ARG GLY TYR
SEQRES  36 B  513  LEU ALA ASP VAL GLU LEU SER LYS ILE GLY SER PHE GLU
SEQRES  37 B  513  ALA ALA LEU LEU ALA TYR VAL ASP ARG ASP HIS ALA PRO
SEQRES  38 B  513  LEU MET GLN GLU ILE ASN GLN THR GLY GLY TYR ASN ASP
SEQRES  39 B  513  GLU ILE GLU GLY LYS LEU LYS GLY ILE LEU ASP SER PHE
SEQRES  40 B  513  LYS ALA THR GLN SER TRP
SEQRES   1 C  513  MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES   2 C  513  GLN ARG ILE ALA GLN PHE ASN VAL VAL SER GLU ALA HIS
SEQRES   3 C  513  ASN GLU GLY THR ILE VAL SER VAL SER ASP GLY VAL ILE
SEQRES   4 C  513  ARG ILE HIS GLY LEU ALA ASP CYS MET GLN GLY GLU MET
SEQRES   5 C  513  ILE SER LEU PRO GLY ASN ARG TYR ALA ILE ALA LEU ASN
SEQRES   6 C  513  LEU GLU ARG ASP SER VAL GLY ALA VAL VAL MET GLY PRO
SEQRES   7 C  513  TYR ALA ASP LEU ALA GLU GLY MET LYS VAL LYS CYS THR
SEQRES   8 C  513  GLY ARG ILE LEU GLU VAL PRO VAL GLY ARG GLY LEU LEU
SEQRES   9 C  513  GLY ARG VAL VAL ASN THR LEU GLY ALA PRO ILE ASP GLY
SEQRES  10 C  513  LYS GLY PRO LEU ASP HIS ASP GLY PHE SER ALA VAL GLU
SEQRES  11 C  513  ALA ILE ALA PRO GLY VAL ILE GLU ARG GLN SER VAL ASP
SEQRES  12 C  513  GLN PRO VAL GLN THR GLY TYR LYS ALA VAL ASP SER MET
SEQRES  13 C  513  ILE PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES  14 C  513  ASP ARG GLN THR GLY LYS THR ALA LEU ALA ILE ASP ALA
SEQRES  15 C  513  ILE ILE ASN GLN ARG ASP SER GLY ILE LYS CYS ILE TYR
SEQRES  16 C  513  VAL ALA ILE GLY GLN LYS ALA SER THR ILE SER ASN VAL
SEQRES  17 C  513  VAL ARG LYS LEU GLU GLU HIS GLY ALA LEU ALA ASN THR
SEQRES  18 C  513  ILE VAL VAL VAL ALA THR ALA SER GLU SER ALA ALA LEU
SEQRES  19 C  513  GLN TYR LEU ALA PRO TYR ALA GLY CYS ALA MET GLY GLU
SEQRES  20 C  513  TYR PHE ARG ASP ARG GLY GLU ASP ALA LEU ILE ILE TYR
SEQRES  21 C  513  ASP ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN ILE
SEQRES  22 C  513  SER LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA PHE
SEQRES  23 C  513  PRO GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU
SEQRES  24 C  513  ARG ALA ALA ARG VAL ASN ALA GLU TYR VAL GLU ALA PHE
SEQRES  25 C  513  THR LYS GLY GLU VAL LYS GLY LYS THR GLY SER LEU THR
SEQRES  26 C  513  ALA LEU PRO ILE ILE GLU THR GLN ALA GLY ASP VAL SER
SEQRES  27 C  513  ALA PHE VAL PRO THR ASN VAL ILE SER ILE THR ASP GLY
SEQRES  28 C  513  GLN ILE PHE LEU GLU THR ASN LEU PHE ASN ALA GLY ILE
SEQRES  29 C  513  ARG PRO ALA VAL ASN PRO GLY ILE SER VAL SER ARG VAL
SEQRES  30 C  513  GLY GLY ALA ALA GLN THR LYS ILE MET LYS LYS LEU SER
SEQRES  31 C  513  GLY GLY ILE ARG THR ALA LEU ALA GLN TYR ARG GLU LEU
SEQRES  32 C  513  ALA ALA PHE SER GLN PHE ALA SER ASP LEU ASP ASP ALA
SEQRES  33 C  513  THR ARG LYS GLN LEU ASP HIS GLY GLN LYS VAL THR GLU
SEQRES  34 C  513  LEU LEU LYS GLN LYS GLN TYR ALA PRO MET SER VAL ALA
SEQRES  35 C  513  GLN GLN SER LEU VAL LEU PHE ALA ALA GLU ARG GLY TYR
SEQRES  36 C  513  LEU ALA ASP VAL GLU LEU SER LYS ILE GLY SER PHE GLU
SEQRES  37 C  513  ALA ALA LEU LEU ALA TYR VAL ASP ARG ASP HIS ALA PRO
SEQRES  38 C  513  LEU MET GLN GLU ILE ASN GLN THR GLY GLY TYR ASN ASP
SEQRES  39 C  513  GLU ILE GLU GLY LYS LEU LYS GLY ILE LEU ASP SER PHE
SEQRES  40 C  513  LYS ALA THR GLN SER TRP
SEQRES   1 D  459  ALA THR GLY LYS ILE VAL GLN VAL ILE GLY ALA VAL VAL
SEQRES   2 D  459  ASP VAL GLU PHE PRO GLN ASP ALA VAL PRO ARG VAL TYR
SEQRES   3 D  459  ASP ALA LEU GLU VAL GLN ASN GLY ASN GLU ARG LEU VAL
SEQRES   4 D  459  LEU GLU VAL GLN GLN GLN LEU GLY GLY GLY ILE VAL ARG
SEQRES   5 D  459  THR ILE ALA MET GLY SER SER ASP GLY LEU ARG ARG GLY
SEQRES   6 D  459  LEU ASP VAL LYS ASP LEU GLU HIS PRO ILE GLU VAL PRO
SEQRES   7 D  459  VAL GLY GLU ALA THR LEU GLY ARG ILE MET ASN VAL LEU
SEQRES   8 D  459  GLY GLU PRO VAL ASP MET LYS GLY GLU ILE GLY GLU GLU
SEQRES   9 D  459  GLU ARG TRP ALA ILE HIS ARG ALA ALA PRO SER TYR GLU
SEQRES  10 D  459  GLU LEU SER ASN SER GLN GLU LEU LEU GLU THR GLY ILE
SEQRES  11 D  459  LYS VAL ILE ASP LEU MET CYS PRO PHE ALA LYS GLY GLY
SEQRES  12 D  459  LYS VAL GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR
SEQRES  13 D  459  VAL ASN MET MET GLU LEU ILE ARG ASN ILE ALA ILE GLU
SEQRES  14 D  459  HIS SER GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG
SEQRES  15 D  459  THR ARG GLU GLY ASN ASP PHE TYR HIS GLU MET THR ASP
SEQRES  16 D  459  SER ASN VAL ILE ASP LYS VAL SER LEU VAL TYR GLY GLN
SEQRES  17 D  459  MET ASN GLU PRO PRO GLY ASN ARG LEU ARG VAL ALA LEU
SEQRES  18 D  459  THR GLY LEU THR MET ALA GLU LYS PHE ARG ASP GLU GLY
SEQRES  19 D  459  ARG ASP VAL LEU LEU PHE VAL ASP ASN ILE TYR ARG TYR
SEQRES  20 D  459  THR LEU ALA GLY THR GLU VAL SER ALA LEU LEU GLY ARG
SEQRES  21 D  459  MET PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA GLU
SEQRES  22 D  459  GLU MET GLY VAL LEU GLN GLU ARG ILE THR SER THR LYS
SEQRES  23 D  459  THR GLY SER ILE THR SER VAL GLN ALA VAL TYR VAL PRO
SEQRES  24 D  459  ALA ASP ASP LEU THR ASP PRO SER PRO ALA THR THR PHE
SEQRES  25 D  459  ALA HIS LEU ASP ALA THR VAL VAL LEU SER ARG GLN ILE
SEQRES  26 D  459  ALA SER LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP
SEQRES  27 D  459  SER THR SER ARG GLN LEU ASP PRO LEU VAL VAL GLY GLN
SEQRES  28 D  459  GLU HIS TYR ASP THR ALA ARG GLY VAL GLN SER ILE LEU
SEQRES  29 D  459  GLN ARG TYR GLN GLU LEU LYS ASP ILE ILE ALA ILE LEU
SEQRES  30 D  459  GLY MET ASP GLU LEU SER GLU GLU ASP LYS LEU VAL VAL
SEQRES  31 D  459  ALA ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO
SEQRES  32 D  459  PHE PHE VAL ALA GLU VAL PHE THR GLY SER PRO GLY LYS
SEQRES  33 D  459  TYR VAL SER LEU LYS ASP THR ILE ARG GLY PHE LYS GLY
SEQRES  34 D  459  ILE MET GLU GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA
SEQRES  35 D  459  PHE TYR MET VAL GLY SER ILE GLU GLU ALA VAL GLU LYS
SEQRES  36 D  459  ALA LYS LYS LEU
SEQRES   1 E  459  ALA THR GLY LYS ILE VAL GLN VAL ILE GLY ALA VAL VAL
SEQRES   2 E  459  ASP VAL GLU PHE PRO GLN ASP ALA VAL PRO ARG VAL TYR
SEQRES   3 E  459  ASP ALA LEU GLU VAL GLN ASN GLY ASN GLU ARG LEU VAL
SEQRES   4 E  459  LEU GLU VAL GLN GLN GLN LEU GLY GLY GLY ILE VAL ARG
SEQRES   5 E  459  THR ILE ALA MET GLY SER SER ASP GLY LEU ARG ARG GLY
SEQRES   6 E  459  LEU ASP VAL LYS ASP LEU GLU HIS PRO ILE GLU VAL PRO
SEQRES   7 E  459  VAL GLY GLU ALA THR LEU GLY ARG ILE MET ASN VAL LEU
SEQRES   8 E  459  GLY GLU PRO VAL ASP MET LYS GLY GLU ILE GLY GLU GLU
SEQRES   9 E  459  GLU ARG TRP ALA ILE HIS ARG ALA ALA PRO SER TYR GLU
SEQRES  10 E  459  GLU LEU SER ASN SER GLN GLU LEU LEU GLU THR GLY ILE
SEQRES  11 E  459  LYS VAL ILE ASP LEU MET CYS PRO PHE ALA LYS GLY GLY
SEQRES  12 E  459  LYS VAL GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR
SEQRES  13 E  459  VAL ASN MET MET GLU LEU ILE ARG ASN ILE ALA ILE GLU
SEQRES  14 E  459  HIS SER GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG
SEQRES  15 E  459  THR ARG GLU GLY ASN ASP PHE TYR HIS GLU MET THR ASP
SEQRES  16 E  459  SER ASN VAL ILE ASP LYS VAL SER LEU VAL TYR GLY GLN
SEQRES  17 E  459  MET ASN GLU PRO PRO GLY ASN ARG LEU ARG VAL ALA LEU
SEQRES  18 E  459  THR GLY LEU THR MET ALA GLU LYS PHE ARG ASP GLU GLY
SEQRES  19 E  459  ARG ASP VAL LEU LEU PHE VAL ASP ASN ILE TYR ARG TYR
SEQRES  20 E  459  THR LEU ALA GLY THR GLU VAL SER ALA LEU LEU GLY ARG
SEQRES  21 E  459  MET PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA GLU
SEQRES  22 E  459  GLU MET GLY VAL LEU GLN GLU ARG ILE THR SER THR LYS
SEQRES  23 E  459  THR GLY SER ILE THR SER VAL GLN ALA VAL TYR VAL PRO
SEQRES  24 E  459  ALA ASP ASP LEU THR ASP PRO SER PRO ALA THR THR PHE
SEQRES  25 E  459  ALA HIS LEU ASP ALA THR VAL VAL LEU SER ARG GLN ILE
SEQRES  26 E  459  ALA SER LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP
SEQRES  27 E  459  SER THR SER ARG GLN LEU ASP PRO LEU VAL VAL GLY GLN
SEQRES  28 E  459  GLU HIS TYR ASP THR ALA ARG GLY VAL GLN SER ILE LEU
SEQRES  29 E  459  GLN ARG TYR GLN GLU LEU LYS ASP ILE ILE ALA ILE LEU
SEQRES  30 E  459  GLY MET ASP GLU LEU SER GLU GLU ASP LYS LEU VAL VAL
SEQRES  31 E  459  ALA ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO
SEQRES  32 E  459  PHE PHE VAL ALA GLU VAL PHE THR GLY SER PRO GLY LYS
SEQRES  33 E  459  TYR VAL SER LEU LYS ASP THR ILE ARG GLY PHE LYS GLY
SEQRES  34 E  459  ILE MET GLU GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA
SEQRES  35 E  459  PHE TYR MET VAL GLY SER ILE GLU GLU ALA VAL GLU LYS
SEQRES  36 E  459  ALA LYS LYS LEU
SEQRES   1 F  459  ALA THR GLY LYS ILE VAL GLN VAL ILE GLY ALA VAL VAL
SEQRES   2 F  459  ASP VAL GLU PHE PRO GLN ASP ALA VAL PRO ARG VAL TYR
SEQRES   3 F  459  ASP ALA LEU GLU VAL GLN ASN GLY ASN GLU ARG LEU VAL
SEQRES   4 F  459  LEU GLU VAL GLN GLN GLN LEU GLY GLY GLY ILE VAL ARG
SEQRES   5 F  459  THR ILE ALA MET GLY SER SER ASP GLY LEU ARG ARG GLY
SEQRES   6 F  459  LEU ASP VAL LYS ASP LEU GLU HIS PRO ILE GLU VAL PRO
SEQRES   7 F  459  VAL GLY GLU ALA THR LEU GLY ARG ILE MET ASN VAL LEU
SEQRES   8 F  459  GLY GLU PRO VAL ASP MET LYS GLY GLU ILE GLY GLU GLU
SEQRES   9 F  459  GLU ARG TRP ALA ILE HIS ARG ALA ALA PRO SER TYR GLU
SEQRES  10 F  459  GLU LEU SER ASN SER GLN GLU LEU LEU GLU THR GLY ILE
SEQRES  11 F  459  LYS VAL ILE ASP LEU MET CYS PRO PHE ALA LYS GLY GLY
SEQRES  12 F  459  LYS VAL GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR
SEQRES  13 F  459  VAL ASN MET MET GLU LEU ILE ARG ASN ILE ALA ILE GLU
SEQRES  14 F  459  HIS SER GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG
SEQRES  15 F  459  THR ARG GLU GLY ASN ASP PHE TYR HIS GLU MET THR ASP
SEQRES  16 F  459  SER ASN VAL ILE ASP LYS VAL SER LEU VAL TYR GLY GLN
SEQRES  17 F  459  MET ASN GLU PRO PRO GLY ASN ARG LEU ARG VAL ALA LEU
SEQRES  18 F  459  THR GLY LEU THR MET ALA GLU LYS PHE ARG ASP GLU GLY
SEQRES  19 F  459  ARG ASP VAL LEU LEU PHE VAL ASP ASN ILE TYR ARG TYR
SEQRES  20 F  459  THR LEU ALA GLY THR GLU VAL SER ALA LEU LEU GLY ARG
SEQRES  21 F  459  MET PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA GLU
SEQRES  22 F  459  GLU MET GLY VAL LEU GLN GLU ARG ILE THR SER THR LYS
SEQRES  23 F  459  THR GLY SER ILE THR SER VAL GLN ALA VAL TYR VAL PRO
SEQRES  24 F  459  ALA ASP ASP LEU THR ASP PRO SER PRO ALA THR THR PHE
SEQRES  25 F  459  ALA HIS LEU ASP ALA THR VAL VAL LEU SER ARG GLN ILE
SEQRES  26 F  459  ALA SER LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP
SEQRES  27 F  459  SER THR SER ARG GLN LEU ASP PRO LEU VAL VAL GLY GLN
SEQRES  28 F  459  GLU HIS TYR ASP THR ALA ARG GLY VAL GLN SER ILE LEU
SEQRES  29 F  459  GLN ARG TYR GLN GLU LEU LYS ASP ILE ILE ALA ILE LEU
SEQRES  30 F  459  GLY MET ASP GLU LEU SER GLU GLU ASP LYS LEU VAL VAL
SEQRES  31 F  459  ALA ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO
SEQRES  32 F  459  PHE PHE VAL ALA GLU VAL PHE THR GLY SER PRO GLY LYS
SEQRES  33 F  459  TYR VAL SER LEU LYS ASP THR ILE ARG GLY PHE LYS GLY
SEQRES  34 F  459  ILE MET GLU GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA
SEQRES  35 F  459  PHE TYR MET VAL GLY SER ILE GLU GLU ALA VAL GLU LYS
SEQRES  36 F  459  ALA LYS LYS LEU
SEQRES   1 G  286  ALA GLY ALA LYS GLU ILE ARG SER LYS ILE ALA SER VAL
SEQRES   2 G  286  GLN ASN THR GLN LYS ILE THR LYS ALA MET GLU MET VAL
SEQRES   3 G  286  ALA ALA SER LYS MET ARG LYS SER GLN ASP ARG MET ALA
SEQRES   4 G  286  ALA SER ARG PRO TYR ALA GLU THR MET ARG LYS VAL ILE
SEQRES   5 G  286  GLY HIS LEU ALA HIS GLY ASN LEU GLU TYR LYS HIS PRO
SEQRES   6 G  286  TYR LEU GLU ASP ARG ASP VAL LYS ARG VAL GLY TYR LEU
SEQRES   7 G  286  VAL VAL SER THR ASP ARG GLY LEU CYS GLY GLY LEU ASN
SEQRES   8 G  286  ILE ASN LEU PHE LYS LYS LEU LEU ALA GLU MET LYS THR
SEQRES   9 G  286  TRP THR ASP LYS GLY VAL GLN CYS ASP LEU ALA MET ILE
SEQRES  10 G  286  GLY SER LYS GLY VAL SER PHE PHE ASN SER VAL GLY GLY
SEQRES  11 G  286  ASN VAL VAL ALA GLN VAL THR GLY MET GLY ASP ASN PRO
SEQRES  12 G  286  SER LEU SER GLU LEU ILE GLY PRO VAL LYS VAL MET LEU
SEQRES  13 G  286  GLN ALA TYR ASP GLU GLY ARG LEU ASP LYS LEU TYR ILE
SEQRES  14 G  286  VAL SER ASN LYS PHE ILE ASN THR MET SER GLN VAL PRO
SEQRES  15 G  286  THR ILE SER GLN LEU LEU PRO LEU PRO ALA SER ASP ASP
SEQRES  16 G  286  ASP ASP LEU LYS HIS LYS SER TRP ASP TYR LEU TYR GLU
SEQRES  17 G  286  PRO ASP PRO LYS ALA LEU LEU ASP THR LEU LEU ARG ARG
SEQRES  18 G  286  TYR VAL GLU SER GLN VAL TYR GLN GLY VAL VAL GLU ASN
SEQRES  19 G  286  LEU ALA SER GLU GLN ALA ALA ARG MET VAL ALA MET LYS
SEQRES  20 G  286  ALA ALA THR ASP ASN GLY GLY SER LEU ILE LYS GLU LEU
SEQRES  21 G  286  GLN LEU VAL TYR ASN LYS ALA ARG GLN ALA SER ILE THR
SEQRES  22 G  286  GLN GLU LEU THR GLU ILE VAL SER GLY ALA ALA ALA VAL
SEQRES   1 H  138  ALA MET THR TYR HIS LEU ASP VAL VAL SER ALA GLU GLN
SEQRES   2 H  138  GLN MET PHE SER GLY LEU VAL GLU LYS ILE GLN VAL THR
SEQRES   3 H  138  GLY SER GLU GLY GLU LEU GLY ILE TYR PRO GLY HIS ALA
SEQRES   4 H  138  PRO LEU LEU THR ALA ILE LYS PRO GLY MET ILE ARG ILE
SEQRES   5 H  138  VAL LYS GLN HIS GLY HIS GLU GLU PHE ILE TYR LEU SER
SEQRES   6 H  138  GLY GLY ILE LEU GLU VAL GLN PRO GLY ASN VAL THR VAL
SEQRES   7 H  138  LEU ALA ASP THR ALA ILE ARG GLY GLN ASP LEU ASP GLU
SEQRES   8 H  138  ALA ARG ALA MET GLU ALA LYS ARG LYS ALA GLU GLU HIS
SEQRES   9 H  138  ILE SER SER SER HIS GLY ASP VAL ASP TYR ALA GLN ALA
SEQRES  10 H  138  SER ALA GLU LEU ALA LYS ALA ILE ALA GLN LEU ARG VAL
SEQRES  11 H  138  ILE GLU LEU THR LYS LYS ALA MET
SEQRES   1 I  513  MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES   2 I  513  GLN ARG ILE ALA GLN PHE ASN VAL VAL SER GLU ALA HIS
SEQRES   3 I  513  ASN GLU GLY THR ILE VAL SER VAL SER ASP GLY VAL ILE
SEQRES   4 I  513  ARG ILE HIS GLY LEU ALA ASP CYS MET GLN GLY GLU MET
SEQRES   5 I  513  ILE SER LEU PRO GLY ASN ARG TYR ALA ILE ALA LEU ASN
SEQRES   6 I  513  LEU GLU ARG ASP SER VAL GLY ALA VAL VAL MET GLY PRO
SEQRES   7 I  513  TYR ALA ASP LEU ALA GLU GLY MET LYS VAL LYS CYS THR
SEQRES   8 I  513  GLY ARG ILE LEU GLU VAL PRO VAL GLY ARG GLY LEU LEU
SEQRES   9 I  513  GLY ARG VAL VAL ASN THR LEU GLY ALA PRO ILE ASP GLY
SEQRES  10 I  513  LYS GLY PRO LEU ASP HIS ASP GLY PHE SER ALA VAL GLU
SEQRES  11 I  513  ALA ILE ALA PRO GLY VAL ILE GLU ARG GLN SER VAL ASP
SEQRES  12 I  513  GLN PRO VAL GLN THR GLY TYR LYS ALA VAL ASP SER MET
SEQRES  13 I  513  ILE PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES  14 I  513  ASP ARG GLN THR GLY LYS THR ALA LEU ALA ILE ASP ALA
SEQRES  15 I  513  ILE ILE ASN GLN ARG ASP SER GLY ILE LYS CYS ILE TYR
SEQRES  16 I  513  VAL ALA ILE GLY GLN LYS ALA SER THR ILE SER ASN VAL
SEQRES  17 I  513  VAL ARG LYS LEU GLU GLU HIS GLY ALA LEU ALA ASN THR
SEQRES  18 I  513  ILE VAL VAL VAL ALA THR ALA SER GLU SER ALA ALA LEU
SEQRES  19 I  513  GLN TYR LEU ALA PRO TYR ALA GLY CYS ALA MET GLY GLU
SEQRES  20 I  513  TYR PHE ARG ASP ARG GLY GLU ASP ALA LEU ILE ILE TYR
SEQRES  21 I  513  ASP ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN ILE
SEQRES  22 I  513  SER LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA PHE
SEQRES  23 I  513  PRO GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU
SEQRES  24 I  513  ARG ALA ALA ARG VAL ASN ALA GLU TYR VAL GLU ALA PHE
SEQRES  25 I  513  THR LYS GLY GLU VAL LYS GLY LYS THR GLY SER LEU THR
SEQRES  26 I  513  ALA LEU PRO ILE ILE GLU THR GLN ALA GLY ASP VAL SER
SEQRES  27 I  513  ALA PHE VAL PRO THR ASN VAL ILE SER ILE THR ASP GLY
SEQRES  28 I  513  GLN ILE PHE LEU GLU THR ASN LEU PHE ASN ALA GLY ILE
SEQRES  29 I  513  ARG PRO ALA VAL ASN PRO GLY ILE SER VAL SER ARG VAL
SEQRES  30 I  513  GLY GLY ALA ALA GLN THR LYS ILE MET LYS LYS LEU SER
SEQRES  31 I  513  GLY GLY ILE ARG THR ALA LEU ALA GLN TYR ARG GLU LEU
SEQRES  32 I  513  ALA ALA PHE SER GLN PHE ALA SER ASP LEU ASP ASP ALA
SEQRES  33 I  513  THR ARG LYS GLN LEU ASP HIS GLY GLN LYS VAL THR GLU
SEQRES  34 I  513  LEU LEU LYS GLN LYS GLN TYR ALA PRO MET SER VAL ALA
SEQRES  35 I  513  GLN GLN SER LEU VAL LEU PHE ALA ALA GLU ARG GLY TYR
SEQRES  36 I  513  LEU ALA ASP VAL GLU LEU SER LYS ILE GLY SER PHE GLU
SEQRES  37 I  513  ALA ALA LEU LEU ALA TYR VAL ASP ARG ASP HIS ALA PRO
SEQRES  38 I  513  LEU MET GLN GLU ILE ASN GLN THR GLY GLY TYR ASN ASP
SEQRES  39 I  513  GLU ILE GLU GLY LYS LEU LYS GLY ILE LEU ASP SER PHE
SEQRES  40 I  513  LYS ALA THR GLN SER TRP
SEQRES   1 J  513  MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES   2 J  513  GLN ARG ILE ALA GLN PHE ASN VAL VAL SER GLU ALA HIS
SEQRES   3 J  513  ASN GLU GLY THR ILE VAL SER VAL SER ASP GLY VAL ILE
SEQRES   4 J  513  ARG ILE HIS GLY LEU ALA ASP CYS MET GLN GLY GLU MET
SEQRES   5 J  513  ILE SER LEU PRO GLY ASN ARG TYR ALA ILE ALA LEU ASN
SEQRES   6 J  513  LEU GLU ARG ASP SER VAL GLY ALA VAL VAL MET GLY PRO
SEQRES   7 J  513  TYR ALA ASP LEU ALA GLU GLY MET LYS VAL LYS CYS THR
SEQRES   8 J  513  GLY ARG ILE LEU GLU VAL PRO VAL GLY ARG GLY LEU LEU
SEQRES   9 J  513  GLY ARG VAL VAL ASN THR LEU GLY ALA PRO ILE ASP GLY
SEQRES  10 J  513  LYS GLY PRO LEU ASP HIS ASP GLY PHE SER ALA VAL GLU
SEQRES  11 J  513  ALA ILE ALA PRO GLY VAL ILE GLU ARG GLN SER VAL ASP
SEQRES  12 J  513  GLN PRO VAL GLN THR GLY TYR LYS ALA VAL ASP SER MET
SEQRES  13 J  513  ILE PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES  14 J  513  ASP ARG GLN THR GLY LYS THR ALA LEU ALA ILE ASP ALA
SEQRES  15 J  513  ILE ILE ASN GLN ARG ASP SER GLY ILE LYS CYS ILE TYR
SEQRES  16 J  513  VAL ALA ILE GLY GLN LYS ALA SER THR ILE SER ASN VAL
SEQRES  17 J  513  VAL ARG LYS LEU GLU GLU HIS GLY ALA LEU ALA ASN THR
SEQRES  18 J  513  ILE VAL VAL VAL ALA THR ALA SER GLU SER ALA ALA LEU
SEQRES  19 J  513  GLN TYR LEU ALA PRO TYR ALA GLY CYS ALA MET GLY GLU
SEQRES  20 J  513  TYR PHE ARG ASP ARG GLY GLU ASP ALA LEU ILE ILE TYR
SEQRES  21 J  513  ASP ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN ILE
SEQRES  22 J  513  SER LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA PHE
SEQRES  23 J  513  PRO GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU
SEQRES  24 J  513  ARG ALA ALA ARG VAL ASN ALA GLU TYR VAL GLU ALA PHE
SEQRES  25 J  513  THR LYS GLY GLU VAL LYS GLY LYS THR GLY SER LEU THR
SEQRES  26 J  513  ALA LEU PRO ILE ILE GLU THR GLN ALA GLY ASP VAL SER
SEQRES  27 J  513  ALA PHE VAL PRO THR ASN VAL ILE SER ILE THR ASP GLY
SEQRES  28 J  513  GLN ILE PHE LEU GLU THR ASN LEU PHE ASN ALA GLY ILE
SEQRES  29 J  513  ARG PRO ALA VAL ASN PRO GLY ILE SER VAL SER ARG VAL
SEQRES  30 J  513  GLY GLY ALA ALA GLN THR LYS ILE MET LYS LYS LEU SER
SEQRES  31 J  513  GLY GLY ILE ARG THR ALA LEU ALA GLN TYR ARG GLU LEU
SEQRES  32 J  513  ALA ALA PHE SER GLN PHE ALA SER ASP LEU ASP ASP ALA
SEQRES  33 J  513  THR ARG LYS GLN LEU ASP HIS GLY GLN LYS VAL THR GLU
SEQRES  34 J  513  LEU LEU LYS GLN LYS GLN TYR ALA PRO MET SER VAL ALA
SEQRES  35 J  513  GLN GLN SER LEU VAL LEU PHE ALA ALA GLU ARG GLY TYR
SEQRES  36 J  513  LEU ALA ASP VAL GLU LEU SER LYS ILE GLY SER PHE GLU
SEQRES  37 J  513  ALA ALA LEU LEU ALA TYR VAL ASP ARG ASP HIS ALA PRO
SEQRES  38 J  513  LEU MET GLN GLU ILE ASN GLN THR GLY GLY TYR ASN ASP
SEQRES  39 J  513  GLU ILE GLU GLY LYS LEU LYS GLY ILE LEU ASP SER PHE
SEQRES  40 J  513  LYS ALA THR GLN SER TRP
SEQRES   1 K  513  MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES   2 K  513  GLN ARG ILE ALA GLN PHE ASN VAL VAL SER GLU ALA HIS
SEQRES   3 K  513  ASN GLU GLY THR ILE VAL SER VAL SER ASP GLY VAL ILE
SEQRES   4 K  513  ARG ILE HIS GLY LEU ALA ASP CYS MET GLN GLY GLU MET
SEQRES   5 K  513  ILE SER LEU PRO GLY ASN ARG TYR ALA ILE ALA LEU ASN
SEQRES   6 K  513  LEU GLU ARG ASP SER VAL GLY ALA VAL VAL MET GLY PRO
SEQRES   7 K  513  TYR ALA ASP LEU ALA GLU GLY MET LYS VAL LYS CYS THR
SEQRES   8 K  513  GLY ARG ILE LEU GLU VAL PRO VAL GLY ARG GLY LEU LEU
SEQRES   9 K  513  GLY ARG VAL VAL ASN THR LEU GLY ALA PRO ILE ASP GLY
SEQRES  10 K  513  LYS GLY PRO LEU ASP HIS ASP GLY PHE SER ALA VAL GLU
SEQRES  11 K  513  ALA ILE ALA PRO GLY VAL ILE GLU ARG GLN SER VAL ASP
SEQRES  12 K  513  GLN PRO VAL GLN THR GLY TYR LYS ALA VAL ASP SER MET
SEQRES  13 K  513  ILE PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES  14 K  513  ASP ARG GLN THR GLY LYS THR ALA LEU ALA ILE ASP ALA
SEQRES  15 K  513  ILE ILE ASN GLN ARG ASP SER GLY ILE LYS CYS ILE TYR
SEQRES  16 K  513  VAL ALA ILE GLY GLN LYS ALA SER THR ILE SER ASN VAL
SEQRES  17 K  513  VAL ARG LYS LEU GLU GLU HIS GLY ALA LEU ALA ASN THR
SEQRES  18 K  513  ILE VAL VAL VAL ALA THR ALA SER GLU SER ALA ALA LEU
SEQRES  19 K  513  GLN TYR LEU ALA PRO TYR ALA GLY CYS ALA MET GLY GLU
SEQRES  20 K  513  TYR PHE ARG ASP ARG GLY GLU ASP ALA LEU ILE ILE TYR
SEQRES  21 K  513  ASP ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN ILE
SEQRES  22 K  513  SER LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA PHE
SEQRES  23 K  513  PRO GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU
SEQRES  24 K  513  ARG ALA ALA ARG VAL ASN ALA GLU TYR VAL GLU ALA PHE
SEQRES  25 K  513  THR LYS GLY GLU VAL LYS GLY LYS THR GLY SER LEU THR
SEQRES  26 K  513  ALA LEU PRO ILE ILE GLU THR GLN ALA GLY ASP VAL SER
SEQRES  27 K  513  ALA PHE VAL PRO THR ASN VAL ILE SER ILE THR ASP GLY
SEQRES  28 K  513  GLN ILE PHE LEU GLU THR ASN LEU PHE ASN ALA GLY ILE
SEQRES  29 K  513  ARG PRO ALA VAL ASN PRO GLY ILE SER VAL SER ARG VAL
SEQRES  30 K  513  GLY GLY ALA ALA GLN THR LYS ILE MET LYS LYS LEU SER
SEQRES  31 K  513  GLY GLY ILE ARG THR ALA LEU ALA GLN TYR ARG GLU LEU
SEQRES  32 K  513  ALA ALA PHE SER GLN PHE ALA SER ASP LEU ASP ASP ALA
SEQRES  33 K  513  THR ARG LYS GLN LEU ASP HIS GLY GLN LYS VAL THR GLU
SEQRES  34 K  513  LEU LEU LYS GLN LYS GLN TYR ALA PRO MET SER VAL ALA
SEQRES  35 K  513  GLN GLN SER LEU VAL LEU PHE ALA ALA GLU ARG GLY TYR
SEQRES  36 K  513  LEU ALA ASP VAL GLU LEU SER LYS ILE GLY SER PHE GLU
SEQRES  37 K  513  ALA ALA LEU LEU ALA TYR VAL ASP ARG ASP HIS ALA PRO
SEQRES  38 K  513  LEU MET GLN GLU ILE ASN GLN THR GLY GLY TYR ASN ASP
SEQRES  39 K  513  GLU ILE GLU GLY LYS LEU LYS GLY ILE LEU ASP SER PHE
SEQRES  40 K  513  LYS ALA THR GLN SER TRP
SEQRES   1 L  459  ALA THR GLY LYS ILE VAL GLN VAL ILE GLY ALA VAL VAL
SEQRES   2 L  459  ASP VAL GLU PHE PRO GLN ASP ALA VAL PRO ARG VAL TYR
SEQRES   3 L  459  ASP ALA LEU GLU VAL GLN ASN GLY ASN GLU ARG LEU VAL
SEQRES   4 L  459  LEU GLU VAL GLN GLN GLN LEU GLY GLY GLY ILE VAL ARG
SEQRES   5 L  459  THR ILE ALA MET GLY SER SER ASP GLY LEU ARG ARG GLY
SEQRES   6 L  459  LEU ASP VAL LYS ASP LEU GLU HIS PRO ILE GLU VAL PRO
SEQRES   7 L  459  VAL GLY GLU ALA THR LEU GLY ARG ILE MET ASN VAL LEU
SEQRES   8 L  459  GLY GLU PRO VAL ASP MET LYS GLY GLU ILE GLY GLU GLU
SEQRES   9 L  459  GLU ARG TRP ALA ILE HIS ARG ALA ALA PRO SER TYR GLU
SEQRES  10 L  459  GLU LEU SER ASN SER GLN GLU LEU LEU GLU THR GLY ILE
SEQRES  11 L  459  LYS VAL ILE ASP LEU MET CYS PRO PHE ALA LYS GLY GLY
SEQRES  12 L  459  LYS VAL GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR
SEQRES  13 L  459  VAL ASN MET MET GLU LEU ILE ARG ASN ILE ALA ILE GLU
SEQRES  14 L  459  HIS SER GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG
SEQRES  15 L  459  THR ARG GLU GLY ASN ASP PHE TYR HIS GLU MET THR ASP
SEQRES  16 L  459  SER ASN VAL ILE ASP LYS VAL SER LEU VAL TYR GLY GLN
SEQRES  17 L  459  MET ASN GLU PRO PRO GLY ASN ARG LEU ARG VAL ALA LEU
SEQRES  18 L  459  THR GLY LEU THR MET ALA GLU LYS PHE ARG ASP GLU GLY
SEQRES  19 L  459  ARG ASP VAL LEU LEU PHE VAL ASP ASN ILE TYR ARG TYR
SEQRES  20 L  459  THR LEU ALA GLY THR GLU VAL SER ALA LEU LEU GLY ARG
SEQRES  21 L  459  MET PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA GLU
SEQRES  22 L  459  GLU MET GLY VAL LEU GLN GLU ARG ILE THR SER THR LYS
SEQRES  23 L  459  THR GLY SER ILE THR SER VAL GLN ALA VAL TYR VAL PRO
SEQRES  24 L  459  ALA ASP ASP LEU THR ASP PRO SER PRO ALA THR THR PHE
SEQRES  25 L  459  ALA HIS LEU ASP ALA THR VAL VAL LEU SER ARG GLN ILE
SEQRES  26 L  459  ALA SER LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP
SEQRES  27 L  459  SER THR SER ARG GLN LEU ASP PRO LEU VAL VAL GLY GLN
SEQRES  28 L  459  GLU HIS TYR ASP THR ALA ARG GLY VAL GLN SER ILE LEU
SEQRES  29 L  459  GLN ARG TYR GLN GLU LEU LYS ASP ILE ILE ALA ILE LEU
SEQRES  30 L  459  GLY MET ASP GLU LEU SER GLU GLU ASP LYS LEU VAL VAL
SEQRES  31 L  459  ALA ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO
SEQRES  32 L  459  PHE PHE VAL ALA GLU VAL PHE THR GLY SER PRO GLY LYS
SEQRES  33 L  459  TYR VAL SER LEU LYS ASP THR ILE ARG GLY PHE LYS GLY
SEQRES  34 L  459  ILE MET GLU GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA
SEQRES  35 L  459  PHE TYR MET VAL GLY SER ILE GLU GLU ALA VAL GLU LYS
SEQRES  36 L  459  ALA LYS LYS LEU
SEQRES   1 M  459  ALA THR GLY LYS ILE VAL GLN VAL ILE GLY ALA VAL VAL
SEQRES   2 M  459  ASP VAL GLU PHE PRO GLN ASP ALA VAL PRO ARG VAL TYR
SEQRES   3 M  459  ASP ALA LEU GLU VAL GLN ASN GLY ASN GLU ARG LEU VAL
SEQRES   4 M  459  LEU GLU VAL GLN GLN GLN LEU GLY GLY GLY ILE VAL ARG
SEQRES   5 M  459  THR ILE ALA MET GLY SER SER ASP GLY LEU ARG ARG GLY
SEQRES   6 M  459  LEU ASP VAL LYS ASP LEU GLU HIS PRO ILE GLU VAL PRO
SEQRES   7 M  459  VAL GLY GLU ALA THR LEU GLY ARG ILE MET ASN VAL LEU
SEQRES   8 M  459  GLY GLU PRO VAL ASP MET LYS GLY GLU ILE GLY GLU GLU
SEQRES   9 M  459  GLU ARG TRP ALA ILE HIS ARG ALA ALA PRO SER TYR GLU
SEQRES  10 M  459  GLU LEU SER ASN SER GLN GLU LEU LEU GLU THR GLY ILE
SEQRES  11 M  459  LYS VAL ILE ASP LEU MET CYS PRO PHE ALA LYS GLY GLY
SEQRES  12 M  459  LYS VAL GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR
SEQRES  13 M  459  VAL ASN MET MET GLU LEU ILE ARG ASN ILE ALA ILE GLU
SEQRES  14 M  459  HIS SER GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG
SEQRES  15 M  459  THR ARG GLU GLY ASN ASP PHE TYR HIS GLU MET THR ASP
SEQRES  16 M  459  SER ASN VAL ILE ASP LYS VAL SER LEU VAL TYR GLY GLN
SEQRES  17 M  459  MET ASN GLU PRO PRO GLY ASN ARG LEU ARG VAL ALA LEU
SEQRES  18 M  459  THR GLY LEU THR MET ALA GLU LYS PHE ARG ASP GLU GLY
SEQRES  19 M  459  ARG ASP VAL LEU LEU PHE VAL ASP ASN ILE TYR ARG TYR
SEQRES  20 M  459  THR LEU ALA GLY THR GLU VAL SER ALA LEU LEU GLY ARG
SEQRES  21 M  459  MET PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA GLU
SEQRES  22 M  459  GLU MET GLY VAL LEU GLN GLU ARG ILE THR SER THR LYS
SEQRES  23 M  459  THR GLY SER ILE THR SER VAL GLN ALA VAL TYR VAL PRO
SEQRES  24 M  459  ALA ASP ASP LEU THR ASP PRO SER PRO ALA THR THR PHE
SEQRES  25 M  459  ALA HIS LEU ASP ALA THR VAL VAL LEU SER ARG GLN ILE
SEQRES  26 M  459  ALA SER LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP
SEQRES  27 M  459  SER THR SER ARG GLN LEU ASP PRO LEU VAL VAL GLY GLN
SEQRES  28 M  459  GLU HIS TYR ASP THR ALA ARG GLY VAL GLN SER ILE LEU
SEQRES  29 M  459  GLN ARG TYR GLN GLU LEU LYS ASP ILE ILE ALA ILE LEU
SEQRES  30 M  459  GLY MET ASP GLU LEU SER GLU GLU ASP LYS LEU VAL VAL
SEQRES  31 M  459  ALA ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO
SEQRES  32 M  459  PHE PHE VAL ALA GLU VAL PHE THR GLY SER PRO GLY LYS
SEQRES  33 M  459  TYR VAL SER LEU LYS ASP THR ILE ARG GLY PHE LYS GLY
SEQRES  34 M  459  ILE MET GLU GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA
SEQRES  35 M  459  PHE TYR MET VAL GLY SER ILE GLU GLU ALA VAL GLU LYS
SEQRES  36 M  459  ALA LYS LYS LEU
SEQRES   1 N  459  ALA THR GLY LYS ILE VAL GLN VAL ILE GLY ALA VAL VAL
SEQRES   2 N  459  ASP VAL GLU PHE PRO GLN ASP ALA VAL PRO ARG VAL TYR
SEQRES   3 N  459  ASP ALA LEU GLU VAL GLN ASN GLY ASN GLU ARG LEU VAL
SEQRES   4 N  459  LEU GLU VAL GLN GLN GLN LEU GLY GLY GLY ILE VAL ARG
SEQRES   5 N  459  THR ILE ALA MET GLY SER SER ASP GLY LEU ARG ARG GLY
SEQRES   6 N  459  LEU ASP VAL LYS ASP LEU GLU HIS PRO ILE GLU VAL PRO
SEQRES   7 N  459  VAL GLY GLU ALA THR LEU GLY ARG ILE MET ASN VAL LEU
SEQRES   8 N  459  GLY GLU PRO VAL ASP MET LYS GLY GLU ILE GLY GLU GLU
SEQRES   9 N  459  GLU ARG TRP ALA ILE HIS ARG ALA ALA PRO SER TYR GLU
SEQRES  10 N  459  GLU LEU SER ASN SER GLN GLU LEU LEU GLU THR GLY ILE
SEQRES  11 N  459  LYS VAL ILE ASP LEU MET CYS PRO PHE ALA LYS GLY GLY
SEQRES  12 N  459  LYS VAL GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR
SEQRES  13 N  459  VAL ASN MET MET GLU LEU ILE ARG ASN ILE ALA ILE GLU
SEQRES  14 N  459  HIS SER GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG
SEQRES  15 N  459  THR ARG GLU GLY ASN ASP PHE TYR HIS GLU MET THR ASP
SEQRES  16 N  459  SER ASN VAL ILE ASP LYS VAL SER LEU VAL TYR GLY GLN
SEQRES  17 N  459  MET ASN GLU PRO PRO GLY ASN ARG LEU ARG VAL ALA LEU
SEQRES  18 N  459  THR GLY LEU THR MET ALA GLU LYS PHE ARG ASP GLU GLY
SEQRES  19 N  459  ARG ASP VAL LEU LEU PHE VAL ASP ASN ILE TYR ARG TYR
SEQRES  20 N  459  THR LEU ALA GLY THR GLU VAL SER ALA LEU LEU GLY ARG
SEQRES  21 N  459  MET PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA GLU
SEQRES  22 N  459  GLU MET GLY VAL LEU GLN GLU ARG ILE THR SER THR LYS
SEQRES  23 N  459  THR GLY SER ILE THR SER VAL GLN ALA VAL TYR VAL PRO
SEQRES  24 N  459  ALA ASP ASP LEU THR ASP PRO SER PRO ALA THR THR PHE
SEQRES  25 N  459  ALA HIS LEU ASP ALA THR VAL VAL LEU SER ARG GLN ILE
SEQRES  26 N  459  ALA SER LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP
SEQRES  27 N  459  SER THR SER ARG GLN LEU ASP PRO LEU VAL VAL GLY GLN
SEQRES  28 N  459  GLU HIS TYR ASP THR ALA ARG GLY VAL GLN SER ILE LEU
SEQRES  29 N  459  GLN ARG TYR GLN GLU LEU LYS ASP ILE ILE ALA ILE LEU
SEQRES  30 N  459  GLY MET ASP GLU LEU SER GLU GLU ASP LYS LEU VAL VAL
SEQRES  31 N  459  ALA ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO
SEQRES  32 N  459  PHE PHE VAL ALA GLU VAL PHE THR GLY SER PRO GLY LYS
SEQRES  33 N  459  TYR VAL SER LEU LYS ASP THR ILE ARG GLY PHE LYS GLY
SEQRES  34 N  459  ILE MET GLU GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA
SEQRES  35 N  459  PHE TYR MET VAL GLY SER ILE GLU GLU ALA VAL GLU LYS
SEQRES  36 N  459  ALA LYS LYS LEU
SEQRES   1 O  286  ALA GLY ALA LYS GLU ILE ARG SER LYS ILE ALA SER VAL
SEQRES   2 O  286  GLN ASN THR GLN LYS ILE THR LYS ALA MET GLU MET VAL
SEQRES   3 O  286  ALA ALA SER LYS MET ARG LYS SER GLN ASP ARG MET ALA
SEQRES   4 O  286  ALA SER ARG PRO TYR ALA GLU THR MET ARG LYS VAL ILE
SEQRES   5 O  286  GLY HIS LEU ALA HIS GLY ASN LEU GLU TYR LYS HIS PRO
SEQRES   6 O  286  TYR LEU GLU ASP ARG ASP VAL LYS ARG VAL GLY TYR LEU
SEQRES   7 O  286  VAL VAL SER THR ASP ARG GLY LEU CYS GLY GLY LEU ASN
SEQRES   8 O  286  ILE ASN LEU PHE LYS LYS LEU LEU ALA GLU MET LYS THR
SEQRES   9 O  286  TRP THR ASP LYS GLY VAL GLN CYS ASP LEU ALA MET ILE
SEQRES  10 O  286  GLY SER LYS GLY VAL SER PHE PHE ASN SER VAL GLY GLY
SEQRES  11 O  286  ASN VAL VAL ALA GLN VAL THR GLY MET GLY ASP ASN PRO
SEQRES  12 O  286  SER LEU SER GLU LEU ILE GLY PRO VAL LYS VAL MET LEU
SEQRES  13 O  286  GLN ALA TYR ASP GLU GLY ARG LEU ASP LYS LEU TYR ILE
SEQRES  14 O  286  VAL SER ASN LYS PHE ILE ASN THR MET SER GLN VAL PRO
SEQRES  15 O  286  THR ILE SER GLN LEU LEU PRO LEU PRO ALA SER ASP ASP
SEQRES  16 O  286  ASP ASP LEU LYS HIS LYS SER TRP ASP TYR LEU TYR GLU
SEQRES  17 O  286  PRO ASP PRO LYS ALA LEU LEU ASP THR LEU LEU ARG ARG
SEQRES  18 O  286  TYR VAL GLU SER GLN VAL TYR GLN GLY VAL VAL GLU ASN
SEQRES  19 O  286  LEU ALA SER GLU GLN ALA ALA ARG MET VAL ALA MET LYS
SEQRES  20 O  286  ALA ALA THR ASP ASN GLY GLY SER LEU ILE LYS GLU LEU
SEQRES  21 O  286  GLN LEU VAL TYR ASN LYS ALA ARG GLN ALA SER ILE THR
SEQRES  22 O  286  GLN GLU LEU THR GLU ILE VAL SER GLY ALA ALA ALA VAL
SEQRES   1 P  138  ALA MET THR TYR HIS LEU ASP VAL VAL SER ALA GLU GLN
SEQRES   2 P  138  GLN MET PHE SER GLY LEU VAL GLU LYS ILE GLN VAL THR
SEQRES   3 P  138  GLY SER GLU GLY GLU LEU GLY ILE TYR PRO GLY HIS ALA
SEQRES   4 P  138  PRO LEU LEU THR ALA ILE LYS PRO GLY MET ILE ARG ILE
SEQRES   5 P  138  VAL LYS GLN HIS GLY HIS GLU GLU PHE ILE TYR LEU SER
SEQRES   6 P  138  GLY GLY ILE LEU GLU VAL GLN PRO GLY ASN VAL THR VAL
SEQRES   7 P  138  LEU ALA ASP THR ALA ILE ARG GLY GLN ASP LEU ASP GLU
SEQRES   8 P  138  ALA ARG ALA MET GLU ALA LYS ARG LYS ALA GLU GLU HIS
SEQRES   9 P  138  ILE SER SER SER HIS GLY ASP VAL ASP TYR ALA GLN ALA
SEQRES  10 P  138  SER ALA GLU LEU ALA LYS ALA ILE ALA GLN LEU ARG VAL
SEQRES  11 P  138  ILE GLU LEU THR LYS LYS ALA MET
SEQRES   1 Q  513  MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES   2 Q  513  GLN ARG ILE ALA GLN PHE ASN VAL VAL SER GLU ALA HIS
SEQRES   3 Q  513  ASN GLU GLY THR ILE VAL SER VAL SER ASP GLY VAL ILE
SEQRES   4 Q  513  ARG ILE HIS GLY LEU ALA ASP CYS MET GLN GLY GLU MET
SEQRES   5 Q  513  ILE SER LEU PRO GLY ASN ARG TYR ALA ILE ALA LEU ASN
SEQRES   6 Q  513  LEU GLU ARG ASP SER VAL GLY ALA VAL VAL MET GLY PRO
SEQRES   7 Q  513  TYR ALA ASP LEU ALA GLU GLY MET LYS VAL LYS CYS THR
SEQRES   8 Q  513  GLY ARG ILE LEU GLU VAL PRO VAL GLY ARG GLY LEU LEU
SEQRES   9 Q  513  GLY ARG VAL VAL ASN THR LEU GLY ALA PRO ILE ASP GLY
SEQRES  10 Q  513  LYS GLY PRO LEU ASP HIS ASP GLY PHE SER ALA VAL GLU
SEQRES  11 Q  513  ALA ILE ALA PRO GLY VAL ILE GLU ARG GLN SER VAL ASP
SEQRES  12 Q  513  GLN PRO VAL GLN THR GLY TYR LYS ALA VAL ASP SER MET
SEQRES  13 Q  513  ILE PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES  14 Q  513  ASP ARG GLN THR GLY LYS THR ALA LEU ALA ILE ASP ALA
SEQRES  15 Q  513  ILE ILE ASN GLN ARG ASP SER GLY ILE LYS CYS ILE TYR
SEQRES  16 Q  513  VAL ALA ILE GLY GLN LYS ALA SER THR ILE SER ASN VAL
SEQRES  17 Q  513  VAL ARG LYS LEU GLU GLU HIS GLY ALA LEU ALA ASN THR
SEQRES  18 Q  513  ILE VAL VAL VAL ALA THR ALA SER GLU SER ALA ALA LEU
SEQRES  19 Q  513  GLN TYR LEU ALA PRO TYR ALA GLY CYS ALA MET GLY GLU
SEQRES  20 Q  513  TYR PHE ARG ASP ARG GLY GLU ASP ALA LEU ILE ILE TYR
SEQRES  21 Q  513  ASP ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN ILE
SEQRES  22 Q  513  SER LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA PHE
SEQRES  23 Q  513  PRO GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU
SEQRES  24 Q  513  ARG ALA ALA ARG VAL ASN ALA GLU TYR VAL GLU ALA PHE
SEQRES  25 Q  513  THR LYS GLY GLU VAL LYS GLY LYS THR GLY SER LEU THR
SEQRES  26 Q  513  ALA LEU PRO ILE ILE GLU THR GLN ALA GLY ASP VAL SER
SEQRES  27 Q  513  ALA PHE VAL PRO THR ASN VAL ILE SER ILE THR ASP GLY
SEQRES  28 Q  513  GLN ILE PHE LEU GLU THR ASN LEU PHE ASN ALA GLY ILE
SEQRES  29 Q  513  ARG PRO ALA VAL ASN PRO GLY ILE SER VAL SER ARG VAL
SEQRES  30 Q  513  GLY GLY ALA ALA GLN THR LYS ILE MET LYS LYS LEU SER
SEQRES  31 Q  513  GLY GLY ILE ARG THR ALA LEU ALA GLN TYR ARG GLU LEU
SEQRES  32 Q  513  ALA ALA PHE SER GLN PHE ALA SER ASP LEU ASP ASP ALA
SEQRES  33 Q  513  THR ARG LYS GLN LEU ASP HIS GLY GLN LYS VAL THR GLU
SEQRES  34 Q  513  LEU LEU LYS GLN LYS GLN TYR ALA PRO MET SER VAL ALA
SEQRES  35 Q  513  GLN GLN SER LEU VAL LEU PHE ALA ALA GLU ARG GLY TYR
SEQRES  36 Q  513  LEU ALA ASP VAL GLU LEU SER LYS ILE GLY SER PHE GLU
SEQRES  37 Q  513  ALA ALA LEU LEU ALA TYR VAL ASP ARG ASP HIS ALA PRO
SEQRES  38 Q  513  LEU MET GLN GLU ILE ASN GLN THR GLY GLY TYR ASN ASP
SEQRES  39 Q  513  GLU ILE GLU GLY LYS LEU LYS GLY ILE LEU ASP SER PHE
SEQRES  40 Q  513  LYS ALA THR GLN SER TRP
SEQRES   1 R  513  MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES   2 R  513  GLN ARG ILE ALA GLN PHE ASN VAL VAL SER GLU ALA HIS
SEQRES   3 R  513  ASN GLU GLY THR ILE VAL SER VAL SER ASP GLY VAL ILE
SEQRES   4 R  513  ARG ILE HIS GLY LEU ALA ASP CYS MET GLN GLY GLU MET
SEQRES   5 R  513  ILE SER LEU PRO GLY ASN ARG TYR ALA ILE ALA LEU ASN
SEQRES   6 R  513  LEU GLU ARG ASP SER VAL GLY ALA VAL VAL MET GLY PRO
SEQRES   7 R  513  TYR ALA ASP LEU ALA GLU GLY MET LYS VAL LYS CYS THR
SEQRES   8 R  513  GLY ARG ILE LEU GLU VAL PRO VAL GLY ARG GLY LEU LEU
SEQRES   9 R  513  GLY ARG VAL VAL ASN THR LEU GLY ALA PRO ILE ASP GLY
SEQRES  10 R  513  LYS GLY PRO LEU ASP HIS ASP GLY PHE SER ALA VAL GLU
SEQRES  11 R  513  ALA ILE ALA PRO GLY VAL ILE GLU ARG GLN SER VAL ASP
SEQRES  12 R  513  GLN PRO VAL GLN THR GLY TYR LYS ALA VAL ASP SER MET
SEQRES  13 R  513  ILE PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES  14 R  513  ASP ARG GLN THR GLY LYS THR ALA LEU ALA ILE ASP ALA
SEQRES  15 R  513  ILE ILE ASN GLN ARG ASP SER GLY ILE LYS CYS ILE TYR
SEQRES  16 R  513  VAL ALA ILE GLY GLN LYS ALA SER THR ILE SER ASN VAL
SEQRES  17 R  513  VAL ARG LYS LEU GLU GLU HIS GLY ALA LEU ALA ASN THR
SEQRES  18 R  513  ILE VAL VAL VAL ALA THR ALA SER GLU SER ALA ALA LEU
SEQRES  19 R  513  GLN TYR LEU ALA PRO TYR ALA GLY CYS ALA MET GLY GLU
SEQRES  20 R  513  TYR PHE ARG ASP ARG GLY GLU ASP ALA LEU ILE ILE TYR
SEQRES  21 R  513  ASP ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN ILE
SEQRES  22 R  513  SER LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA PHE
SEQRES  23 R  513  PRO GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU
SEQRES  24 R  513  ARG ALA ALA ARG VAL ASN ALA GLU TYR VAL GLU ALA PHE
SEQRES  25 R  513  THR LYS GLY GLU VAL LYS GLY LYS THR GLY SER LEU THR
SEQRES  26 R  513  ALA LEU PRO ILE ILE GLU THR GLN ALA GLY ASP VAL SER
SEQRES  27 R  513  ALA PHE VAL PRO THR ASN VAL ILE SER ILE THR ASP GLY
SEQRES  28 R  513  GLN ILE PHE LEU GLU THR ASN LEU PHE ASN ALA GLY ILE
SEQRES  29 R  513  ARG PRO ALA VAL ASN PRO GLY ILE SER VAL SER ARG VAL
SEQRES  30 R  513  GLY GLY ALA ALA GLN THR LYS ILE MET LYS LYS LEU SER
SEQRES  31 R  513  GLY GLY ILE ARG THR ALA LEU ALA GLN TYR ARG GLU LEU
SEQRES  32 R  513  ALA ALA PHE SER GLN PHE ALA SER ASP LEU ASP ASP ALA
SEQRES  33 R  513  THR ARG LYS GLN LEU ASP HIS GLY GLN LYS VAL THR GLU
SEQRES  34 R  513  LEU LEU LYS GLN LYS GLN TYR ALA PRO MET SER VAL ALA
SEQRES  35 R  513  GLN GLN SER LEU VAL LEU PHE ALA ALA GLU ARG GLY TYR
SEQRES  36 R  513  LEU ALA ASP VAL GLU LEU SER LYS ILE GLY SER PHE GLU
SEQRES  37 R  513  ALA ALA LEU LEU ALA TYR VAL ASP ARG ASP HIS ALA PRO
SEQRES  38 R  513  LEU MET GLN GLU ILE ASN GLN THR GLY GLY TYR ASN ASP
SEQRES  39 R  513  GLU ILE GLU GLY LYS LEU LYS GLY ILE LEU ASP SER PHE
SEQRES  40 R  513  LYS ALA THR GLN SER TRP
SEQRES   1 S  513  MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES   2 S  513  GLN ARG ILE ALA GLN PHE ASN VAL VAL SER GLU ALA HIS
SEQRES   3 S  513  ASN GLU GLY THR ILE VAL SER VAL SER ASP GLY VAL ILE
SEQRES   4 S  513  ARG ILE HIS GLY LEU ALA ASP CYS MET GLN GLY GLU MET
SEQRES   5 S  513  ILE SER LEU PRO GLY ASN ARG TYR ALA ILE ALA LEU ASN
SEQRES   6 S  513  LEU GLU ARG ASP SER VAL GLY ALA VAL VAL MET GLY PRO
SEQRES   7 S  513  TYR ALA ASP LEU ALA GLU GLY MET LYS VAL LYS CYS THR
SEQRES   8 S  513  GLY ARG ILE LEU GLU VAL PRO VAL GLY ARG GLY LEU LEU
SEQRES   9 S  513  GLY ARG VAL VAL ASN THR LEU GLY ALA PRO ILE ASP GLY
SEQRES  10 S  513  LYS GLY PRO LEU ASP HIS ASP GLY PHE SER ALA VAL GLU
SEQRES  11 S  513  ALA ILE ALA PRO GLY VAL ILE GLU ARG GLN SER VAL ASP
SEQRES  12 S  513  GLN PRO VAL GLN THR GLY TYR LYS ALA VAL ASP SER MET
SEQRES  13 S  513  ILE PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES  14 S  513  ASP ARG GLN THR GLY LYS THR ALA LEU ALA ILE ASP ALA
SEQRES  15 S  513  ILE ILE ASN GLN ARG ASP SER GLY ILE LYS CYS ILE TYR
SEQRES  16 S  513  VAL ALA ILE GLY GLN LYS ALA SER THR ILE SER ASN VAL
SEQRES  17 S  513  VAL ARG LYS LEU GLU GLU HIS GLY ALA LEU ALA ASN THR
SEQRES  18 S  513  ILE VAL VAL VAL ALA THR ALA SER GLU SER ALA ALA LEU
SEQRES  19 S  513  GLN TYR LEU ALA PRO TYR ALA GLY CYS ALA MET GLY GLU
SEQRES  20 S  513  TYR PHE ARG ASP ARG GLY GLU ASP ALA LEU ILE ILE TYR
SEQRES  21 S  513  ASP ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN ILE
SEQRES  22 S  513  SER LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA PHE
SEQRES  23 S  513  PRO GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU
SEQRES  24 S  513  ARG ALA ALA ARG VAL ASN ALA GLU TYR VAL GLU ALA PHE
SEQRES  25 S  513  THR LYS GLY GLU VAL LYS GLY LYS THR GLY SER LEU THR
SEQRES  26 S  513  ALA LEU PRO ILE ILE GLU THR GLN ALA GLY ASP VAL SER
SEQRES  27 S  513  ALA PHE VAL PRO THR ASN VAL ILE SER ILE THR ASP GLY
SEQRES  28 S  513  GLN ILE PHE LEU GLU THR ASN LEU PHE ASN ALA GLY ILE
SEQRES  29 S  513  ARG PRO ALA VAL ASN PRO GLY ILE SER VAL SER ARG VAL
SEQRES  30 S  513  GLY GLY ALA ALA GLN THR LYS ILE MET LYS LYS LEU SER
SEQRES  31 S  513  GLY GLY ILE ARG THR ALA LEU ALA GLN TYR ARG GLU LEU
SEQRES  32 S  513  ALA ALA PHE SER GLN PHE ALA SER ASP LEU ASP ASP ALA
SEQRES  33 S  513  THR ARG LYS GLN LEU ASP HIS GLY GLN LYS VAL THR GLU
SEQRES  34 S  513  LEU LEU LYS GLN LYS GLN TYR ALA PRO MET SER VAL ALA
SEQRES  35 S  513  GLN GLN SER LEU VAL LEU PHE ALA ALA GLU ARG GLY TYR
SEQRES  36 S  513  LEU ALA ASP VAL GLU LEU SER LYS ILE GLY SER PHE GLU
SEQRES  37 S  513  ALA ALA LEU LEU ALA TYR VAL ASP ARG ASP HIS ALA PRO
SEQRES  38 S  513  LEU MET GLN GLU ILE ASN GLN THR GLY GLY TYR ASN ASP
SEQRES  39 S  513  GLU ILE GLU GLY LYS LEU LYS GLY ILE LEU ASP SER PHE
SEQRES  40 S  513  LYS ALA THR GLN SER TRP
SEQRES   1 T  459  ALA THR GLY LYS ILE VAL GLN VAL ILE GLY ALA VAL VAL
SEQRES   2 T  459  ASP VAL GLU PHE PRO GLN ASP ALA VAL PRO ARG VAL TYR
SEQRES   3 T  459  ASP ALA LEU GLU VAL GLN ASN GLY ASN GLU ARG LEU VAL
SEQRES   4 T  459  LEU GLU VAL GLN GLN GLN LEU GLY GLY GLY ILE VAL ARG
SEQRES   5 T  459  THR ILE ALA MET GLY SER SER ASP GLY LEU ARG ARG GLY
SEQRES   6 T  459  LEU ASP VAL LYS ASP LEU GLU HIS PRO ILE GLU VAL PRO
SEQRES   7 T  459  VAL GLY GLU ALA THR LEU GLY ARG ILE MET ASN VAL LEU
SEQRES   8 T  459  GLY GLU PRO VAL ASP MET LYS GLY GLU ILE GLY GLU GLU
SEQRES   9 T  459  GLU ARG TRP ALA ILE HIS ARG ALA ALA PRO SER TYR GLU
SEQRES  10 T  459  GLU LEU SER ASN SER GLN GLU LEU LEU GLU THR GLY ILE
SEQRES  11 T  459  LYS VAL ILE ASP LEU MET CYS PRO PHE ALA LYS GLY GLY
SEQRES  12 T  459  LYS VAL GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR
SEQRES  13 T  459  VAL ASN MET MET GLU LEU ILE ARG ASN ILE ALA ILE GLU
SEQRES  14 T  459  HIS SER GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG
SEQRES  15 T  459  THR ARG GLU GLY ASN ASP PHE TYR HIS GLU MET THR ASP
SEQRES  16 T  459  SER ASN VAL ILE ASP LYS VAL SER LEU VAL TYR GLY GLN
SEQRES  17 T  459  MET ASN GLU PRO PRO GLY ASN ARG LEU ARG VAL ALA LEU
SEQRES  18 T  459  THR GLY LEU THR MET ALA GLU LYS PHE ARG ASP GLU GLY
SEQRES  19 T  459  ARG ASP VAL LEU LEU PHE VAL ASP ASN ILE TYR ARG TYR
SEQRES  20 T  459  THR LEU ALA GLY THR GLU VAL SER ALA LEU LEU GLY ARG
SEQRES  21 T  459  MET PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA GLU
SEQRES  22 T  459  GLU MET GLY VAL LEU GLN GLU ARG ILE THR SER THR LYS
SEQRES  23 T  459  THR GLY SER ILE THR SER VAL GLN ALA VAL TYR VAL PRO
SEQRES  24 T  459  ALA ASP ASP LEU THR ASP PRO SER PRO ALA THR THR PHE
SEQRES  25 T  459  ALA HIS LEU ASP ALA THR VAL VAL LEU SER ARG GLN ILE
SEQRES  26 T  459  ALA SER LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP
SEQRES  27 T  459  SER THR SER ARG GLN LEU ASP PRO LEU VAL VAL GLY GLN
SEQRES  28 T  459  GLU HIS TYR ASP THR ALA ARG GLY VAL GLN SER ILE LEU
SEQRES  29 T  459  GLN ARG TYR GLN GLU LEU LYS ASP ILE ILE ALA ILE LEU
SEQRES  30 T  459  GLY MET ASP GLU LEU SER GLU GLU ASP LYS LEU VAL VAL
SEQRES  31 T  459  ALA ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO
SEQRES  32 T  459  PHE PHE VAL ALA GLU VAL PHE THR GLY SER PRO GLY LYS
SEQRES  33 T  459  TYR VAL SER LEU LYS ASP THR ILE ARG GLY PHE LYS GLY
SEQRES  34 T  459  ILE MET GLU GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA
SEQRES  35 T  459  PHE TYR MET VAL GLY SER ILE GLU GLU ALA VAL GLU LYS
SEQRES  36 T  459  ALA LYS LYS LEU
SEQRES   1 U  459  ALA THR GLY LYS ILE VAL GLN VAL ILE GLY ALA VAL VAL
SEQRES   2 U  459  ASP VAL GLU PHE PRO GLN ASP ALA VAL PRO ARG VAL TYR
SEQRES   3 U  459  ASP ALA LEU GLU VAL GLN ASN GLY ASN GLU ARG LEU VAL
SEQRES   4 U  459  LEU GLU VAL GLN GLN GLN LEU GLY GLY GLY ILE VAL ARG
SEQRES   5 U  459  THR ILE ALA MET GLY SER SER ASP GLY LEU ARG ARG GLY
SEQRES   6 U  459  LEU ASP VAL LYS ASP LEU GLU HIS PRO ILE GLU VAL PRO
SEQRES   7 U  459  VAL GLY GLU ALA THR LEU GLY ARG ILE MET ASN VAL LEU
SEQRES   8 U  459  GLY GLU PRO VAL ASP MET LYS GLY GLU ILE GLY GLU GLU
SEQRES   9 U  459  GLU ARG TRP ALA ILE HIS ARG ALA ALA PRO SER TYR GLU
SEQRES  10 U  459  GLU LEU SER ASN SER GLN GLU LEU LEU GLU THR GLY ILE
SEQRES  11 U  459  LYS VAL ILE ASP LEU MET CYS PRO PHE ALA LYS GLY GLY
SEQRES  12 U  459  LYS VAL GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR
SEQRES  13 U  459  VAL ASN MET MET GLU LEU ILE ARG ASN ILE ALA ILE GLU
SEQRES  14 U  459  HIS SER GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG
SEQRES  15 U  459  THR ARG GLU GLY ASN ASP PHE TYR HIS GLU MET THR ASP
SEQRES  16 U  459  SER ASN VAL ILE ASP LYS VAL SER LEU VAL TYR GLY GLN
SEQRES  17 U  459  MET ASN GLU PRO PRO GLY ASN ARG LEU ARG VAL ALA LEU
SEQRES  18 U  459  THR GLY LEU THR MET ALA GLU LYS PHE ARG ASP GLU GLY
SEQRES  19 U  459  ARG ASP VAL LEU LEU PHE VAL ASP ASN ILE TYR ARG TYR
SEQRES  20 U  459  THR LEU ALA GLY THR GLU VAL SER ALA LEU LEU GLY ARG
SEQRES  21 U  459  MET PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA GLU
SEQRES  22 U  459  GLU MET GLY VAL LEU GLN GLU ARG ILE THR SER THR LYS
SEQRES  23 U  459  THR GLY SER ILE THR SER VAL GLN ALA VAL TYR VAL PRO
SEQRES  24 U  459  ALA ASP ASP LEU THR ASP PRO SER PRO ALA THR THR PHE
SEQRES  25 U  459  ALA HIS LEU ASP ALA THR VAL VAL LEU SER ARG GLN ILE
SEQRES  26 U  459  ALA SER LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP
SEQRES  27 U  459  SER THR SER ARG GLN LEU ASP PRO LEU VAL VAL GLY GLN
SEQRES  28 U  459  GLU HIS TYR ASP THR ALA ARG GLY VAL GLN SER ILE LEU
SEQRES  29 U  459  GLN ARG TYR GLN GLU LEU LYS ASP ILE ILE ALA ILE LEU
SEQRES  30 U  459  GLY MET ASP GLU LEU SER GLU GLU ASP LYS LEU VAL VAL
SEQRES  31 U  459  ALA ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO
SEQRES  32 U  459  PHE PHE VAL ALA GLU VAL PHE THR GLY SER PRO GLY LYS
SEQRES  33 U  459  TYR VAL SER LEU LYS ASP THR ILE ARG GLY PHE LYS GLY
SEQRES  34 U  459  ILE MET GLU GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA
SEQRES  35 U  459  PHE TYR MET VAL GLY SER ILE GLU GLU ALA VAL GLU LYS
SEQRES  36 U  459  ALA LYS LYS LEU
SEQRES   1 V  459  ALA THR GLY LYS ILE VAL GLN VAL ILE GLY ALA VAL VAL
SEQRES   2 V  459  ASP VAL GLU PHE PRO GLN ASP ALA VAL PRO ARG VAL TYR
SEQRES   3 V  459  ASP ALA LEU GLU VAL GLN ASN GLY ASN GLU ARG LEU VAL
SEQRES   4 V  459  LEU GLU VAL GLN GLN GLN LEU GLY GLY GLY ILE VAL ARG
SEQRES   5 V  459  THR ILE ALA MET GLY SER SER ASP GLY LEU ARG ARG GLY
SEQRES   6 V  459  LEU ASP VAL LYS ASP LEU GLU HIS PRO ILE GLU VAL PRO
SEQRES   7 V  459  VAL GLY GLU ALA THR LEU GLY ARG ILE MET ASN VAL LEU
SEQRES   8 V  459  GLY GLU PRO VAL ASP MET LYS GLY GLU ILE GLY GLU GLU
SEQRES   9 V  459  GLU ARG TRP ALA ILE HIS ARG ALA ALA PRO SER TYR GLU
SEQRES  10 V  459  GLU LEU SER ASN SER GLN GLU LEU LEU GLU THR GLY ILE
SEQRES  11 V  459  LYS VAL ILE ASP LEU MET CYS PRO PHE ALA LYS GLY GLY
SEQRES  12 V  459  LYS VAL GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR
SEQRES  13 V  459  VAL ASN MET MET GLU LEU ILE ARG ASN ILE ALA ILE GLU
SEQRES  14 V  459  HIS SER GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG
SEQRES  15 V  459  THR ARG GLU GLY ASN ASP PHE TYR HIS GLU MET THR ASP
SEQRES  16 V  459  SER ASN VAL ILE ASP LYS VAL SER LEU VAL TYR GLY GLN
SEQRES  17 V  459  MET ASN GLU PRO PRO GLY ASN ARG LEU ARG VAL ALA LEU
SEQRES  18 V  459  THR GLY LEU THR MET ALA GLU LYS PHE ARG ASP GLU GLY
SEQRES  19 V  459  ARG ASP VAL LEU LEU PHE VAL ASP ASN ILE TYR ARG TYR
SEQRES  20 V  459  THR LEU ALA GLY THR GLU VAL SER ALA LEU LEU GLY ARG
SEQRES  21 V  459  MET PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA GLU
SEQRES  22 V  459  GLU MET GLY VAL LEU GLN GLU ARG ILE THR SER THR LYS
SEQRES  23 V  459  THR GLY SER ILE THR SER VAL GLN ALA VAL TYR VAL PRO
SEQRES  24 V  459  ALA ASP ASP LEU THR ASP PRO SER PRO ALA THR THR PHE
SEQRES  25 V  459  ALA HIS LEU ASP ALA THR VAL VAL LEU SER ARG GLN ILE
SEQRES  26 V  459  ALA SER LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP
SEQRES  27 V  459  SER THR SER ARG GLN LEU ASP PRO LEU VAL VAL GLY GLN
SEQRES  28 V  459  GLU HIS TYR ASP THR ALA ARG GLY VAL GLN SER ILE LEU
SEQRES  29 V  459  GLN ARG TYR GLN GLU LEU LYS ASP ILE ILE ALA ILE LEU
SEQRES  30 V  459  GLY MET ASP GLU LEU SER GLU GLU ASP LYS LEU VAL VAL
SEQRES  31 V  459  ALA ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO
SEQRES  32 V  459  PHE PHE VAL ALA GLU VAL PHE THR GLY SER PRO GLY LYS
SEQRES  33 V  459  TYR VAL SER LEU LYS ASP THR ILE ARG GLY PHE LYS GLY
SEQRES  34 V  459  ILE MET GLU GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA
SEQRES  35 V  459  PHE TYR MET VAL GLY SER ILE GLU GLU ALA VAL GLU LYS
SEQRES  36 V  459  ALA LYS LYS LEU
SEQRES   1 W  286  ALA GLY ALA LYS GLU ILE ARG SER LYS ILE ALA SER VAL
SEQRES   2 W  286  GLN ASN THR GLN LYS ILE THR LYS ALA MET GLU MET VAL
SEQRES   3 W  286  ALA ALA SER LYS MET ARG LYS SER GLN ASP ARG MET ALA
SEQRES   4 W  286  ALA SER ARG PRO TYR ALA GLU THR MET ARG LYS VAL ILE
SEQRES   5 W  286  GLY HIS LEU ALA HIS GLY ASN LEU GLU TYR LYS HIS PRO
SEQRES   6 W  286  TYR LEU GLU ASP ARG ASP VAL LYS ARG VAL GLY TYR LEU
SEQRES   7 W  286  VAL VAL SER THR ASP ARG GLY LEU CYS GLY GLY LEU ASN
SEQRES   8 W  286  ILE ASN LEU PHE LYS LYS LEU LEU ALA GLU MET LYS THR
SEQRES   9 W  286  TRP THR ASP LYS GLY VAL GLN CYS ASP LEU ALA MET ILE
SEQRES  10 W  286  GLY SER LYS GLY VAL SER PHE PHE ASN SER VAL GLY GLY
SEQRES  11 W  286  ASN VAL VAL ALA GLN VAL THR GLY MET GLY ASP ASN PRO
SEQRES  12 W  286  SER LEU SER GLU LEU ILE GLY PRO VAL LYS VAL MET LEU
SEQRES  13 W  286  GLN ALA TYR ASP GLU GLY ARG LEU ASP LYS LEU TYR ILE
SEQRES  14 W  286  VAL SER ASN LYS PHE ILE ASN THR MET SER GLN VAL PRO
SEQRES  15 W  286  THR ILE SER GLN LEU LEU PRO LEU PRO ALA SER ASP ASP
SEQRES  16 W  286  ASP ASP LEU LYS HIS LYS SER TRP ASP TYR LEU TYR GLU
SEQRES  17 W  286  PRO ASP PRO LYS ALA LEU LEU ASP THR LEU LEU ARG ARG
SEQRES  18 W  286  TYR VAL GLU SER GLN VAL TYR GLN GLY VAL VAL GLU ASN
SEQRES  19 W  286  LEU ALA SER GLU GLN ALA ALA ARG MET VAL ALA MET LYS
SEQRES  20 W  286  ALA ALA THR ASP ASN GLY GLY SER LEU ILE LYS GLU LEU
SEQRES  21 W  286  GLN LEU VAL TYR ASN LYS ALA ARG GLN ALA SER ILE THR
SEQRES  22 W  286  GLN GLU LEU THR GLU ILE VAL SER GLY ALA ALA ALA VAL
SEQRES   1 X  138  ALA MET THR TYR HIS LEU ASP VAL VAL SER ALA GLU GLN
SEQRES   2 X  138  GLN MET PHE SER GLY LEU VAL GLU LYS ILE GLN VAL THR
SEQRES   3 X  138  GLY SER GLU GLY GLU LEU GLY ILE TYR PRO GLY HIS ALA
SEQRES   4 X  138  PRO LEU LEU THR ALA ILE LYS PRO GLY MET ILE ARG ILE
SEQRES   5 X  138  VAL LYS GLN HIS GLY HIS GLU GLU PHE ILE TYR LEU SER
SEQRES   6 X  138  GLY GLY ILE LEU GLU VAL GLN PRO GLY ASN VAL THR VAL
SEQRES   7 X  138  LEU ALA ASP THR ALA ILE ARG GLY GLN ASP LEU ASP GLU
SEQRES   8 X  138  ALA ARG ALA MET GLU ALA LYS ARG LYS ALA GLU GLU HIS
SEQRES   9 X  138  ILE SER SER SER HIS GLY ASP VAL ASP TYR ALA GLN ALA
SEQRES  10 X  138  SER ALA GLU LEU ALA LYS ALA ILE ALA GLN LEU ARG VAL
SEQRES  11 X  138  ILE GLU LEU THR LYS LYS ALA MET
SEQRES   1 Y  513  MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES   2 Y  513  GLN ARG ILE ALA GLN PHE ASN VAL VAL SER GLU ALA HIS
SEQRES   3 Y  513  ASN GLU GLY THR ILE VAL SER VAL SER ASP GLY VAL ILE
SEQRES   4 Y  513  ARG ILE HIS GLY LEU ALA ASP CYS MET GLN GLY GLU MET
SEQRES   5 Y  513  ILE SER LEU PRO GLY ASN ARG TYR ALA ILE ALA LEU ASN
SEQRES   6 Y  513  LEU GLU ARG ASP SER VAL GLY ALA VAL VAL MET GLY PRO
SEQRES   7 Y  513  TYR ALA ASP LEU ALA GLU GLY MET LYS VAL LYS CYS THR
SEQRES   8 Y  513  GLY ARG ILE LEU GLU VAL PRO VAL GLY ARG GLY LEU LEU
SEQRES   9 Y  513  GLY ARG VAL VAL ASN THR LEU GLY ALA PRO ILE ASP GLY
SEQRES  10 Y  513  LYS GLY PRO LEU ASP HIS ASP GLY PHE SER ALA VAL GLU
SEQRES  11 Y  513  ALA ILE ALA PRO GLY VAL ILE GLU ARG GLN SER VAL ASP
SEQRES  12 Y  513  GLN PRO VAL GLN THR GLY TYR LYS ALA VAL ASP SER MET
SEQRES  13 Y  513  ILE PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES  14 Y  513  ASP ARG GLN THR GLY LYS THR ALA LEU ALA ILE ASP ALA
SEQRES  15 Y  513  ILE ILE ASN GLN ARG ASP SER GLY ILE LYS CYS ILE TYR
SEQRES  16 Y  513  VAL ALA ILE GLY GLN LYS ALA SER THR ILE SER ASN VAL
SEQRES  17 Y  513  VAL ARG LYS LEU GLU GLU HIS GLY ALA LEU ALA ASN THR
SEQRES  18 Y  513  ILE VAL VAL VAL ALA THR ALA SER GLU SER ALA ALA LEU
SEQRES  19 Y  513  GLN TYR LEU ALA PRO TYR ALA GLY CYS ALA MET GLY GLU
SEQRES  20 Y  513  TYR PHE ARG ASP ARG GLY GLU ASP ALA LEU ILE ILE TYR
SEQRES  21 Y  513  ASP ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN ILE
SEQRES  22 Y  513  SER LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA PHE
SEQRES  23 Y  513  PRO GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU
SEQRES  24 Y  513  ARG ALA ALA ARG VAL ASN ALA GLU TYR VAL GLU ALA PHE
SEQRES  25 Y  513  THR LYS GLY GLU VAL LYS GLY LYS THR GLY SER LEU THR
SEQRES  26 Y  513  ALA LEU PRO ILE ILE GLU THR GLN ALA GLY ASP VAL SER
SEQRES  27 Y  513  ALA PHE VAL PRO THR ASN VAL ILE SER ILE THR ASP GLY
SEQRES  28 Y  513  GLN ILE PHE LEU GLU THR ASN LEU PHE ASN ALA GLY ILE
SEQRES  29 Y  513  ARG PRO ALA VAL ASN PRO GLY ILE SER VAL SER ARG VAL
SEQRES  30 Y  513  GLY GLY ALA ALA GLN THR LYS ILE MET LYS LYS LEU SER
SEQRES  31 Y  513  GLY GLY ILE ARG THR ALA LEU ALA GLN TYR ARG GLU LEU
SEQRES  32 Y  513  ALA ALA PHE SER GLN PHE ALA SER ASP LEU ASP ASP ALA
SEQRES  33 Y  513  THR ARG LYS GLN LEU ASP HIS GLY GLN LYS VAL THR GLU
SEQRES  34 Y  513  LEU LEU LYS GLN LYS GLN TYR ALA PRO MET SER VAL ALA
SEQRES  35 Y  513  GLN GLN SER LEU VAL LEU PHE ALA ALA GLU ARG GLY TYR
SEQRES  36 Y  513  LEU ALA ASP VAL GLU LEU SER LYS ILE GLY SER PHE GLU
SEQRES  37 Y  513  ALA ALA LEU LEU ALA TYR VAL ASP ARG ASP HIS ALA PRO
SEQRES  38 Y  513  LEU MET GLN GLU ILE ASN GLN THR GLY GLY TYR ASN ASP
SEQRES  39 Y  513  GLU ILE GLU GLY LYS LEU LYS GLY ILE LEU ASP SER PHE
SEQRES  40 Y  513  LYS ALA THR GLN SER TRP
SEQRES   1 Z  513  MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES   2 Z  513  GLN ARG ILE ALA GLN PHE ASN VAL VAL SER GLU ALA HIS
SEQRES   3 Z  513  ASN GLU GLY THR ILE VAL SER VAL SER ASP GLY VAL ILE
SEQRES   4 Z  513  ARG ILE HIS GLY LEU ALA ASP CYS MET GLN GLY GLU MET
SEQRES   5 Z  513  ILE SER LEU PRO GLY ASN ARG TYR ALA ILE ALA LEU ASN
SEQRES   6 Z  513  LEU GLU ARG ASP SER VAL GLY ALA VAL VAL MET GLY PRO
SEQRES   7 Z  513  TYR ALA ASP LEU ALA GLU GLY MET LYS VAL LYS CYS THR
SEQRES   8 Z  513  GLY ARG ILE LEU GLU VAL PRO VAL GLY ARG GLY LEU LEU
SEQRES   9 Z  513  GLY ARG VAL VAL ASN THR LEU GLY ALA PRO ILE ASP GLY
SEQRES  10 Z  513  LYS GLY PRO LEU ASP HIS ASP GLY PHE SER ALA VAL GLU
SEQRES  11 Z  513  ALA ILE ALA PRO GLY VAL ILE GLU ARG GLN SER VAL ASP
SEQRES  12 Z  513  GLN PRO VAL GLN THR GLY TYR LYS ALA VAL ASP SER MET
SEQRES  13 Z  513  ILE PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES  14 Z  513  ASP ARG GLN THR GLY LYS THR ALA LEU ALA ILE ASP ALA
SEQRES  15 Z  513  ILE ILE ASN GLN ARG ASP SER GLY ILE LYS CYS ILE TYR
SEQRES  16 Z  513  VAL ALA ILE GLY GLN LYS ALA SER THR ILE SER ASN VAL
SEQRES  17 Z  513  VAL ARG LYS LEU GLU GLU HIS GLY ALA LEU ALA ASN THR
SEQRES  18 Z  513  ILE VAL VAL VAL ALA THR ALA SER GLU SER ALA ALA LEU
SEQRES  19 Z  513  GLN TYR LEU ALA PRO TYR ALA GLY CYS ALA MET GLY GLU
SEQRES  20 Z  513  TYR PHE ARG ASP ARG GLY GLU ASP ALA LEU ILE ILE TYR
SEQRES  21 Z  513  ASP ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN ILE
SEQRES  22 Z  513  SER LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA PHE
SEQRES  23 Z  513  PRO GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU
SEQRES  24 Z  513  ARG ALA ALA ARG VAL ASN ALA GLU TYR VAL GLU ALA PHE
SEQRES  25 Z  513  THR LYS GLY GLU VAL LYS GLY LYS THR GLY SER LEU THR
SEQRES  26 Z  513  ALA LEU PRO ILE ILE GLU THR GLN ALA GLY ASP VAL SER
SEQRES  27 Z  513  ALA PHE VAL PRO THR ASN VAL ILE SER ILE THR ASP GLY
SEQRES  28 Z  513  GLN ILE PHE LEU GLU THR ASN LEU PHE ASN ALA GLY ILE
SEQRES  29 Z  513  ARG PRO ALA VAL ASN PRO GLY ILE SER VAL SER ARG VAL
SEQRES  30 Z  513  GLY GLY ALA ALA GLN THR LYS ILE MET LYS LYS LEU SER
SEQRES  31 Z  513  GLY GLY ILE ARG THR ALA LEU ALA GLN TYR ARG GLU LEU
SEQRES  32 Z  513  ALA ALA PHE SER GLN PHE ALA SER ASP LEU ASP ASP ALA
SEQRES  33 Z  513  THR ARG LYS GLN LEU ASP HIS GLY GLN LYS VAL THR GLU
SEQRES  34 Z  513  LEU LEU LYS GLN LYS GLN TYR ALA PRO MET SER VAL ALA
SEQRES  35 Z  513  GLN GLN SER LEU VAL LEU PHE ALA ALA GLU ARG GLY TYR
SEQRES  36 Z  513  LEU ALA ASP VAL GLU LEU SER LYS ILE GLY SER PHE GLU
SEQRES  37 Z  513  ALA ALA LEU LEU ALA TYR VAL ASP ARG ASP HIS ALA PRO
SEQRES  38 Z  513  LEU MET GLN GLU ILE ASN GLN THR GLY GLY TYR ASN ASP
SEQRES  39 Z  513  GLU ILE GLU GLY LYS LEU LYS GLY ILE LEU ASP SER PHE
SEQRES  40 Z  513  LYS ALA THR GLN SER TRP
SEQRES   1 a  513  MET GLN LEU ASN SER THR GLU ILE SER GLU LEU ILE LYS
SEQRES   2 a  513  GLN ARG ILE ALA GLN PHE ASN VAL VAL SER GLU ALA HIS
SEQRES   3 a  513  ASN GLU GLY THR ILE VAL SER VAL SER ASP GLY VAL ILE
SEQRES   4 a  513  ARG ILE HIS GLY LEU ALA ASP CYS MET GLN GLY GLU MET
SEQRES   5 a  513  ILE SER LEU PRO GLY ASN ARG TYR ALA ILE ALA LEU ASN
SEQRES   6 a  513  LEU GLU ARG ASP SER VAL GLY ALA VAL VAL MET GLY PRO
SEQRES   7 a  513  TYR ALA ASP LEU ALA GLU GLY MET LYS VAL LYS CYS THR
SEQRES   8 a  513  GLY ARG ILE LEU GLU VAL PRO VAL GLY ARG GLY LEU LEU
SEQRES   9 a  513  GLY ARG VAL VAL ASN THR LEU GLY ALA PRO ILE ASP GLY
SEQRES  10 a  513  LYS GLY PRO LEU ASP HIS ASP GLY PHE SER ALA VAL GLU
SEQRES  11 a  513  ALA ILE ALA PRO GLY VAL ILE GLU ARG GLN SER VAL ASP
SEQRES  12 a  513  GLN PRO VAL GLN THR GLY TYR LYS ALA VAL ASP SER MET
SEQRES  13 a  513  ILE PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES  14 a  513  ASP ARG GLN THR GLY LYS THR ALA LEU ALA ILE ASP ALA
SEQRES  15 a  513  ILE ILE ASN GLN ARG ASP SER GLY ILE LYS CYS ILE TYR
SEQRES  16 a  513  VAL ALA ILE GLY GLN LYS ALA SER THR ILE SER ASN VAL
SEQRES  17 a  513  VAL ARG LYS LEU GLU GLU HIS GLY ALA LEU ALA ASN THR
SEQRES  18 a  513  ILE VAL VAL VAL ALA THR ALA SER GLU SER ALA ALA LEU
SEQRES  19 a  513  GLN TYR LEU ALA PRO TYR ALA GLY CYS ALA MET GLY GLU
SEQRES  20 a  513  TYR PHE ARG ASP ARG GLY GLU ASP ALA LEU ILE ILE TYR
SEQRES  21 a  513  ASP ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN ILE
SEQRES  22 a  513  SER LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA PHE
SEQRES  23 a  513  PRO GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU
SEQRES  24 a  513  ARG ALA ALA ARG VAL ASN ALA GLU TYR VAL GLU ALA PHE
SEQRES  25 a  513  THR LYS GLY GLU VAL LYS GLY LYS THR GLY SER LEU THR
SEQRES  26 a  513  ALA LEU PRO ILE ILE GLU THR GLN ALA GLY ASP VAL SER
SEQRES  27 a  513  ALA PHE VAL PRO THR ASN VAL ILE SER ILE THR ASP GLY
SEQRES  28 a  513  GLN ILE PHE LEU GLU THR ASN LEU PHE ASN ALA GLY ILE
SEQRES  29 a  513  ARG PRO ALA VAL ASN PRO GLY ILE SER VAL SER ARG VAL
SEQRES  30 a  513  GLY GLY ALA ALA GLN THR LYS ILE MET LYS LYS LEU SER
SEQRES  31 a  513  GLY GLY ILE ARG THR ALA LEU ALA GLN TYR ARG GLU LEU
SEQRES  32 a  513  ALA ALA PHE SER GLN PHE ALA SER ASP LEU ASP ASP ALA
SEQRES  33 a  513  THR ARG LYS GLN LEU ASP HIS GLY GLN LYS VAL THR GLU
SEQRES  34 a  513  LEU LEU LYS GLN LYS GLN TYR ALA PRO MET SER VAL ALA
SEQRES  35 a  513  GLN GLN SER LEU VAL LEU PHE ALA ALA GLU ARG GLY TYR
SEQRES  36 a  513  LEU ALA ASP VAL GLU LEU SER LYS ILE GLY SER PHE GLU
SEQRES  37 a  513  ALA ALA LEU LEU ALA TYR VAL ASP ARG ASP HIS ALA PRO
SEQRES  38 a  513  LEU MET GLN GLU ILE ASN GLN THR GLY GLY TYR ASN ASP
SEQRES  39 a  513  GLU ILE GLU GLY LYS LEU LYS GLY ILE LEU ASP SER PHE
SEQRES  40 a  513  LYS ALA THR GLN SER TRP
SEQRES   1 b  459  ALA THR GLY LYS ILE VAL GLN VAL ILE GLY ALA VAL VAL
SEQRES   2 b  459  ASP VAL GLU PHE PRO GLN ASP ALA VAL PRO ARG VAL TYR
SEQRES   3 b  459  ASP ALA LEU GLU VAL GLN ASN GLY ASN GLU ARG LEU VAL
SEQRES   4 b  459  LEU GLU VAL GLN GLN GLN LEU GLY GLY GLY ILE VAL ARG
SEQRES   5 b  459  THR ILE ALA MET GLY SER SER ASP GLY LEU ARG ARG GLY
SEQRES   6 b  459  LEU ASP VAL LYS ASP LEU GLU HIS PRO ILE GLU VAL PRO
SEQRES   7 b  459  VAL GLY GLU ALA THR LEU GLY ARG ILE MET ASN VAL LEU
SEQRES   8 b  459  GLY GLU PRO VAL ASP MET LYS GLY GLU ILE GLY GLU GLU
SEQRES   9 b  459  GLU ARG TRP ALA ILE HIS ARG ALA ALA PRO SER TYR GLU
SEQRES  10 b  459  GLU LEU SER ASN SER GLN GLU LEU LEU GLU THR GLY ILE
SEQRES  11 b  459  LYS VAL ILE ASP LEU MET CYS PRO PHE ALA LYS GLY GLY
SEQRES  12 b  459  LYS VAL GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR
SEQRES  13 b  459  VAL ASN MET MET GLU LEU ILE ARG ASN ILE ALA ILE GLU
SEQRES  14 b  459  HIS SER GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG
SEQRES  15 b  459  THR ARG GLU GLY ASN ASP PHE TYR HIS GLU MET THR ASP
SEQRES  16 b  459  SER ASN VAL ILE ASP LYS VAL SER LEU VAL TYR GLY GLN
SEQRES  17 b  459  MET ASN GLU PRO PRO GLY ASN ARG LEU ARG VAL ALA LEU
SEQRES  18 b  459  THR GLY LEU THR MET ALA GLU LYS PHE ARG ASP GLU GLY
SEQRES  19 b  459  ARG ASP VAL LEU LEU PHE VAL ASP ASN ILE TYR ARG TYR
SEQRES  20 b  459  THR LEU ALA GLY THR GLU VAL SER ALA LEU LEU GLY ARG
SEQRES  21 b  459  MET PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA GLU
SEQRES  22 b  459  GLU MET GLY VAL LEU GLN GLU ARG ILE THR SER THR LYS
SEQRES  23 b  459  THR GLY SER ILE THR SER VAL GLN ALA VAL TYR VAL PRO
SEQRES  24 b  459  ALA ASP ASP LEU THR ASP PRO SER PRO ALA THR THR PHE
SEQRES  25 b  459  ALA HIS LEU ASP ALA THR VAL VAL LEU SER ARG GLN ILE
SEQRES  26 b  459  ALA SER LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP
SEQRES  27 b  459  SER THR SER ARG GLN LEU ASP PRO LEU VAL VAL GLY GLN
SEQRES  28 b  459  GLU HIS TYR ASP THR ALA ARG GLY VAL GLN SER ILE LEU
SEQRES  29 b  459  GLN ARG TYR GLN GLU LEU LYS ASP ILE ILE ALA ILE LEU
SEQRES  30 b  459  GLY MET ASP GLU LEU SER GLU GLU ASP LYS LEU VAL VAL
SEQRES  31 b  459  ALA ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO
SEQRES  32 b  459  PHE PHE VAL ALA GLU VAL PHE THR GLY SER PRO GLY LYS
SEQRES  33 b  459  TYR VAL SER LEU LYS ASP THR ILE ARG GLY PHE LYS GLY
SEQRES  34 b  459  ILE MET GLU GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA
SEQRES  35 b  459  PHE TYR MET VAL GLY SER ILE GLU GLU ALA VAL GLU LYS
SEQRES  36 b  459  ALA LYS LYS LEU
SEQRES   1 c  459  ALA THR GLY LYS ILE VAL GLN VAL ILE GLY ALA VAL VAL
SEQRES   2 c  459  ASP VAL GLU PHE PRO GLN ASP ALA VAL PRO ARG VAL TYR
SEQRES   3 c  459  ASP ALA LEU GLU VAL GLN ASN GLY ASN GLU ARG LEU VAL
SEQRES   4 c  459  LEU GLU VAL GLN GLN GLN LEU GLY GLY GLY ILE VAL ARG
SEQRES   5 c  459  THR ILE ALA MET GLY SER SER ASP GLY LEU ARG ARG GLY
SEQRES   6 c  459  LEU ASP VAL LYS ASP LEU GLU HIS PRO ILE GLU VAL PRO
SEQRES   7 c  459  VAL GLY GLU ALA THR LEU GLY ARG ILE MET ASN VAL LEU
SEQRES   8 c  459  GLY GLU PRO VAL ASP MET LYS GLY GLU ILE GLY GLU GLU
SEQRES   9 c  459  GLU ARG TRP ALA ILE HIS ARG ALA ALA PRO SER TYR GLU
SEQRES  10 c  459  GLU LEU SER ASN SER GLN GLU LEU LEU GLU THR GLY ILE
SEQRES  11 c  459  LYS VAL ILE ASP LEU MET CYS PRO PHE ALA LYS GLY GLY
SEQRES  12 c  459  LYS VAL GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR
SEQRES  13 c  459  VAL ASN MET MET GLU LEU ILE ARG ASN ILE ALA ILE GLU
SEQRES  14 c  459  HIS SER GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG
SEQRES  15 c  459  THR ARG GLU GLY ASN ASP PHE TYR HIS GLU MET THR ASP
SEQRES  16 c  459  SER ASN VAL ILE ASP LYS VAL SER LEU VAL TYR GLY GLN
SEQRES  17 c  459  MET ASN GLU PRO PRO GLY ASN ARG LEU ARG VAL ALA LEU
SEQRES  18 c  459  THR GLY LEU THR MET ALA GLU LYS PHE ARG ASP GLU GLY
SEQRES  19 c  459  ARG ASP VAL LEU LEU PHE VAL ASP ASN ILE TYR ARG TYR
SEQRES  20 c  459  THR LEU ALA GLY THR GLU VAL SER ALA LEU LEU GLY ARG
SEQRES  21 c  459  MET PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA GLU
SEQRES  22 c  459  GLU MET GLY VAL LEU GLN GLU ARG ILE THR SER THR LYS
SEQRES  23 c  459  THR GLY SER ILE THR SER VAL GLN ALA VAL TYR VAL PRO
SEQRES  24 c  459  ALA ASP ASP LEU THR ASP PRO SER PRO ALA THR THR PHE
SEQRES  25 c  459  ALA HIS LEU ASP ALA THR VAL VAL LEU SER ARG GLN ILE
SEQRES  26 c  459  ALA SER LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP
SEQRES  27 c  459  SER THR SER ARG GLN LEU ASP PRO LEU VAL VAL GLY GLN
SEQRES  28 c  459  GLU HIS TYR ASP THR ALA ARG GLY VAL GLN SER ILE LEU
SEQRES  29 c  459  GLN ARG TYR GLN GLU LEU LYS ASP ILE ILE ALA ILE LEU
SEQRES  30 c  459  GLY MET ASP GLU LEU SER GLU GLU ASP LYS LEU VAL VAL
SEQRES  31 c  459  ALA ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO
SEQRES  32 c  459  PHE PHE VAL ALA GLU VAL PHE THR GLY SER PRO GLY LYS
SEQRES  33 c  459  TYR VAL SER LEU LYS ASP THR ILE ARG GLY PHE LYS GLY
SEQRES  34 c  459  ILE MET GLU GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA
SEQRES  35 c  459  PHE TYR MET VAL GLY SER ILE GLU GLU ALA VAL GLU LYS
SEQRES  36 c  459  ALA LYS LYS LEU
SEQRES   1 d  459  ALA THR GLY LYS ILE VAL GLN VAL ILE GLY ALA VAL VAL
SEQRES   2 d  459  ASP VAL GLU PHE PRO GLN ASP ALA VAL PRO ARG VAL TYR
SEQRES   3 d  459  ASP ALA LEU GLU VAL GLN ASN GLY ASN GLU ARG LEU VAL
SEQRES   4 d  459  LEU GLU VAL GLN GLN GLN LEU GLY GLY GLY ILE VAL ARG
SEQRES   5 d  459  THR ILE ALA MET GLY SER SER ASP GLY LEU ARG ARG GLY
SEQRES   6 d  459  LEU ASP VAL LYS ASP LEU GLU HIS PRO ILE GLU VAL PRO
SEQRES   7 d  459  VAL GLY GLU ALA THR LEU GLY ARG ILE MET ASN VAL LEU
SEQRES   8 d  459  GLY GLU PRO VAL ASP MET LYS GLY GLU ILE GLY GLU GLU
SEQRES   9 d  459  GLU ARG TRP ALA ILE HIS ARG ALA ALA PRO SER TYR GLU
SEQRES  10 d  459  GLU LEU SER ASN SER GLN GLU LEU LEU GLU THR GLY ILE
SEQRES  11 d  459  LYS VAL ILE ASP LEU MET CYS PRO PHE ALA LYS GLY GLY
SEQRES  12 d  459  LYS VAL GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR
SEQRES  13 d  459  VAL ASN MET MET GLU LEU ILE ARG ASN ILE ALA ILE GLU
SEQRES  14 d  459  HIS SER GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG
SEQRES  15 d  459  THR ARG GLU GLY ASN ASP PHE TYR HIS GLU MET THR ASP
SEQRES  16 d  459  SER ASN VAL ILE ASP LYS VAL SER LEU VAL TYR GLY GLN
SEQRES  17 d  459  MET ASN GLU PRO PRO GLY ASN ARG LEU ARG VAL ALA LEU
SEQRES  18 d  459  THR GLY LEU THR MET ALA GLU LYS PHE ARG ASP GLU GLY
SEQRES  19 d  459  ARG ASP VAL LEU LEU PHE VAL ASP ASN ILE TYR ARG TYR
SEQRES  20 d  459  THR LEU ALA GLY THR GLU VAL SER ALA LEU LEU GLY ARG
SEQRES  21 d  459  MET PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA GLU
SEQRES  22 d  459  GLU MET GLY VAL LEU GLN GLU ARG ILE THR SER THR LYS
SEQRES  23 d  459  THR GLY SER ILE THR SER VAL GLN ALA VAL TYR VAL PRO
SEQRES  24 d  459  ALA ASP ASP LEU THR ASP PRO SER PRO ALA THR THR PHE
SEQRES  25 d  459  ALA HIS LEU ASP ALA THR VAL VAL LEU SER ARG GLN ILE
SEQRES  26 d  459  ALA SER LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP
SEQRES  27 d  459  SER THR SER ARG GLN LEU ASP PRO LEU VAL VAL GLY GLN
SEQRES  28 d  459  GLU HIS TYR ASP THR ALA ARG GLY VAL GLN SER ILE LEU
SEQRES  29 d  459  GLN ARG TYR GLN GLU LEU LYS ASP ILE ILE ALA ILE LEU
SEQRES  30 d  459  GLY MET ASP GLU LEU SER GLU GLU ASP LYS LEU VAL VAL
SEQRES  31 d  459  ALA ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO
SEQRES  32 d  459  PHE PHE VAL ALA GLU VAL PHE THR GLY SER PRO GLY LYS
SEQRES  33 d  459  TYR VAL SER LEU LYS ASP THR ILE ARG GLY PHE LYS GLY
SEQRES  34 d  459  ILE MET GLU GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA
SEQRES  35 d  459  PHE TYR MET VAL GLY SER ILE GLU GLU ALA VAL GLU LYS
SEQRES  36 d  459  ALA LYS LYS LEU
SEQRES   1 e  286  ALA GLY ALA LYS GLU ILE ARG SER LYS ILE ALA SER VAL
SEQRES   2 e  286  GLN ASN THR GLN LYS ILE THR LYS ALA MET GLU MET VAL
SEQRES   3 e  286  ALA ALA SER LYS MET ARG LYS SER GLN ASP ARG MET ALA
SEQRES   4 e  286  ALA SER ARG PRO TYR ALA GLU THR MET ARG LYS VAL ILE
SEQRES   5 e  286  GLY HIS LEU ALA HIS GLY ASN LEU GLU TYR LYS HIS PRO
SEQRES   6 e  286  TYR LEU GLU ASP ARG ASP VAL LYS ARG VAL GLY TYR LEU
SEQRES   7 e  286  VAL VAL SER THR ASP ARG GLY LEU CYS GLY GLY LEU ASN
SEQRES   8 e  286  ILE ASN LEU PHE LYS LYS LEU LEU ALA GLU MET LYS THR
SEQRES   9 e  286  TRP THR ASP LYS GLY VAL GLN CYS ASP LEU ALA MET ILE
SEQRES  10 e  286  GLY SER LYS GLY VAL SER PHE PHE ASN SER VAL GLY GLY
SEQRES  11 e  286  ASN VAL VAL ALA GLN VAL THR GLY MET GLY ASP ASN PRO
SEQRES  12 e  286  SER LEU SER GLU LEU ILE GLY PRO VAL LYS VAL MET LEU
SEQRES  13 e  286  GLN ALA TYR ASP GLU GLY ARG LEU ASP LYS LEU TYR ILE
SEQRES  14 e  286  VAL SER ASN LYS PHE ILE ASN THR MET SER GLN VAL PRO
SEQRES  15 e  286  THR ILE SER GLN LEU LEU PRO LEU PRO ALA SER ASP ASP
SEQRES  16 e  286  ASP ASP LEU LYS HIS LYS SER TRP ASP TYR LEU TYR GLU
SEQRES  17 e  286  PRO ASP PRO LYS ALA LEU LEU ASP THR LEU LEU ARG ARG
SEQRES  18 e  286  TYR VAL GLU SER GLN VAL TYR GLN GLY VAL VAL GLU ASN
SEQRES  19 e  286  LEU ALA SER GLU GLN ALA ALA ARG MET VAL ALA MET LYS
SEQRES  20 e  286  ALA ALA THR ASP ASN GLY GLY SER LEU ILE LYS GLU LEU
SEQRES  21 e  286  GLN LEU VAL TYR ASN LYS ALA ARG GLN ALA SER ILE THR
SEQRES  22 e  286  GLN GLU LEU THR GLU ILE VAL SER GLY ALA ALA ALA VAL
SEQRES   1 f  138  ALA MET THR TYR HIS LEU ASP VAL VAL SER ALA GLU GLN
SEQRES   2 f  138  GLN MET PHE SER GLY LEU VAL GLU LYS ILE GLN VAL THR
SEQRES   3 f  138  GLY SER GLU GLY GLU LEU GLY ILE TYR PRO GLY HIS ALA
SEQRES   4 f  138  PRO LEU LEU THR ALA ILE LYS PRO GLY MET ILE ARG ILE
SEQRES   5 f  138  VAL LYS GLN HIS GLY HIS GLU GLU PHE ILE TYR LEU SER
SEQRES   6 f  138  GLY GLY ILE LEU GLU VAL GLN PRO GLY ASN VAL THR VAL
SEQRES   7 f  138  LEU ALA ASP THR ALA ILE ARG GLY GLN ASP LEU ASP GLU
SEQRES   8 f  138  ALA ARG ALA MET GLU ALA LYS ARG LYS ALA GLU GLU HIS
SEQRES   9 f  138  ILE SER SER SER HIS GLY ASP VAL ASP TYR ALA GLN ALA
SEQRES  10 f  138  SER ALA GLU LEU ALA LYS ALA ILE ALA GLN LEU ARG VAL
SEQRES  11 f  138  ILE GLU LEU THR LYS LYS ALA MET
HET    ANP  A 600      31
HET     MG  A 601       1
HET    ANP  B 600      31
HET     MG  B 601       1
HET    ANP  C 600      31
HET     MG  C 601       1
HET    ADP  D 600      27
HET     MG  D 601       1
HET    SO4  D 630       5
HET    SO4  E 530       5
HET    SO4  F 530       5
HET    SO4  G 300       5
HET    SO4  H 200       5
HET    ANP  I 600      31
HET     MG  I 601       1
HET    ANP  J 600      31
HET     MG  J 601       1
HET    ANP  K 600      31
HET     MG  K 601       1
HET    ADP  L 600      27
HET     MG  L 601       1
HET    SO4  L 630       5
HET    SO4  M 530       5
HET    SO4  N 530       5
HET    SO4  O 300       5
HET    SO4  P 200       5
HET    ANP  Q 600      31
HET     MG  Q 601       1
HET    ANP  R 600      31
HET     MG  R 601       1
HET    ANP  S 600      31
HET     MG  S 601       1
HET    ADP  T 600      27
HET     MG  T 601       1
HET    SO4  T 630       5
HET    SO4  U 530       5
HET    SO4  V 530       5
HET    SO4  W 300       5
HET    ANP  Y 600      31
HET     MG  Y 601       1
HET    ANP  Z 600      31
HET     MG  Z 601       1
HET    ANP  a 600      31
HET     MG  a 601       1
HET    ADP  b 600      27
HET     MG  b 601       1
HET    SO4  b 630       5
HET    SO4  c 530       5
HET    SO4  d 530       5
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM      MG MAGNESIUM ION
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM     SO4 SULFATE ION
FORMUL  33  ANP    12(C10 H17 N6 O12 P3)
FORMUL  34   MG    16(MG 2+)
FORMUL  39  ADP    4(C10 H15 N5 O10 P2)
FORMUL  41  SO4    17(O4 S 2-)
FORMUL  82  HOH   *64(H2 O)
HELIX    1   1 GLY A  100  LEU A  104  5                                   5
HELIX    2   2 TYR A  150  ILE A  157  1                                   8
HELIX    3   3 GLY A  174  ASN A  185  1                                  12
HELIX    4   4 LYS A  201  GLY A  216  1                                  16
HELIX    5   5 SER A  231  ARG A  252  1                                  22
HELIX    6   6 ASP A  262  LEU A  277  1                                  16
HELIX    7   7 ASP A  289  GLU A  299  1                                  11
HELIX    8   8 ASN A  305  LYS A  314  1                                  10
HELIX    9   9 GLN A  333  ASP A  336  5                                   4
HELIX   10  10 ALA A  339  THR A  349  1                                  11
HELIX   11  11 GLU A  356  ASN A  361  1                                   6
HELIX   12  12 VAL A  377  GLN A  382  5                                   6
HELIX   13  13 THR A  383  GLN A  408  1                                  26
HELIX   14  14 ASP A  414  LEU A  431  1                                  18
HELIX   15  15 ALA A  442  ARG A  453  1                                  12
HELIX   16  16 LEU A  461  ASP A  476  1                                  16
HELIX   17  17 ARG A  477  HIS A  479  5                                   3
HELIX   18  18 ALA A  480  GLY A  490  1                                  11
HELIX   19  19 ASN A  493  LYS A  508  1                                  16
HELIX   20  20 TYR B  150  ILE B  157  1                                   8
HELIX   21  21 GLY B  174  ASN B  185  1                                  12
HELIX   22  22 LYS B  201  HIS B  215  1                                  15
HELIX   23  23 SER B  231  ARG B  252  1                                  22
HELIX   24  24 ASP B  262  LEU B  277  1                                  16
HELIX   25  25 GLY B  282  PHE B  286  5                                   5
HELIX   26  26 PRO B  287  GLY B  288  5                                   2
HELIX   27  27 ASP B  289  GLU B  299  1                                  11
HELIX   28  28 ASN B  305  LYS B  314  1                                  10
HELIX   29  29 ALA B  339  THR B  349  1                                  11
HELIX   30  30 GLU B  356  ALA B  362  1                                   7
HELIX   31  31 VAL B  377  GLN B  382  5                                   6
HELIX   32  32 THR B  383  GLN B  399  1                                  17
HELIX   33  33 ALA B  416  LYS B  432  1                                  17
HELIX   34  34 GLN B  443  PHE B  449  1                                   7
HELIX   35  35 GLY B  454  GLU B  460  1                                   7
HELIX   36  36 LEU B  461  ALA B  480  1                                  20
HELIX   37  37 PRO B  481  GLU B  485  5                                   5
HELIX   38  38 ASN B  493  LYS B  508  1                                  16
HELIX   39  39 GLY C  100  LEU C  104  5                                   5
HELIX   40  40 TYR C  150  ILE C  157  1                                   8
HELIX   41  41 GLY C  174  ASN C  185  1                                  12
HELIX   42  42 LYS C  201  HIS C  215  1                                  15
HELIX   43  43 ALA C  217  ALA C  219  5                                   3
HELIX   44  44 SER C  231  ARG C  252  1                                  22
HELIX   45  45 ASP C  262  LEU C  277  1                                  16
HELIX   46  46 GLY C  282  PHE C  286  5                                   5
HELIX   47  47 PRO C  287  GLY C  288  5                                   2
HELIX   48  48 ASP C  289  ARG C  300  1                                  12
HELIX   49  49 ASN C  305  GLU C  310  5                                   6
HELIX   50  50 ALA C  339  THR C  349  1                                  11
HELIX   51  51 GLU C  356  GLY C  363  1                                   8
HELIX   52  52 VAL C  377  GLN C  382  5                                   6
HELIX   53  53 THR C  383  ALA C  404  1                                  22
HELIX   54  54 ALA C  405  GLN C  408  5                                   4
HELIX   55  55 ASP C  414  LEU C  431  1                                  18
HELIX   56  56 ALA C  442  GLU C  452  1                                  11
HELIX   57  57 LYS C  463  GLU C  468  1                                   6
HELIX   58  58 GLU C  468  ASP C  476  1                                   9
HELIX   59  59 ALA C  480  GLY C  490  1                                  11
HELIX   60  60 ASP C  494  SER C  506  1                                  13
HELIX   61  61 ILE D  130  MET D  136  1                                   7
HELIX   62  62 GLY D  154  GLU D  169  1                                  16
HELIX   63  63 ARG D  182  SER D  196  1                                  15
HELIX   64  64 ASN D  197  ASP D  200  5                                   4
HELIX   65  65 PRO D  212  ARG D  231  1                                  20
HELIX   66  66 ASN D  243  LEU D  258  1                                  16
HELIX   67  67 SER D  263  TYR D  267  5                                   5
HELIX   68  68 THR D  270  ARG D  281  1                                  12
HELIX   69  69 PRO D  299  ASP D  302  5                                   4
HELIX   70  70 ASP D  305  ALA D  313  1                                   9
HELIX   71  71 SER D  322  LEU D  328  1                                   7
HELIX   72  72 ASP D  345  GLY D  350  1                                   6
HELIX   73  73 GLY D  350  LEU D  377  1                                  28
HELIX   74  74 GLY D  378  LEU D  382  5                                   5
HELIX   75  75 GLU D  385  LEU D  400  1                                  16
HELIX   76  76 ALA D  407  GLY D  412  1                                   6
HELIX   77  77 SER D  419  MET D  431  1                                  13
HELIX   78  78 GLU D  432  LEU D  438  5                                   7
HELIX   79  79 PRO D  439  TYR D  444  5                                   6
HELIX   80  80 SER D  448  LEU D  459  1                                  12
HELIX   81  81 PRO E   18  VAL E   22  5                                   5
HELIX   82  82 ILE E  130  CYS E  137  1                                   8
HELIX   83  83 GLY E  154  GLU E  169  1                                  16
HELIX   84  84 ARG E  182  SER E  196  1                                  15
HELIX   85  85 VAL E  198  ASP E  200  5                                   3
HELIX   86  86 PRO E  212  GLU E  233  1                                  22
HELIX   87  87 ASN E  243  LEU E  258  1                                  16
HELIX   88  88 SER E  263  TYR E  267  5                                   5
HELIX   89  89 THR E  270  ARG E  281  1                                  12
HELIX   90  90 VAL E  298  ASP E  302  5                                   5
HELIX   91  91 ASP E  305  ALA E  313  1                                   9
HELIX   92  92 SER E  322  GLY E  329  1                                   8
HELIX   93  93 GLY E  350  LEU E  370  1                                  21
HELIX   94  94 LYS E  371  ILE E  376  1                                   6
HELIX   95  95 GLY E  378  LEU E  382  5                                   5
HELIX   96  96 SER E  383  LEU E  388  1                                   6
HELIX   97  97 LEU E  388  LEU E  400  1                                  13
HELIX   98  98 SER E  419  GLU E  432  1                                  14
HELIX   99  99 PRO E  439  TYR E  444  5                                   6
HELIX  100 100 SER E  448  LEU E  459  1                                  12
HELIX  101 101 PRO F   18  VAL F   22  5                                   5
HELIX  102 102 GLY F   80  LEU F   84  5                                   5
HELIX  103 103 ILE F  130  CYS F  137  1                                   8
HELIX  104 104 GLY F  154  ALA F  167  1                                  14
HELIX  105 105 ARG F  182  SER F  196  1                                  15
HELIX  106 106 ASN F  197  VAL F  202  5                                   6
HELIX  107 107 PRO F  212  ASP F  232  1                                  21
HELIX  108 108 ASN F  243  ALA F  256  1                                  14
HELIX  109 109 SER F  263  TYR F  267  5                                   5
HELIX  110 110 THR F  270  ILE F  282  1                                  13
HELIX  111 111 VAL F  298  ASP F  302  5                                   5
HELIX  112 112 ASP F  305  PHE F  312  1                                   8
HELIX  113 113 ALA F  313  LEU F  315  5                                   3
HELIX  114 114 SER F  322  SER F  327  1                                   6
HELIX  115 115 ASP F  345  GLY F  378  1                                  34
HELIX  116 116 MET F  379  LEU F  382  5                                   4
HELIX  117 117 SER F  383  LEU F  400  1                                  18
HELIX  118 118 PHE F  405  VAL F  409  5                                   5
HELIX  119 119 SER F  419  GLY F  433  1                                  15
HELIX  120 120 PRO F  439  PHE F  443  5                                   5
HELIX  121 121 SER F  448  LEU F  459  1                                  12
HELIX  122 122 GLY G    2  ALA G   40  1                                  39
HELIX  123 123 SER G   41  LEU G   60  1                                  20
HELIX  124 124 GLY G   89  ASP G  107  1                                  19
HELIX  125 125 GLY G  118  GLY G  129  1                                  12
HELIX  126 126 SER G  144  GLU G  161  1                                  18
HELIX  127 127 SER G  193  LEU G  198  1                                   6
HELIX  128 128 ASP G  210  ALA G  284  1                                  75
HELIX  129 129 GLY H   86  GLU H  103  1                                  18
HELIX  130 130 VAL H  112  ALA H  126  1                                  15
HELIX  131 131 ARG H  129  THR H  134  1                                   6
HELIX  132 132 GLY I  100  LEU I  104  5                                   5
HELIX  133 133 TYR I  150  ILE I  157  1                                   8
HELIX  134 134 GLY I  174  ASN I  185  1                                  12
HELIX  135 135 LYS I  201  GLY I  216  1                                  16
HELIX  136 136 SER I  231  ARG I  252  1                                  22
HELIX  137 137 ASP I  262  LEU I  277  1                                  16
HELIX  138 138 ASP I  289  GLU I  299  1                                  11
HELIX  139 139 ASN I  305  LYS I  314  1                                  10
HELIX  140 140 GLN I  333  ASP I  336  5                                   4
HELIX  141 141 ALA I  339  THR I  349  1                                  11
HELIX  142 142 GLU I  356  ASN I  361  1                                   6
HELIX  143 143 VAL I  377  GLN I  382  5                                   6
HELIX  144 144 THR I  383  GLN I  408  1                                  26
HELIX  145 145 ASP I  414  LEU I  431  1                                  18
HELIX  146 146 ALA I  442  ARG I  453  1                                  12
HELIX  147 147 LEU I  461  ASP I  476  1                                  16
HELIX  148 148 ARG I  477  HIS I  479  5                                   3
HELIX  149 149 ALA I  480  GLY I  490  1                                  11
HELIX  150 150 ASN I  493  LYS I  508  1                                  16
HELIX  151 151 TYR J  150  ILE J  157  1                                   8
HELIX  152 152 GLY J  174  ASN J  185  1                                  12
HELIX  153 153 LYS J  201  HIS J  215  1                                  15
HELIX  154 154 SER J  231  ARG J  252  1                                  22
HELIX  155 155 ASP J  262  LEU J  277  1                                  16
HELIX  156 156 GLY J  282  PHE J  286  5                                   5
HELIX  157 157 PRO J  287  GLY J  288  5                                   2
HELIX  158 158 ASP J  289  GLU J  299  1                                  11
HELIX  159 159 ASN J  305  LYS J  314  1                                  10
HELIX  160 160 ALA J  339  THR J  349  1                                  11
HELIX  161 161 GLU J  356  ALA J  362  1                                   7
HELIX  162 162 VAL J  377  GLN J  382  5                                   6
HELIX  163 163 THR J  383  GLN J  399  1                                  17
HELIX  164 164 ALA J  416  LYS J  432  1                                  17
HELIX  165 165 GLN J  443  PHE J  449  1                                   7
HELIX  166 166 GLY J  454  GLU J  460  1                                   7
HELIX  167 167 LEU J  461  ALA J  480  1                                  20
HELIX  168 168 PRO J  481  GLU J  485  5                                   5
HELIX  169 169 ASN J  493  LYS J  508  1                                  16
HELIX  170 170 GLY K  100  LEU K  104  5                                   5
HELIX  171 171 TYR K  150  ILE K  157  1                                   8
HELIX  172 172 GLY K  174  ASN K  185  1                                  12
HELIX  173 173 LYS K  201  HIS K  215  1                                  15
HELIX  174 174 ALA K  217  ALA K  219  5                                   3
HELIX  175 175 SER K  231  ARG K  252  1                                  22
HELIX  176 176 ASP K  262  LEU K  277  1                                  16
HELIX  177 177 GLY K  282  PHE K  286  5                                   5
HELIX  178 178 PRO K  287  GLY K  288  5                                   2
HELIX  179 179 ASP K  289  ARG K  300  1                                  12
HELIX  180 180 ASN K  305  GLU K  310  5                                   6
HELIX  181 181 ALA K  339  THR K  349  1                                  11
HELIX  182 182 GLU K  356  GLY K  363  1                                   8
HELIX  183 183 VAL K  377  GLN K  382  5                                   6
HELIX  184 184 THR K  383  ALA K  404  1                                  22
HELIX  185 185 ALA K  405  GLN K  408  5                                   4
HELIX  186 186 ASP K  414  LEU K  431  1                                  18
HELIX  187 187 ALA K  442  GLU K  452  1                                  11
HELIX  188 188 LYS K  463  GLU K  468  1                                   6
HELIX  189 189 GLU K  468  ASP K  476  1                                   9
HELIX  190 190 ALA K  480  GLY K  490  1                                  11
HELIX  191 191 ASP K  494  SER K  506  1                                  13
HELIX  192 192 ILE L  130  MET L  136  1                                   7
HELIX  193 193 GLY L  154  GLU L  169  1                                  16
HELIX  194 194 ARG L  182  SER L  196  1                                  15
HELIX  195 195 ASN L  197  ASP L  200  5                                   4
HELIX  196 196 PRO L  212  ARG L  231  1                                  20
HELIX  197 197 ASN L  243  LEU L  258  1                                  16
HELIX  198 198 SER L  263  TYR L  267  5                                   5
HELIX  199 199 THR L  270  ARG L  281  1                                  12
HELIX  200 200 PRO L  299  ASP L  302  5                                   4
HELIX  201 201 ASP L  305  ALA L  313  1                                   9
HELIX  202 202 SER L  322  LEU L  328  1                                   7
HELIX  203 203 ASP L  345  GLY L  350  1                                   6
HELIX  204 204 GLY L  350  LEU L  377  1                                  28
HELIX  205 205 GLY L  378  LEU L  382  5                                   5
HELIX  206 206 GLU L  385  LEU L  400  1                                  16
HELIX  207 207 SER L  419  MET L  431  1                                  13
HELIX  208 208 GLU L  432  LEU L  438  5                                   7
HELIX  209 209 PRO L  439  TYR L  444  5                                   6
HELIX  210 210 SER L  448  LEU L  459  1                                  12
HELIX  211 211 PRO M   18  VAL M   22  5                                   5
HELIX  212 212 ILE M  130  CYS M  137  1                                   8
HELIX  213 213 GLY M  154  GLU M  169  1                                  16
HELIX  214 214 ARG M  182  SER M  196  1                                  15
HELIX  215 215 VAL M  198  ASP M  200  5                                   3
HELIX  216 216 PRO M  212  GLU M  233  1                                  22
HELIX  217 217 ASN M  243  LEU M  258  1                                  16
HELIX  218 218 SER M  263  TYR M  267  5                                   5
HELIX  219 219 THR M  270  ILE M  282  1                                  13
HELIX  220 220 VAL M  298  ASP M  302  5                                   5
HELIX  221 221 ASP M  305  ALA M  313  1                                   9
HELIX  222 222 SER M  322  GLY M  329  1                                   8
HELIX  223 223 GLY M  350  LEU M  370  1                                  21
HELIX  224 224 SER M  383  LEU M  400  1                                  18
HELIX  225 225 SER M  419  GLU M  432  1                                  14
HELIX  226 226 PRO M  439  TYR M  444  5                                   6
HELIX  227 227 SER M  448  LEU M  459  1                                  12
HELIX  228 228 PRO N   18  VAL N   22  5                                   5
HELIX  229 229 GLY N   80  LEU N   84  5                                   5
HELIX  230 230 ILE N  130  CYS N  137  1                                   8
HELIX  231 231 GLY N  154  ALA N  167  1                                  14
HELIX  232 232 ARG N  182  SER N  196  1                                  15
HELIX  233 233 ASN N  197  VAL N  202  5                                   6
HELIX  234 234 PRO N  212  ASP N  232  1                                  21
HELIX  235 235 ASN N  243  ALA N  256  1                                  14
HELIX  236 236 SER N  263  TYR N  267  5                                   5
HELIX  237 237 GLN N  268  PRO N  269  5                                   2
HELIX  238 238 THR N  270  ILE N  282  1                                  13
HELIX  239 239 VAL N  298  ASP N  302  5                                   5
HELIX  240 240 ASP N  305  PHE N  312  1                                   8
HELIX  241 241 ALA N  313  LEU N  315  5                                   3
HELIX  242 242 SER N  322  SER N  327  1                                   6
HELIX  243 243 ASP N  345  GLY N  350  1                                   6
HELIX  244 244 GLY N  350  GLY N  378  1                                  29
HELIX  245 245 MET N  379  LEU N  382  5                                   4
HELIX  246 246 SER N  383  LEU N  400  1                                  18
HELIX  247 247 PHE N  405  THR N  411  5                                   7
HELIX  248 248 SER N  419  GLY N  433  1                                  15
HELIX  249 249 PRO N  439  PHE N  443  5                                   5
HELIX  250 250 SER N  448  LEU N  459  1                                  12
HELIX  251 251 GLY O    2  ALA O   40  1                                  39
HELIX  252 252 SER O   41  LEU O   60  1                                  20
HELIX  253 253 GLY O   89  ASP O  107  1                                  19
HELIX  254 254 GLY O  118  GLY O  129  1                                  12
HELIX  255 255 SER O  144  GLU O  161  1                                  18
HELIX  256 256 SER O  193  LEU O  198  1                                   6
HELIX  257 257 ASP O  210  ALA O  284  1                                  75
HELIX  258 258 GLY P   86  GLU P  103  1                                  18
HELIX  259 259 VAL P  112  ALA P  126  1                                  15
HELIX  260 260 ARG P  129  THR P  134  1                                   6
HELIX  261 261 GLY Q  100  LEU Q  104  5                                   5
HELIX  262 262 TYR Q  150  ILE Q  157  1                                   8
HELIX  263 263 GLY Q  174  ASN Q  185  1                                  12
HELIX  264 264 LYS Q  201  GLY Q  216  1                                  16
HELIX  265 265 SER Q  231  ARG Q  252  1                                  22
HELIX  266 266 ASP Q  262  LEU Q  277  1                                  16
HELIX  267 267 ASP Q  289  GLU Q  299  1                                  11
HELIX  268 268 ASN Q  305  LYS Q  314  1                                  10
HELIX  269 269 GLN Q  333  ASP Q  336  5                                   4
HELIX  270 270 ALA Q  339  THR Q  349  1                                  11
HELIX  271 271 GLU Q  356  ASN Q  361  1                                   6
HELIX  272 272 VAL Q  377  GLN Q  382  5                                   6
HELIX  273 273 THR Q  383  GLN Q  408  1                                  26
HELIX  274 274 ASP Q  414  LEU Q  431  1                                  18
HELIX  275 275 ALA Q  442  ARG Q  453  1                                  12
HELIX  276 276 LEU Q  461  ASP Q  476  1                                  16
HELIX  277 277 ARG Q  477  HIS Q  479  5                                   3
HELIX  278 278 ALA Q  480  GLY Q  490  1                                  11
HELIX  279 279 ASN Q  493  LYS Q  508  1                                  16
HELIX  280 280 TYR R  150  ILE R  157  1                                   8
HELIX  281 281 GLY R  174  ASN R  185  1                                  12
HELIX  282 282 LYS R  201  HIS R  215  1                                  15
HELIX  283 283 SER R  231  ARG R  252  1                                  22
HELIX  284 284 ASP R  262  LEU R  277  1                                  16
HELIX  285 285 GLY R  282  PHE R  286  5                                   5
HELIX  286 286 PRO R  287  GLY R  288  5                                   2
HELIX  287 287 ASP R  289  GLU R  299  1                                  11
HELIX  288 288 ASN R  305  LYS R  314  1                                  10
HELIX  289 289 ALA R  339  THR R  349  1                                  11
HELIX  290 290 GLU R  356  ALA R  362  1                                   7
HELIX  291 291 VAL R  377  GLN R  382  5                                   6
HELIX  292 292 THR R  383  GLN R  399  1                                  17
HELIX  293 293 ALA R  416  LYS R  432  1                                  17
HELIX  294 294 GLN R  443  PHE R  449  1                                   7
HELIX  295 295 GLY R  454  GLU R  460  1                                   7
HELIX  296 296 LEU R  461  ALA R  480  1                                  20
HELIX  297 297 PRO R  481  GLU R  485  5                                   5
HELIX  298 298 ASN R  493  LYS R  508  1                                  16
HELIX  299 299 GLY S  100  LEU S  104  5                                   5
HELIX  300 300 TYR S  150  ILE S  157  1                                   8
HELIX  301 301 GLY S  174  ASN S  185  1                                  12
HELIX  302 302 LYS S  201  HIS S  215  1                                  15
HELIX  303 303 ALA S  217  ALA S  219  5                                   3
HELIX  304 304 SER S  231  ARG S  252  1                                  22
HELIX  305 305 ASP S  262  LEU S  277  1                                  16
HELIX  306 306 GLY S  282  PHE S  286  5                                   5
HELIX  307 307 PRO S  287  GLY S  288  5                                   2
HELIX  308 308 ASP S  289  ARG S  300  1                                  12
HELIX  309 309 ASN S  305  GLU S  310  5                                   6
HELIX  310 310 ALA S  339  THR S  349  1                                  11
HELIX  311 311 GLU S  356  GLY S  363  1                                   8
HELIX  312 312 VAL S  377  GLN S  382  5                                   6
HELIX  313 313 THR S  383  ALA S  404  1                                  22
HELIX  314 314 ALA S  405  GLN S  408  5                                   4
HELIX  315 315 ASP S  414  LEU S  431  1                                  18
HELIX  316 316 ALA S  442  GLU S  452  1                                  11
HELIX  317 317 LYS S  463  GLU S  468  1                                   6
HELIX  318 318 GLU S  468  ASP S  476  1                                   9
HELIX  319 319 ALA S  480  GLY S  490  1                                  11
HELIX  320 320 ASP S  494  SER S  506  1                                  13
HELIX  321 321 ILE T  130  MET T  136  1                                   7
HELIX  322 322 GLY T  154  GLU T  169  1                                  16
HELIX  323 323 ARG T  182  SER T  196  1                                  15
HELIX  324 324 ASN T  197  ASP T  200  5                                   4
HELIX  325 325 PRO T  212  ARG T  231  1                                  20
HELIX  326 326 ASN T  243  LEU T  258  1                                  16
HELIX  327 327 SER T  263  TYR T  267  5                                   5
HELIX  328 328 THR T  270  ARG T  281  1                                  12
HELIX  329 329 PRO T  299  ASP T  302  5                                   4
HELIX  330 330 ASP T  305  ALA T  313  1                                   9
HELIX  331 331 SER T  322  LEU T  328  1                                   7
HELIX  332 332 ASP T  345  GLY T  350  1                                   6
HELIX  333 333 GLY T  350  LEU T  377  1                                  28
HELIX  334 334 GLY T  378  LEU T  382  5                                   5
HELIX  335 335 GLU T  385  LEU T  400  1                                  16
HELIX  336 336 SER T  419  MET T  431  1                                  13
HELIX  337 337 GLU T  432  LEU T  438  5                                   7
HELIX  338 338 PRO T  439  TYR T  444  5                                   6
HELIX  339 339 SER T  448  LEU T  459  1                                  12
HELIX  340 340 PRO U   18  VAL U   22  5                                   5
HELIX  341 341 ILE U  130  CYS U  137  1                                   8
HELIX  342 342 GLY U  154  GLU U  169  1                                  16
HELIX  343 343 ARG U  182  SER U  196  1                                  15
HELIX  344 344 VAL U  198  ASP U  200  5                                   3
HELIX  345 345 PRO U  212  GLU U  233  1                                  22
HELIX  346 346 ASN U  243  LEU U  258  1                                  16
HELIX  347 347 SER U  263  TYR U  267  5                                   5
HELIX  348 348 THR U  270  ARG U  281  1                                  12
HELIX  349 349 VAL U  298  ASP U  302  5                                   5
HELIX  350 350 ASP U  305  ALA U  313  1                                   9
HELIX  351 351 SER U  322  GLY U  329  1                                   8
HELIX  352 352 GLY U  350  LEU U  370  1                                  21
HELIX  353 353 SER U  383  LEU U  388  1                                   6
HELIX  354 354 LEU U  388  LEU U  400  1                                  13
HELIX  355 355 SER U  419  GLU U  432  1                                  14
HELIX  356 356 PRO U  439  TYR U  444  5                                   6
HELIX  357 357 SER U  448  LEU U  459  1                                  12
HELIX  358 358 PRO V   18  VAL V   22  5                                   5
HELIX  359 359 GLY V   80  LEU V   84  5                                   5
HELIX  360 360 ILE V  130  CYS V  137  1                                   8
HELIX  361 361 GLY V  154  ALA V  167  1                                  14
HELIX  362 362 ARG V  182  SER V  196  1                                  15
HELIX  363 363 ASN V  197  VAL V  202  5                                   6
HELIX  364 364 PRO V  212  ASP V  232  1                                  21
HELIX  365 365 ASN V  243  ALA V  256  1                                  14
HELIX  366 366 SER V  263  TYR V  267  5                                   5
HELIX  367 367 GLN V  268  PRO V  269  5                                   2
HELIX  368 368 THR V  270  ILE V  282  1                                  13
HELIX  369 369 PRO V  299  ASP V  302  5                                   4
HELIX  370 370 ASP V  305  PHE V  312  1                                   8
HELIX  371 371 ALA V  313  LEU V  315  5                                   3
HELIX  372 372 SER V  322  SER V  327  1                                   6
HELIX  373 373 ASP V  345  GLY V  378  1                                  34
HELIX  374 374 MET V  379  LEU V  382  5                                   4
HELIX  375 375 SER V  383  LEU V  400  1                                  18
HELIX  376 376 PHE V  405  VAL V  409  5                                   5
HELIX  377 377 SER V  419  GLY V  433  1                                  15
HELIX  378 378 PRO V  439  PHE V  443  5                                   5
HELIX  379 379 SER V  448  LEU V  459  1                                  12
HELIX  380 380 GLY W    2  ALA W   40  1                                  39
HELIX  381 381 SER W   41  LEU W   60  1                                  20
HELIX  382 382 GLY W   89  ASP W  107  1                                  19
HELIX  383 383 GLY W  118  GLY W  129  1                                  12
HELIX  384 384 SER W  144  GLU W  161  1                                  18
HELIX  385 385 SER W  193  LEU W  198  1                                   6
HELIX  386 386 ASP W  210  ALA W  284  1                                  75
HELIX  387 387 GLY X   86  GLU X  103  1                                  18
HELIX  388 388 VAL X  112  ALA X  126  1                                  15
HELIX  389 389 ARG X  129  THR X  134  1                                   6
HELIX  390 390 GLY Y  100  LEU Y  104  5                                   5
HELIX  391 391 TYR Y  150  ILE Y  157  1                                   8
HELIX  392 392 GLY Y  174  ASN Y  185  1                                  12
HELIX  393 393 LYS Y  201  GLY Y  216  1                                  16
HELIX  394 394 SER Y  231  ARG Y  252  1                                  22
HELIX  395 395 ASP Y  262  LEU Y  277  1                                  16
HELIX  396 396 ASP Y  289  GLU Y  299  1                                  11
HELIX  397 397 ASN Y  305  LYS Y  314  1                                  10
HELIX  398 398 GLN Y  333  ASP Y  336  5                                   4
HELIX  399 399 ALA Y  339  THR Y  349  1                                  11
HELIX  400 400 GLU Y  356  ASN Y  361  1                                   6
HELIX  401 401 VAL Y  377  GLN Y  382  5                                   6
HELIX  402 402 THR Y  383  GLN Y  408  1                                  26
HELIX  403 403 ASP Y  414  LEU Y  431  1                                  18
HELIX  404 404 ALA Y  442  ARG Y  453  1                                  12
HELIX  405 405 LEU Y  461  ASP Y  476  1                                  16
HELIX  406 406 ARG Y  477  HIS Y  479  5                                   3
HELIX  407 407 ALA Y  480  GLY Y  490  1                                  11
HELIX  408 408 ASN Y  493  LYS Y  508  1                                  16
HELIX  409 409 TYR Z  150  ILE Z  157  1                                   8
HELIX  410 410 GLY Z  174  ASN Z  185  1                                  12
HELIX  411 411 LYS Z  201  HIS Z  215  1                                  15
HELIX  412 412 SER Z  231  ARG Z  252  1                                  22
HELIX  413 413 ASP Z  262  LEU Z  277  1                                  16
HELIX  414 414 GLY Z  282  PHE Z  286  5                                   5
HELIX  415 415 PRO Z  287  GLY Z  288  5                                   2
HELIX  416 416 ASP Z  289  GLU Z  299  1                                  11
HELIX  417 417 ASN Z  305  LYS Z  314  1                                  10
HELIX  418 418 ALA Z  339  THR Z  349  1                                  11
HELIX  419 419 GLU Z  356  ALA Z  362  1                                   7
HELIX  420 420 VAL Z  377  GLN Z  382  5                                   6
HELIX  421 421 THR Z  383  GLN Z  399  1                                  17
HELIX  422 422 ALA Z  416  LYS Z  432  1                                  17
HELIX  423 423 GLN Z  443  PHE Z  449  1                                   7
HELIX  424 424 GLY Z  454  GLU Z  460  1                                   7
HELIX  425 425 LEU Z  461  ALA Z  480  1                                  20
HELIX  426 426 PRO Z  481  GLU Z  485  5                                   5
HELIX  427 427 ASN Z  493  LYS Z  508  1                                  16
HELIX  428 428 GLY a  100  LEU a  104  5                                   5
HELIX  429 429 TYR a  150  ILE a  157  1                                   8
HELIX  430 430 GLY a  174  ASN a  185  1                                  12
HELIX  431 431 LYS a  201  HIS a  215  1                                  15
HELIX  432 432 ALA a  217  ALA a  219  5                                   3
HELIX  433 433 SER a  231  ARG a  252  1                                  22
HELIX  434 434 ASP a  262  LEU a  277  1                                  16
HELIX  435 435 GLY a  282  PHE a  286  5                                   5
HELIX  436 436 PRO a  287  GLY a  288  5                                   2
HELIX  437 437 ASP a  289  ARG a  300  1                                  12
HELIX  438 438 ASN a  305  GLU a  310  5                                   6
HELIX  439 439 ALA a  339  THR a  349  1                                  11
HELIX  440 440 GLU a  356  GLY a  363  1                                   8
HELIX  441 441 VAL a  377  GLN a  382  5                                   6
HELIX  442 442 THR a  383  ALA a  404  1                                  22
HELIX  443 443 ALA a  405  GLN a  408  5                                   4
HELIX  444 444 ASP a  414  LEU a  431  1                                  18
HELIX  445 445 ALA a  442  GLU a  452  1                                  11
HELIX  446 446 LYS a  463  GLU a  468  1                                   6
HELIX  447 447 GLU a  468  ASP a  476  1                                   9
HELIX  448 448 ALA a  480  GLY a  490  1                                  11
HELIX  449 449 ASP a  494  SER a  506  1                                  13
HELIX  450 450 ILE b  130  MET b  136  1                                   7
HELIX  451 451 GLY b  154  GLU b  169  1                                  16
HELIX  452 452 ARG b  182  SER b  196  1                                  15
HELIX  453 453 ASN b  197  ASP b  200  5                                   4
HELIX  454 454 PRO b  212  ARG b  231  1                                  20
HELIX  455 455 ASN b  243  LEU b  258  1                                  16
HELIX  456 456 SER b  263  TYR b  267  5                                   5
HELIX  457 457 THR b  270  ARG b  281  1                                  12
HELIX  458 458 PRO b  299  ASP b  302  5                                   4
HELIX  459 459 ASP b  305  ALA b  313  1                                   9
HELIX  460 460 SER b  322  LEU b  328  1                                   7
HELIX  461 461 ASP b  345  GLY b  350  1                                   6
HELIX  462 462 GLY b  350  LEU b  377  1                                  28
HELIX  463 463 GLY b  378  LEU b  382  5                                   5
HELIX  464 464 GLU b  385  LEU b  400  1                                  16
HELIX  465 465 SER b  419  MET b  431  1                                  13
HELIX  466 466 GLU b  432  LEU b  438  5                                   7
HELIX  467 467 PRO b  439  TYR b  444  5                                   6
HELIX  468 468 SER b  448  LEU b  459  1                                  12
HELIX  469 469 PRO c   18  VAL c   22  5                                   5
HELIX  470 470 ILE c  130  CYS c  137  1                                   8
HELIX  471 471 GLY c  154  GLU c  169  1                                  16
HELIX  472 472 ARG c  182  SER c  196  1                                  15
HELIX  473 473 VAL c  198  ASP c  200  5                                   3
HELIX  474 474 PRO c  212  GLU c  233  1                                  22
HELIX  475 475 ASN c  243  LEU c  258  1                                  16
HELIX  476 476 SER c  263  TYR c  267  5                                   5
HELIX  477 477 THR c  270  ARG c  281  1                                  12
HELIX  478 478 VAL c  298  ASP c  302  5                                   5
HELIX  479 479 ASP c  305  ALA c  313  1                                   9
HELIX  480 480 SER c  322  GLY c  329  1                                   8
HELIX  481 481 GLY c  350  LEU c  370  1                                  21
HELIX  482 482 LYS c  371  ILE c  376  1                                   6
HELIX  483 483 SER c  383  LEU c  388  1                                   6
HELIX  484 484 LEU c  388  LEU c  400  1                                  13
HELIX  485 485 SER c  419  GLU c  432  1                                  14
HELIX  486 486 PRO c  439  TYR c  444  5                                   6
HELIX  487 487 SER c  448  LEU c  459  1                                  12
HELIX  488 488 PRO d   18  VAL d   22  5                                   5
HELIX  489 489 GLY d   80  LEU d   84  5                                   5
HELIX  490 490 ILE d  130  CYS d  137  1                                   8
HELIX  491 491 GLY d  154  ALA d  167  1                                  14
HELIX  492 492 ARG d  182  SER d  196  1                                  15
HELIX  493 493 ASN d  197  VAL d  202  5                                   6
HELIX  494 494 PRO d  212  ASP d  232  1                                  21
HELIX  495 495 ASN d  243  ALA d  256  1                                  14
HELIX  496 496 SER d  263  TYR d  267  5                                   5
HELIX  497 497 GLN d  268  PRO d  269  5                                   2
HELIX  498 498 THR d  270  ILE d  282  1                                  13
HELIX  499 499 VAL d  298  ASP d  302  5                                   5
HELIX  500 500 ASP d  305  PHE d  312  1                                   8
HELIX  501 501 ALA d  313  LEU d  315  5                                   3
HELIX  502 502 SER d  322  SER d  327  1                                   6
HELIX  503 503 ASP d  345  GLY d  378  1                                  34
HELIX  504 504 MET d  379  LEU d  382  5                                   4
HELIX  505 505 SER d  383  LEU d  400  1                                  18
HELIX  506 506 PHE d  405  VAL d  409  5                                   5
HELIX  507 507 SER d  419  GLY d  433  1                                  15
HELIX  508 508 PRO d  439  PHE d  443  5                                   5
HELIX  509 509 SER d  448  LEU d  459  1                                  12
HELIX  510 510 GLY e    2  ALA e   40  1                                  39
HELIX  511 511 SER e   41  LEU e   60  1                                  20
HELIX  512 512 GLY e   89  ASP e  107  1                                  19
HELIX  513 513 GLY e  118  GLY e  129  1                                  12
HELIX  514 514 SER e  144  GLU e  161  1                                  18
HELIX  515 515 ASP e  210  ALA e  284  1                                  75
HELIX  516 516 GLY f   86  GLU f  103  1                                  18
HELIX  517 517 VAL f  112  ALA f  126  1                                  15
HELIX  518 518 ARG f  129  THR f  134  1                                   6
SHEET    1   A12 ALA E  28  GLN E  32  0
SHEET    2   A12 ARG E  37  GLN E  44 -1  O  LEU E  40   N  LEU E  29
SHEET    3   A12 ILE E  50  ALA E  55 -1  O  ARG E  52   N  GLN E  43
SHEET    4   A12 VAL E  12  GLU E  16 -1  N  VAL E  15   O  VAL E  51
SHEET    5   A12 LYS E   4  ILE E   9 -1  N  GLN E   7   O  ASP E  14
SHEET    6   A12 ARG A  59  LEU A  66 -1  N  LEU A  66   O  VAL E   8
SHEET    7   A12 VAL A  71  VAL A  75 -1  O  GLY A  72   N  ASN A  65
SHEET    8   A12 VAL A  38  GLY A  43 -1  N  ILE A  41   O  VAL A  71
SHEET    9   A12 GLU A  28  SER A  35 -1  N  VAL A  32   O  ARG A  40
SHEET   10   A12 LYS A  87  LYS A  89 -1  O  VAL A  88   N  GLY A  29
SHEET   11   A12 MET A  52  LEU A  55 -1  N  SER A  54   O  LYS A  89
SHEET   12   A12 ARG A  59  LEU A  66 -1  O  ALA A  61   N  ILE A  53
SHEET    1   B 2 GLU A  96  PRO A  98  0
SHEET    2   B 2 PHE A 126  ALA A 128 -1  O  SER A 127   N  VAL A  97
SHEET    1   C 6 VAL A 107  ASN A 109  0
SHEET    2   C 6 THR A 221  ALA A 226  1  O  VAL A 225   N  VAL A 108
SHEET    3   C 6 LYS A 192  ILE A 198  1  N  ALA A 197   O  VAL A 224
SHEET    4   C 6 ASP A 255  ASP A 261  1  O  LEU A 257   N  LYS A 192
SHEET    5   C 6 GLY A 322  ALA A 326  1  O  THR A 325   N  ILE A 258
SHEET    6   C 6 ARG A 303  VAL A 304 -1  N  VAL A 304   O  GLY A 322
SHEET    1   D 4 ILE A 329  GLU A 331  0
SHEET    2   D 4 LEU A 166  GLY A 169  1  N  ILE A 167   O  ILE A 330
SHEET    3   D 4 GLY A 351  LEU A 355  1  O  ILE A 353   N  LEU A 166
SHEET    4   D 4 VAL A 374  SER A 375 -1  O  VAL A 374   N  GLN A 352
SHEET    1   E 7 GLY B  29  SER B  35  0
SHEET    2   E 7 VAL B  38  GLY B  43 -1  O  ARG B  40   N  VAL B  32
SHEET    3   E 7 SER B  70  VAL B  75 -1  O  VAL B  71   N  ILE B  41
SHEET    4   E 7 TYR B  60  ALA B  63 -1  N  ILE B  62   O  VAL B  74
SHEET    5   E 7 MET B  52  SER B  54 -1  N  ILE B  53   O  ALA B  61
SHEET    6   E 7 LYS B  87  CYS B  90 -1  O  LYS B  89   N  SER B  54
SHEET    7   E 7 GLY B  29  SER B  35 -1  N  GLY B  29   O  VAL B  88
SHEET    1   F 8 ASN B  65  LEU B  66  0
SHEET    2   F 8 GLY F   3  ILE F   9 -1  O  VAL F   8   N  LEU B  66
SHEET    3   F 8 ASP F  67  ASP F  70 -1  O  VAL F  68   N  GLY F   3
SHEET    4   F 8 ALA F  28  GLN F  32 -1  N  GLU F  30   O  LYS F  69
SHEET    5   F 8 ARG F  37  GLN F  44 -1  O  LEU F  40   N  LEU F  29
SHEET    6   F 8 ILE F  50  ALA F  55 -1  O  ARG F  52   N  GLN F  43
SHEET    7   F 8 VAL F  12  GLU F  16 -1  N  VAL F  15   O  VAL F  51
SHEET    8   F 8 GLY F   3  ILE F   9 -1  N  ILE F   9   O  VAL F  12
SHEET    1   G 6 ILE B 115  ASP B 116  0
SHEET    2   G 6 VAL B 107  ASN B 109 -1  N  VAL B 107   O  ASP B 116
SHEET    3   G 6 THR B 221  THR B 227  1  O  VAL B 225   N  VAL B 108
SHEET    4   G 6 LYS B 192  GLN B 200  1  N  GLY B 199   O  ALA B 226
SHEET    5   G 6 ASP B 255  ASP B 261  1  O  LEU B 257   N  LYS B 192
SHEET    6   G 6 SER B 323  ALA B 326  1  O  THR B 325   N  ALA B 256
SHEET    1   H 4 ILE B 329  GLU B 331  0
SHEET    2   H 4 LEU B 166  GLY B 169  1  N  GLY B 169   O  ILE B 330
SHEET    3   H 4 GLY B 351  LEU B 355  1  O  LEU B 355   N  ILE B 168
SHEET    4   H 4 VAL B 374  SER B 375 -1  O  VAL B 374   N  GLN B 352
SHEET    1   I14 TYR C  60  GLU C  67  0
SHEET    2   I14 MET C  52  SER C  54 -1  N  ILE C  53   O  ALA C  61
SHEET    3   I14 LYS C  87  CYS C  90 -1  O  LYS C  89   N  SER C  54
SHEET    4   I14 GLU C  28  SER C  35 -1  N  GLY C  29   O  VAL C  88
SHEET    5   I14 VAL C  38  GLY C  43 -1  O  VAL C  38   N  SER C  35
SHEET    6   I14 SER C  70  VAL C  75 -1  O  ALA C  73   N  ILE C  39
SHEET    7   I14 TYR C  60  GLU C  67 -1  N  ASN C  65   O  GLY C  72
SHEET    8   I14 GLY D   3  ILE D   9 -1  O  VAL D   8   N  LEU C  66
SHEET    9   I14 ASP D  67  ASP D  70 -1  O  VAL D  68   N  GLY D   3
SHEET   10   I14 ALA D  28  GLN D  32 -1  N  GLU D  30   O  LYS D  69
SHEET   11   I14 ARG D  37  GLN D  44 -1  O  LEU D  40   N  LEU D  29
SHEET   12   I14 ILE D  50  ALA D  55 -1  O  ARG D  52   N  GLN D  43
SHEET   13   I14 VAL D  12  GLU D  16 -1  N  VAL D  15   O  VAL D  51
SHEET   14   I14 GLY D   3  ILE D   9 -1  N  ILE D   9   O  VAL D  12
SHEET    1   J 2 GLU C  96  PRO C  98  0
SHEET    2   J 2 PHE C 126  ALA C 128 -1  O  SER C 127   N  VAL C  97
SHEET    1   K 6 VAL C 107  VAL C 108  0
SHEET    2   K 6 THR C 221  ALA C 226  1  O  VAL C 223   N  VAL C 108
SHEET    3   K 6 LYS C 192  ILE C 198  1  N  ALA C 197   O  VAL C 224
SHEET    4   K 6 ASP C 255  ASP C 261  1  O  LEU C 257   N  LYS C 192
SHEET    5   K 6 GLY C 322  ALA C 326  1  O  THR C 325   N  ALA C 256
SHEET    6   K 6 ARG C 303  VAL C 304 -1  N  VAL C 304   O  GLY C 322
SHEET    1   L 4 ILE C 329  THR C 332  0
SHEET    2   L 4 GLU C 165  ASP C 170  1  N  ILE C 167   O  ILE C 330
SHEET    3   L 4 GLY C 351  LEU C 355  1  O  GLY C 351   N  LEU C 166
SHEET    4   L 4 VAL C 374  SER C 375 -1  O  VAL C 374   N  GLN C 352
SHEET    1   M 2 GLU D  76  VAL D  77  0
SHEET    2   M 2 TRP D 107  ALA D 108 -1  O  TRP D 107   N  VAL D  77
SHEET    1   N 7 VAL D 202  TYR D 206  0
SHEET    2   N 7 SER D 174  GLY D 178  1  N  PHE D 176   O  VAL D 205
SHEET    3   N 7 ASP D 236  VAL D 241  1  O  PHE D 240   N  VAL D 175
SHEET    4   N 7 SER D 289  TYR D 297  1  O  THR D 291   N  VAL D 237
SHEET    5   N 7 LYS D 144  GLY D 149  1  N  VAL D 145   O  SER D 292
SHEET    6   N 7 ALA D 317  VAL D 320  1  O  VAL D 319   N  GLY D 146
SHEET    7   N 7 THR D 340  SER D 341 -1  O  THR D 340   N  THR D 318
SHEET    1   O 2 GLU E  76  PRO E  78  0
SHEET    2   O 2 ARG E 106  ALA E 108 -1  O  TRP E 107   N  VAL E  77
SHEET    1   P 7 ILE E  87  MET E  88  0
SHEET    2   P 7 VAL E 202  GLY E 207  1  O  TYR E 206   N  MET E  88
SHEET    3   P 7 SER E 174  VAL E 179  1  N  GLY E 178   O  VAL E 205
SHEET    4   P 7 ASP E 236  VAL E 241  1  O  LEU E 238   N  VAL E 175
SHEET    5   P 7 SER E 289  ALA E 295  1  O  THR E 291   N  VAL E 237
SHEET    6   P 7 LYS E 144  PHE E 148  1  N  LEU E 147   O  GLN E 294
SHEET    7   P 7 ALA E 317  VAL E 320  1  O  VAL E 319   N  GLY E 146
SHEET    1   Q 2 LEU E 125  LEU E 126  0
SHEET    2   Q 2 PHE E 139  ALA E 140 -1  O  PHE E 139   N  LEU E 126
SHEET    1   R 2 LEU F 125  LEU F 126  0
SHEET    2   R 2 PHE F 139  ALA F 140 -1  O  PHE F 139   N  LEU F 126
SHEET    1   S 7 TYR F 206  GLN F 208  0
SHEET    2   S 7 TYR F 173  GLU F 181  1  N  GLY F 180   O  GLY F 207
SHEET    3   S 7 ASP F 236  ASP F 242  1  O  LEU F 238   N  VAL F 175
SHEET    4   S 7 SER F 289  ALA F 295  1  O  THR F 291   N  LEU F 239
SHEET    5   S 7 LYS F 144  GLY F 149  1  N  VAL F 145   O  SER F 292
SHEET    6   S 7 ALA F 317  LEU F 321  1  O  LEU F 321   N  PHE F 148
SHEET    7   S 7 THR F 340  SER F 341 -1  O  THR F 340   N  THR F 318
SHEET    1   T 5 VAL G 132  VAL G 136  0
SHEET    2   T 5 GLN G 111  ILE G 117  1  N  MET G 116   O  ALA G 134
SHEET    3   T 5 ARG G  74  VAL G  80  1  N  TYR G  77   O  ALA G 115
SHEET    4   T 5 LYS G 166  ASN G 176  1  O  VAL G 170   N  VAL G  80
SHEET    5   T 5 SER G 179  GLN G 186 -1  O  SER G 185   N  ILE G 169
SHEET    1   U 6 GLU H  59  LEU H  64  0
SHEET    2   U 6 LEU H  41  LYS H  54 -1  N  GLY H  48   O  LEU H  64
SHEET    3   U 6 GLN H  14  GLY H  27 -1  N  GLU H  21   O  VAL H  53
SHEET    4   U 6 TYR H   4  SER H  10 -1  N  TYR H   4   O  VAL H  20
SHEET    5   U 6 ASN H  75  ALA H  80  1  O  VAL H  78   N  ASP H   7
SHEET    6   U 6 GLY H  67  GLN H  72 -1  N  GLN H  72   O  ASN H  75
SHEET    1   V 4 LEU G 206  TYR G 207  0
SHEET    2   V 4 LEU H  41  LYS H  54  1  O  LEU H  42   N  LEU G 206
SHEET    3   V 4 GLN H  14  GLY H  27 -1  N  GLU H  21   O  VAL H  53
SHEET    4   V 4 GLU H  31  ILE H  34 -1  O  LEU H  32   N  VAL H  25
SHEET    1   W12 ALA M  28  GLN M  32  0
SHEET    2   W12 ARG M  37  GLN M  44 -1  O  LEU M  40   N  LEU M  29
SHEET    3   W12 ILE M  50  ALA M  55 -1  O  ARG M  52   N  GLN M  43
SHEET    4   W12 VAL M  12  GLU M  16 -1  N  VAL M  15   O  VAL M  51
SHEET    5   W12 LYS M   4  ILE M   9 -1  N  GLN M   7   O  ASP M  14
SHEET    6   W12 ARG I  59  LEU I  66 -1  N  LEU I  66   O  VAL M   8
SHEET    7   W12 VAL I  71  VAL I  75 -1  O  GLY I  72   N  ASN I  65
SHEET    8   W12 VAL I  38  GLY I  43 -1  N  ILE I  41   O  VAL I  71
SHEET    9   W12 GLU I  28  SER I  35 -1  N  VAL I  32   O  ARG I  40
SHEET   10   W12 LYS I  87  LYS I  89 -1  O  VAL I  88   N  GLY I  29
SHEET   11   W12 MET I  52  LEU I  55 -1  N  SER I  54   O  LYS I  89
SHEET   12   W12 ARG I  59  LEU I  66 -1  O  ALA I  61   N  ILE I  53
SHEET    1   X 2 GLU I  96  PRO I  98  0
SHEET    2   X 2 PHE I 126  ALA I 128 -1  O  SER I 127   N  VAL I  97
SHEET    1   Y 6 VAL I 107  ASN I 109  0
SHEET    2   Y 6 THR I 221  ALA I 226  1  O  VAL I 225   N  VAL I 108
SHEET    3   Y 6 LYS I 192  ILE I 198  1  N  ALA I 197   O  VAL I 224
SHEET    4   Y 6 ASP I 255  ASP I 261  1  O  LEU I 257   N  LYS I 192
SHEET    5   Y 6 GLY I 322  ALA I 326  1  O  THR I 325   N  ILE I 258
SHEET    6   Y 6 ARG I 303  VAL I 304 -1  N  VAL I 304   O  GLY I 322
SHEET    1   Z 4 ILE I 329  GLU I 331  0
SHEET    2   Z 4 LEU I 166  GLY I 169  1  N  ILE I 167   O  ILE I 330
SHEET    3   Z 4 GLY I 351  LEU I 355  1  O  ILE I 353   N  LEU I 166
SHEET    4   Z 4 VAL I 374  SER I 375 -1  O  VAL I 374   N  GLN I 352
SHEET    1  AA 7 GLY J  29  SER J  35  0
SHEET    2  AA 7 VAL J  38  GLY J  43 -1  O  ARG J  40   N  VAL J  32
SHEET    3  AA 7 SER J  70  VAL J  75 -1  O  VAL J  71   N  ILE J  41
SHEET    4  AA 7 TYR J  60  ALA J  63 -1  N  ILE J  62   O  VAL J  74
SHEET    5  AA 7 GLU J  51  SER J  54 -1  N  ILE J  53   O  ALA J  61
SHEET    6  AA 7 LYS J  87  ILE J  94 -1  O  LYS J  89   N  SER J  54
SHEET    7  AA 7 GLY J  29  SER J  35 -1  N  GLY J  29   O  VAL J  88
SHEET    1  AB 8 ASN J  65  LEU J  66  0
SHEET    2  AB 8 GLY N   3  ILE N   9 -1  O  VAL N   8   N  LEU J  66
SHEET    3  AB 8 ASP N  67  ASP N  70 -1  O  VAL N  68   N  GLY N   3
SHEET    4  AB 8 ALA N  28  GLN N  32 -1  N  GLU N  30   O  LYS N  69
SHEET    5  AB 8 ARG N  37  GLN N  44 -1  O  LEU N  40   N  LEU N  29
SHEET    6  AB 8 ILE N  50  ALA N  55 -1  O  ARG N  52   N  GLN N  43
SHEET    7  AB 8 VAL N  12  GLU N  16 -1  N  VAL N  15   O  VAL N  51
SHEET    8  AB 8 GLY N   3  ILE N   9 -1  N  ILE N   9   O  VAL N  12
SHEET    1  AC 6 ILE J 115  ASP J 116  0
SHEET    2  AC 6 VAL J 107  ASN J 109 -1  N  VAL J 107   O  ASP J 116
SHEET    3  AC 6 THR J 221  THR J 227  1  O  VAL J 225   N  VAL J 108
SHEET    4  AC 6 LYS J 192  GLN J 200  1  N  GLY J 199   O  ALA J 226
SHEET    5  AC 6 ASP J 255  ASP J 261  1  O  LEU J 257   N  LYS J 192
SHEET    6  AC 6 SER J 323  ALA J 326  1  O  THR J 325   N  ALA J 256
SHEET    1  AD 4 ILE J 329  GLU J 331  0
SHEET    2  AD 4 LEU J 166  GLY J 169  1  N  GLY J 169   O  ILE J 330
SHEET    3  AD 4 GLY J 351  LEU J 355  1  O  LEU J 355   N  ILE J 168
SHEET    4  AD 4 VAL J 374  SER J 375 -1  O  VAL J 374   N  GLN J 352
SHEET    1  AE14 TYR K  60  GLU K  67  0
SHEET    2  AE14 MET K  52  SER K  54 -1  N  ILE K  53   O  ALA K  61
SHEET    3  AE14 LYS K  87  CYS K  90 -1  O  LYS K  89   N  SER K  54
SHEET    4  AE14 GLU K  28  SER K  35 -1  N  GLY K  29   O  VAL K  88
SHEET    5  AE14 VAL K  38  GLY K  43 -1  O  VAL K  38   N  SER K  35
SHEET    6  AE14 SER K  70  VAL K  75 -1  O  ALA K  73   N  ILE K  39
SHEET    7  AE14 TYR K  60  GLU K  67 -1  N  ASN K  65   O  GLY K  72
SHEET    8  AE14 GLY L   3  ILE L   9 -1  O  VAL L   8   N  LEU K  66
SHEET    9  AE14 ASP L  67  ASP L  70 -1  O  VAL L  68   N  GLY L   3
SHEET   10  AE14 ALA L  28  GLN L  32 -1  N  GLU L  30   O  LYS L  69
SHEET   11  AE14 ARG L  37  GLN L  44 -1  O  LEU L  40   N  LEU L  29
SHEET   12  AE14 ILE L  50  ALA L  55 -1  O  ARG L  52   N  GLN L  43
SHEET   13  AE14 VAL L  12  GLU L  16 -1  N  VAL L  15   O  VAL L  51
SHEET   14  AE14 GLY L   3  ILE L   9 -1  N  ILE L   9   O  VAL L  12
SHEET    1  AF 2 GLU K  96  PRO K  98  0
SHEET    2  AF 2 PHE K 126  ALA K 128 -1  O  SER K 127   N  VAL K  97
SHEET    1  AG 6 VAL K 107  VAL K 108  0
SHEET    2  AG 6 THR K 221  ALA K 226  1  O  VAL K 223   N  VAL K 108
SHEET    3  AG 6 LYS K 192  ILE K 198  1  N  ALA K 197   O  VAL K 224
SHEET    4  AG 6 ASP K 255  ASP K 261  1  O  LEU K 257   N  LYS K 192
SHEET    5  AG 6 GLY K 322  ALA K 326  1  O  THR K 325   N  ALA K 256
SHEET    6  AG 6 ARG K 303  VAL K 304 -1  N  VAL K 304   O  GLY K 322
SHEET    1  AH 4 ILE K 329  THR K 332  0
SHEET    2  AH 4 GLU K 165  ASP K 170  1  N  ILE K 167   O  ILE K 330
SHEET    3  AH 4 GLY K 351  LEU K 355  1  O  GLY K 351   N  LEU K 166
SHEET    4  AH 4 VAL K 374  SER K 375 -1  O  VAL K 374   N  GLN K 352
SHEET    1  AI 2 GLU L  76  VAL L  77  0
SHEET    2  AI 2 TRP L 107  ALA L 108 -1  O  TRP L 107   N  VAL L  77
SHEET    1  AJ 7 VAL L 202  TYR L 206  0
SHEET    2  AJ 7 SER L 174  GLY L 178  1  N  PHE L 176   O  VAL L 205
SHEET    3  AJ 7 ASP L 236  VAL L 241  1  O  PHE L 240   N  VAL L 175
SHEET    4  AJ 7 SER L 289  TYR L 297  1  O  THR L 291   N  VAL L 237
SHEET    5  AJ 7 LYS L 144  GLY L 149  1  N  VAL L 145   O  SER L 292
SHEET    6  AJ 7 ALA L 317  VAL L 320  1  O  VAL L 319   N  GLY L 146
SHEET    7  AJ 7 THR L 340  SER L 341 -1  O  THR L 340   N  THR L 318
SHEET    1  AK 2 GLU M  76  PRO M  78  0
SHEET    2  AK 2 ARG M 106  ALA M 108 -1  O  TRP M 107   N  VAL M  77
SHEET    1  AL 7 ILE M  87  MET M  88  0
SHEET    2  AL 7 VAL M 202  GLY M 207  1  O  TYR M 206   N  MET M  88
SHEET    3  AL 7 SER M 174  VAL M 179  1  N  GLY M 178   O  VAL M 205
SHEET    4  AL 7 ASP M 236  VAL M 241  1  O  LEU M 238   N  VAL M 175
SHEET    5  AL 7 SER M 289  ALA M 295  1  O  THR M 291   N  VAL M 237
SHEET    6  AL 7 LYS M 144  PHE M 148  1  N  LEU M 147   O  GLN M 294
SHEET    7  AL 7 ALA M 317  VAL M 320  1  O  VAL M 319   N  GLY M 146
SHEET    1  AM 2 LEU M 125  LEU M 126  0
SHEET    2  AM 2 PHE M 139  ALA M 140 -1  O  PHE M 139   N  LEU M 126
SHEET    1  AN 2 LEU N 125  LEU N 126  0
SHEET    2  AN 2 PHE N 139  ALA N 140 -1  O  PHE N 139   N  LEU N 126
SHEET    1  AO 7 TYR N 206  GLN N 208  0
SHEET    2  AO 7 TYR N 173  GLU N 181  1  N  GLY N 180   O  GLY N 207
SHEET    3  AO 7 ASP N 236  ASP N 242  1  O  LEU N 238   N  VAL N 175
SHEET    4  AO 7 SER N 289  ALA N 295  1  O  THR N 291   N  LEU N 239
SHEET    5  AO 7 LYS N 144  GLY N 149  1  N  VAL N 145   O  SER N 292
SHEET    6  AO 7 ALA N 317  LEU N 321  1  O  LEU N 321   N  PHE N 148
SHEET    7  AO 7 THR N 340  SER N 341 -1  O  THR N 340   N  THR N 318
SHEET    1  AP 5 VAL O 132  VAL O 136  0
SHEET    2  AP 5 GLN O 111  ILE O 117  1  N  MET O 116   O  ALA O 134
SHEET    3  AP 5 ARG O  74  VAL O  80  1  N  TYR O  77   O  ALA O 115
SHEET    4  AP 5 LYS O 166  ASN O 176  1  O  VAL O 170   N  VAL O  80
SHEET    5  AP 5 SER O 179  LEU O 187 -1  O  SER O 185   N  ILE O 169
SHEET    1  AQ 4 GLN P  14  GLY P  27  0
SHEET    2  AQ 4 LEU P  41  LYS P  54 -1  O  VAL P  53   N  GLU P  21
SHEET    3  AQ 4 GLY P  67  GLN P  72 -1  O  LEU P  69   N  THR P  43
SHEET    4  AQ 4 TYR P   4  SER P  10  0
SHEET    1  AR 4 GLU P  59  LEU P  64  0
SHEET    2  AR 4 LEU P  41  LYS P  54 -1  N  GLY P  48   O  LEU P  64
SHEET    3  AR 4 GLY P  67  GLN P  72 -1  O  LEU P  69   N  THR P  43
SHEET    4  AR 4 ASN P  75  ALA P  80 -1  O  ASN P  75   N  GLN P  72
SHEET    1  AS 4 TYR P   4  SER P  10  0
SHEET    2  AS 4 GLY P  67  GLN P  72  0
SHEET    3  AS 4 LEU P  41  LYS P  54 -1  N  THR P  43   O  LEU P  69
SHEET    4  AS 4 LEU O 206  TYR O 207  1  N  LEU O 206   O  LEU P  42
SHEET    1  AT 4 LEU O 206  TYR O 207  0
SHEET    2  AT 4 LEU P  41  LYS P  54  1  O  LEU P  42   N  LEU O 206
SHEET    3  AT 4 GLN P  14  GLY P  27 -1  N  GLU P  21   O  VAL P  53
SHEET    4  AT 4 GLU P  31  ILE P  34 -1  O  LEU P  32   N  VAL P  25
SHEET    1  AU 5 GLU P  31  ILE P  34  0
SHEET    2  AU 5 GLN P  14  GLY P  27 -1  N  VAL P  25   O  LEU P  32
SHEET    3  AU 5 LEU P  41  LYS P  54 -1  O  VAL P  53   N  GLU P  21
SHEET    4  AU 5 GLY P  67  GLN P  72 -1  O  LEU P  69   N  THR P  43
SHEET    5  AU 5 ASN P  75  ALA P  80 -1  O  ASN P  75   N  GLN P  72
SHEET    1  AV12 ALA U  28  GLN U  32  0
SHEET    2  AV12 ARG U  37  GLN U  44 -1  O  LEU U  40   N  LEU U  29
SHEET    3  AV12 ILE U  50  ALA U  55 -1  O  ARG U  52   N  GLN U  43
SHEET    4  AV12 VAL U  12  GLU U  16 -1  N  VAL U  15   O  VAL U  51
SHEET    5  AV12 LYS U   4  ILE U   9 -1  N  GLN U   7   O  ASP U  14
SHEET    6  AV12 ARG Q  59  LEU Q  66 -1  N  LEU Q  66   O  VAL U   8
SHEET    7  AV12 VAL Q  71  VAL Q  75 -1  O  GLY Q  72   N  ASN Q  65
SHEET    8  AV12 VAL Q  38  GLY Q  43 -1  N  ILE Q  41   O  VAL Q  71
SHEET    9  AV12 GLU Q  28  SER Q  35 -1  N  VAL Q  32   O  ARG Q  40
SHEET   10  AV12 LYS Q  87  LYS Q  89 -1  O  VAL Q  88   N  GLY Q  29
SHEET   11  AV12 MET Q  52  LEU Q  55 -1  N  SER Q  54   O  LYS Q  89
SHEET   12  AV12 ARG Q  59  LEU Q  66 -1  O  ALA Q  61   N  ILE Q  53
SHEET    1  AW 2 GLU Q  96  PRO Q  98  0
SHEET    2  AW 2 PHE Q 126  ALA Q 128 -1  O  SER Q 127   N  VAL Q  97
SHEET    1  AX 6 VAL Q 107  ASN Q 109  0
SHEET    2  AX 6 THR Q 221  ALA Q 226  1  O  VAL Q 225   N  VAL Q 108
SHEET    3  AX 6 LYS Q 192  ILE Q 198  1  N  ALA Q 197   O  VAL Q 224
SHEET    4  AX 6 ASP Q 255  ASP Q 261  1  O  LEU Q 257   N  LYS Q 192
SHEET    5  AX 6 GLY Q 322  ALA Q 326  1  O  THR Q 325   N  ILE Q 258
SHEET    6  AX 6 ARG Q 303  VAL Q 304 -1  N  VAL Q 304   O  GLY Q 322
SHEET    1  AY 4 ILE Q 329  GLU Q 331  0
SHEET    2  AY 4 LEU Q 166  GLY Q 169  1  N  ILE Q 167   O  ILE Q 330
SHEET    3  AY 4 GLY Q 351  LEU Q 355  1  O  ILE Q 353   N  LEU Q 166
SHEET    4  AY 4 VAL Q 374  SER Q 375 -1  O  VAL Q 374   N  GLN Q 352
SHEET    1  AZ 7 GLY R  29  SER R  35  0
SHEET    2  AZ 7 VAL R  38  GLY R  43 -1  O  ARG R  40   N  VAL R  32
SHEET    3  AZ 7 SER R  70  VAL R  75 -1  O  VAL R  71   N  ILE R  41
SHEET    4  AZ 7 TYR R  60  ALA R  63 -1  N  ILE R  62   O  VAL R  74
SHEET    5  AZ 7 MET R  52  SER R  54 -1  N  ILE R  53   O  ALA R  61
SHEET    6  AZ 7 LYS R  87  CYS R  90 -1  O  LYS R  89   N  SER R  54
SHEET    7  AZ 7 GLY R  29  SER R  35 -1  N  GLY R  29   O  VAL R  88
SHEET    1  BA 8 ASN R  65  LEU R  66  0
SHEET    2  BA 8 GLY V   3  ILE V   9 -1  O  VAL V   8   N  LEU R  66
SHEET    3  BA 8 ASP V  67  ASP V  70 -1  O  VAL V  68   N  GLY V   3
SHEET    4  BA 8 ALA V  28  GLN V  32 -1  N  GLU V  30   O  LYS V  69
SHEET    5  BA 8 ARG V  37  GLN V  44 -1  O  LEU V  40   N  LEU V  29
SHEET    6  BA 8 ILE V  50  ALA V  55 -1  O  ARG V  52   N  GLN V  43
SHEET    7  BA 8 VAL V  12  GLU V  16 -1  N  VAL V  15   O  VAL V  51
SHEET    8  BA 8 GLY V   3  ILE V   9 -1  N  ILE V   9   O  VAL V  12
SHEET    1  BB 6 ILE R 115  ASP R 116  0
SHEET    2  BB 6 VAL R 107  ASN R 109 -1  N  VAL R 107   O  ASP R 116
SHEET    3  BB 6 THR R 221  THR R 227  1  O  VAL R 225   N  VAL R 108
SHEET    4  BB 6 LYS R 192  GLN R 200  1  N  GLY R 199   O  ALA R 226
SHEET    5  BB 6 ASP R 255  ASP R 261  1  O  LEU R 257   N  LYS R 192
SHEET    6  BB 6 SER R 323  ALA R 326  1  O  THR R 325   N  ALA R 256
SHEET    1  BC 4 ILE R 329  GLU R 331  0
SHEET    2  BC 4 LEU R 166  GLY R 169  1  N  GLY R 169   O  ILE R 330
SHEET    3  BC 4 GLY R 351  LEU R 355  1  O  LEU R 355   N  ILE R 168
SHEET    4  BC 4 VAL R 374  SER R 375 -1  O  VAL R 374   N  GLN R 352
SHEET    1  BD14 TYR S  60  GLU S  67  0
SHEET    2  BD14 MET S  52  SER S  54 -1  N  ILE S  53   O  ALA S  61
SHEET    3  BD14 LYS S  87  CYS S  90 -1  O  LYS S  89   N  SER S  54
SHEET    4  BD14 GLU S  28  SER S  35 -1  N  GLY S  29   O  VAL S  88
SHEET    5  BD14 VAL S  38  GLY S  43 -1  O  VAL S  38   N  SER S  35
SHEET    6  BD14 SER S  70  VAL S  75 -1  O  ALA S  73   N  ILE S  39
SHEET    7  BD14 TYR S  60  GLU S  67 -1  N  ASN S  65   O  GLY S  72
SHEET    8  BD14 GLY T   3  ILE T   9 -1  O  VAL T   8   N  LEU S  66
SHEET    9  BD14 ASP T  67  ASP T  70 -1  O  VAL T  68   N  GLY T   3
SHEET   10  BD14 ALA T  28  GLN T  32 -1  N  GLU T  30   O  LYS T  69
SHEET   11  BD14 ARG T  37  GLN T  44 -1  O  LEU T  40   N  LEU T  29
SHEET   12  BD14 ILE T  50  ALA T  55 -1  O  ARG T  52   N  GLN T  43
SHEET   13  BD14 VAL T  12  GLU T  16 -1  N  VAL T  15   O  VAL T  51
SHEET   14  BD14 GLY T   3  ILE T   9 -1  N  ILE T   9   O  VAL T  12
SHEET    1  BE 2 GLU S  96  PRO S  98  0
SHEET    2  BE 2 PHE S 126  ALA S 128 -1  O  SER S 127   N  VAL S  97
SHEET    1  BF 6 VAL S 107  VAL S 108  0
SHEET    2  BF 6 THR S 221  ALA S 226  1  O  VAL S 223   N  VAL S 108
SHEET    3  BF 6 LYS S 192  ILE S 198  1  N  ALA S 197   O  VAL S 224
SHEET    4  BF 6 ASP S 255  ASP S 261  1  O  LEU S 257   N  LYS S 192
SHEET    5  BF 6 GLY S 322  ALA S 326  1  O  THR S 325   N  ALA S 256
SHEET    6  BF 6 ARG S 303  VAL S 304 -1  N  VAL S 304   O  GLY S 322
SHEET    1  BG 4 ILE S 329  THR S 332  0
SHEET    2  BG 4 GLU S 165  ASP S 170  1  N  ILE S 167   O  ILE S 330
SHEET    3  BG 4 GLY S 351  LEU S 355  1  O  GLY S 351   N  LEU S 166
SHEET    4  BG 4 VAL S 374  SER S 375 -1  O  VAL S 374   N  GLN S 352
SHEET    1  BH 2 GLU T  76  VAL T  77  0
SHEET    2  BH 2 TRP T 107  ALA T 108 -1  O  TRP T 107   N  VAL T  77
SHEET    1  BI 7 VAL T 202  TYR T 206  0
SHEET    2  BI 7 SER T 174  GLY T 178  1  N  PHE T 176   O  VAL T 205
SHEET    3  BI 7 ASP T 236  VAL T 241  1  O  PHE T 240   N  VAL T 175
SHEET    4  BI 7 SER T 289  TYR T 297  1  O  THR T 291   N  VAL T 237
SHEET    5  BI 7 LYS T 144  GLY T 149  1  N  VAL T 145   O  SER T 292
SHEET    6  BI 7 ALA T 317  VAL T 320  1  O  VAL T 319   N  GLY T 146
SHEET    7  BI 7 THR T 340  SER T 341 -1  O  THR T 340   N  THR T 318
SHEET    1  BJ 2 GLU U  76  PRO U  78  0
SHEET    2  BJ 2 ARG U 106  ALA U 108 -1  O  TRP U 107   N  VAL U  77
SHEET    1  BK 7 ILE U  87  MET U  88  0
SHEET    2  BK 7 VAL U 202  GLY U 207  1  O  TYR U 206   N  MET U  88
SHEET    3  BK 7 SER U 174  VAL U 179  1  N  GLY U 178   O  VAL U 205
SHEET    4  BK 7 ASP U 236  VAL U 241  1  O  LEU U 238   N  VAL U 175
SHEET    5  BK 7 SER U 289  ALA U 295  1  O  THR U 291   N  VAL U 237
SHEET    6  BK 7 LYS U 144  PHE U 148  1  N  LEU U 147   O  GLN U 294
SHEET    7  BK 7 ALA U 317  VAL U 320  1  O  VAL U 319   N  GLY U 146
SHEET    1  BL 2 LEU U 125  LEU U 126  0
SHEET    2  BL 2 PHE U 139  ALA U 140 -1  O  PHE U 139   N  LEU U 126
SHEET    1  BM 2 LEU V 125  LEU V 126  0
SHEET    2  BM 2 PHE V 139  ALA V 140 -1  O  PHE V 139   N  LEU V 126
SHEET    1  BN 7 TYR V 206  GLN V 208  0
SHEET    2  BN 7 TYR V 173  GLU V 181  1  N  GLY V 180   O  GLY V 207
SHEET    3  BN 7 ASP V 236  ASP V 242  1  O  LEU V 238   N  VAL V 175
SHEET    4  BN 7 SER V 289  TYR V 297  1  O  THR V 291   N  LEU V 239
SHEET    5  BN 7 LYS V 144  GLY V 149  1  N  LEU V 147   O  GLN V 294
SHEET    6  BN 7 ALA V 317  LEU V 321  1  O  LEU V 321   N  PHE V 148
SHEET    7  BN 7 THR V 340  SER V 341 -1  O  THR V 340   N  THR V 318
SHEET    1  BO 5 VAL W 132  VAL W 136  0
SHEET    2  BO 5 GLN W 111  ILE W 117  1  N  MET W 116   O  ALA W 134
SHEET    3  BO 5 ARG W  74  VAL W  80  1  N  TYR W  77   O  ALA W 115
SHEET    4  BO 5 LYS W 166  ASN W 176  1  O  VAL W 170   N  VAL W  80
SHEET    5  BO 5 SER W 179  GLN W 186 -1  O  SER W 185   N  ILE W 169
SHEET    1  BP 7 GLU X  31  ILE X  34  0
SHEET    2  BP 7 GLN X  14  GLY X  27 -1  N  VAL X  25   O  LEU X  32
SHEET    3  BP 7 TYR X   4  SER X  10 -1  N  TYR X   4   O  VAL X  20
SHEET    4  BP 7 ASN X  75  ALA X  80  1  O  VAL X  78   N  ASP X   7
SHEET    5  BP 7 GLY X  67  GLN X  72 -1  N  GLN X  72   O  ASN X  75
SHEET    6  BP 7 LEU X  41  LYS X  54 -1  N  THR X  43   O  LEU X  69
SHEET    7  BP 7 GLU X  59  LEU X  64 -1  O  LEU X  64   N  GLY X  48
SHEET    1  BQ 4 GLU X  31  ILE X  34  0
SHEET    2  BQ 4 GLN X  14  GLY X  27 -1  N  VAL X  25   O  LEU X  32
SHEET    3  BQ 4 LEU X  41  LYS X  54 -1  O  VAL X  53   N  GLU X  21
SHEET    4  BQ 4 GLU X  59  LEU X  64 -1  O  LEU X  64   N  GLY X  48
SHEET    1  BR12 ALA c  28  GLN c  32  0
SHEET    2  BR12 ARG c  37  GLN c  44 -1  O  LEU c  40   N  LEU c  29
SHEET    3  BR12 ILE c  50  ALA c  55 -1  O  ARG c  52   N  GLN c  43
SHEET    4  BR12 VAL c  12  GLU c  16 -1  N  VAL c  15   O  VAL c  51
SHEET    5  BR12 LYS c   4  ILE c   9 -1  N  GLN c   7   O  ASP c  14
SHEET    6  BR12 ARG Y  59  LEU Y  66 -1  N  LEU Y  66   O  VAL c   8
SHEET    7  BR12 VAL Y  71  VAL Y  75 -1  O  GLY Y  72   N  ASN Y  65
SHEET    8  BR12 VAL Y  38  GLY Y  43 -1  N  ILE Y  41   O  VAL Y  71
SHEET    9  BR12 GLU Y  28  SER Y  35 -1  N  VAL Y  32   O  ARG Y  40
SHEET   10  BR12 LYS Y  87  LYS Y  89 -1  O  VAL Y  88   N  GLY Y  29
SHEET   11  BR12 MET Y  52  LEU Y  55 -1  N  SER Y  54   O  LYS Y  89
SHEET   12  BR12 ARG Y  59  LEU Y  66 -1  O  ALA Y  61   N  ILE Y  53
SHEET    1  BS 2 GLU Y  96  PRO Y  98  0
SHEET    2  BS 2 PHE Y 126  ALA Y 128 -1  O  SER Y 127   N  VAL Y  97
SHEET    1  BT 6 VAL Y 107  ASN Y 109  0
SHEET    2  BT 6 THR Y 221  ALA Y 226  1  O  VAL Y 225   N  VAL Y 108
SHEET    3  BT 6 LYS Y 192  ILE Y 198  1  N  ALA Y 197   O  VAL Y 224
SHEET    4  BT 6 ASP Y 255  ASP Y 261  1  O  LEU Y 257   N  LYS Y 192
SHEET    5  BT 6 GLY Y 322  ALA Y 326  1  O  THR Y 325   N  ILE Y 258
SHEET    6  BT 6 ARG Y 303  VAL Y 304 -1  N  VAL Y 304   O  GLY Y 322
SHEET    1  BU 4 ILE Y 329  GLU Y 331  0
SHEET    2  BU 4 LEU Y 166  GLY Y 169  1  N  ILE Y 167   O  ILE Y 330
SHEET    3  BU 4 GLY Y 351  LEU Y 355  1  O  ILE Y 353   N  LEU Y 166
SHEET    4  BU 4 VAL Y 374  SER Y 375 -1  O  VAL Y 374   N  GLN Y 352
SHEET    1  BV 7 GLY Z  29  SER Z  35  0
SHEET    2  BV 7 VAL Z  38  GLY Z  43 -1  O  ARG Z  40   N  VAL Z  32
SHEET    3  BV 7 SER Z  70  VAL Z  75 -1  O  VAL Z  71   N  ILE Z  41
SHEET    4  BV 7 TYR Z  60  ALA Z  63 -1  N  ILE Z  62   O  VAL Z  74
SHEET    5  BV 7 GLU Z  51  SER Z  54 -1  N  ILE Z  53   O  ALA Z  61
SHEET    6  BV 7 LYS Z  87  ILE Z  94 -1  O  LYS Z  89   N  SER Z  54
SHEET    7  BV 7 GLY Z  29  SER Z  35 -1  N  GLY Z  29   O  VAL Z  88
SHEET    1  BW 8 ASN Z  65  LEU Z  66  0
SHEET    2  BW 8 GLY d   3  ILE d   9 -1  O  VAL d   8   N  LEU Z  66
SHEET    3  BW 8 ASP d  67  ASP d  70 -1  O  VAL d  68   N  GLY d   3
SHEET    4  BW 8 ALA d  28  GLN d  32 -1  N  GLU d  30   O  LYS d  69
SHEET    5  BW 8 ARG d  37  GLN d  44 -1  O  LEU d  40   N  LEU d  29
SHEET    6  BW 8 ILE d  50  ALA d  55 -1  O  ARG d  52   N  GLN d  43
SHEET    7  BW 8 VAL d  12  GLU d  16 -1  N  VAL d  15   O  VAL d  51
SHEET    8  BW 8 GLY d   3  ILE d   9 -1  N  ILE d   9   O  VAL d  12
SHEET    1  BX 6 ILE Z 115  ASP Z 116  0
SHEET    2  BX 6 VAL Z 107  ASN Z 109 -1  N  VAL Z 107   O  ASP Z 116
SHEET    3  BX 6 THR Z 221  THR Z 227  1  O  VAL Z 225   N  VAL Z 108
SHEET    4  BX 6 LYS Z 192  GLN Z 200  1  N  GLY Z 199   O  ALA Z 226
SHEET    5  BX 6 ASP Z 255  ASP Z 261  1  O  LEU Z 257   N  LYS Z 192
SHEET    6  BX 6 SER Z 323  ALA Z 326  1  O  THR Z 325   N  ALA Z 256
SHEET    1  BY 4 ILE Z 329  GLU Z 331  0
SHEET    2  BY 4 LEU Z 166  GLY Z 169  1  N  GLY Z 169   O  ILE Z 330
SHEET    3  BY 4 GLY Z 351  LEU Z 355  1  O  LEU Z 355   N  ILE Z 168
SHEET    4  BY 4 VAL Z 374  SER Z 375 -1  O  VAL Z 374   N  GLN Z 352
SHEET    1  BZ14 TYR a  60  GLU a  67  0
SHEET    2  BZ14 MET a  52  SER a  54 -1  N  ILE a  53   O  ALA a  61
SHEET    3  BZ14 LYS a  87  CYS a  90 -1  O  LYS a  89   N  SER a  54
SHEET    4  BZ14 GLU a  28  SER a  35 -1  N  GLY a  29   O  VAL a  88
SHEET    5  BZ14 VAL a  38  GLY a  43 -1  O  VAL a  38   N  SER a  35
SHEET    6  BZ14 SER a  70  VAL a  75 -1  O  ALA a  73   N  ILE a  39
SHEET    7  BZ14 TYR a  60  GLU a  67 -1  N  ASN a  65   O  GLY a  72
SHEET    8  BZ14 GLY b   3  ILE b   9 -1  O  VAL b   8   N  LEU a  66
SHEET    9  BZ14 ASP b  67  ASP b  70 -1  O  VAL b  68   N  GLY b   3
SHEET   10  BZ14 ALA b  28  GLN b  32 -1  N  GLU b  30   O  LYS b  69
SHEET   11  BZ14 ARG b  37  GLN b  44 -1  O  LEU b  40   N  LEU b  29
SHEET   12  BZ14 ILE b  50  ALA b  55 -1  O  ARG b  52   N  GLN b  43
SHEET   13  BZ14 VAL b  12  GLU b  16 -1  N  VAL b  15   O  VAL b  51
SHEET   14  BZ14 GLY b   3  ILE b   9 -1  N  ILE b   9   O  VAL b  12
SHEET    1  CA 2 GLU a  96  PRO a  98  0
SHEET    2  CA 2 PHE a 126  ALA a 128 -1  O  SER a 127   N  VAL a  97
SHEET    1  CB 6 VAL a 107  VAL a 108  0
SHEET    2  CB 6 THR a 221  ALA a 226  1  O  VAL a 223   N  VAL a 108
SHEET    3  CB 6 LYS a 192  ILE a 198  1  N  ALA a 197   O  VAL a 224
SHEET    4  CB 6 ASP a 255  ASP a 261  1  O  LEU a 257   N  LYS a 192
SHEET    5  CB 6 GLY a 322  ALA a 326  1  O  THR a 325   N  ALA a 256
SHEET    6  CB 6 ARG a 303  VAL a 304 -1  N  VAL a 304   O  GLY a 322
SHEET    1  CC 4 ILE a 329  THR a 332  0
SHEET    2  CC 4 GLU a 165  ASP a 170  1  N  ILE a 167   O  ILE a 330
SHEET    3  CC 4 GLY a 351  LEU a 355  1  O  GLY a 351   N  LEU a 166
SHEET    4  CC 4 VAL a 374  SER a 375 -1  O  VAL a 374   N  GLN a 352
SHEET    1  CD 2 GLU b  76  VAL b  77  0
SHEET    2  CD 2 TRP b 107  ALA b 108 -1  O  TRP b 107   N  VAL b  77
SHEET    1  CE 7 VAL b 202  TYR b 206  0
SHEET    2  CE 7 SER b 174  GLY b 178  1  N  PHE b 176   O  VAL b 205
SHEET    3  CE 7 ASP b 236  VAL b 241  1  O  PHE b 240   N  VAL b 175
SHEET    4  CE 7 SER b 289  TYR b 297  1  O  THR b 291   N  VAL b 237
SHEET    5  CE 7 LYS b 144  GLY b 149  1  N  VAL b 145   O  SER b 292
SHEET    6  CE 7 ALA b 317  VAL b 320  1  O  VAL b 319   N  GLY b 146
SHEET    7  CE 7 THR b 340  SER b 341 -1  O  THR b 340   N  THR b 318
SHEET    1  CF 2 GLU c  76  PRO c  78  0
SHEET    2  CF 2 ARG c 106  ALA c 108 -1  O  TRP c 107   N  VAL c  77
SHEET    1  CG 7 ILE c  87  MET c  88  0
SHEET    2  CG 7 VAL c 202  GLY c 207  1  O  TYR c 206   N  MET c  88
SHEET    3  CG 7 SER c 174  VAL c 179  1  N  GLY c 178   O  VAL c 205
SHEET    4  CG 7 ASP c 236  VAL c 241  1  O  LEU c 238   N  VAL c 175
SHEET    5  CG 7 SER c 289  ALA c 295  1  O  THR c 291   N  VAL c 237
SHEET    6  CG 7 LYS c 144  PHE c 148  1  N  LEU c 147   O  GLN c 294
SHEET    7  CG 7 ALA c 317  VAL c 320  1  O  VAL c 319   N  GLY c 146
SHEET    1  CH 2 LEU c 125  LEU c 126  0
SHEET    2  CH 2 PHE c 139  ALA c 140 -1  O  PHE c 139   N  LEU c 126
SHEET    1  CI 2 LEU d 125  LEU d 126  0
SHEET    2  CI 2 PHE d 139  ALA d 140 -1  O  PHE d 139   N  LEU d 126
SHEET    1  CJ 7 TYR d 206  GLN d 208  0
SHEET    2  CJ 7 TYR d 173  GLU d 181  1  N  GLY d 180   O  GLY d 207
SHEET    3  CJ 7 ASP d 236  ASP d 242  1  O  LEU d 238   N  VAL d 175
SHEET    4  CJ 7 SER d 289  ALA d 295  1  O  THR d 291   N  LEU d 239
SHEET    5  CJ 7 LYS d 144  GLY d 149  1  N  LEU d 147   O  GLN d 294
SHEET    6  CJ 7 ALA d 317  LEU d 321  1  O  LEU d 321   N  PHE d 148
SHEET    7  CJ 7 THR d 340  SER d 341 -1  O  THR d 340   N  THR d 318
SHEET    1  CK 5 VAL e 132  VAL e 136  0
SHEET    2  CK 5 GLN e 111  ILE e 117  1  N  MET e 116   O  ALA e 134
SHEET    3  CK 5 ARG e  74  VAL e  80  1  N  TYR e  77   O  ALA e 115
SHEET    4  CK 5 LYS e 166  ASN e 176  1  O  VAL e 170   N  VAL e  80
SHEET    5  CK 5 SER e 179  LEU e 187 -1  O  SER e 185   N  ILE e 169
SHEET    1  CL 7 GLU f  31  ILE f  34  0
SHEET    2  CL 7 GLN f  14  GLY f  27 -1  N  VAL f  25   O  LEU f  32
SHEET    3  CL 7 TYR f   4  SER f  10 -1  N  TYR f   4   O  VAL f  20
SHEET    4  CL 7 ASN f  75  ALA f  80  1  O  VAL f  78   N  ASP f   7
SHEET    5  CL 7 GLY f  67  GLN f  72 -1  N  GLN f  72   O  ASN f  75
SHEET    6  CL 7 LEU f  41  LYS f  54 -1  N  THR f  43   O  LEU f  69
SHEET    7  CL 7 GLU f  59  LEU f  64 -1  O  LEU f  64   N  GLY f  48
SHEET    1  CM 4 GLU f  31  ILE f  34  0
SHEET    2  CM 4 GLN f  14  GLY f  27 -1  N  VAL f  25   O  LEU f  32
SHEET    3  CM 4 LEU f  41  LYS f  54 -1  O  VAL f  53   N  GLU f  21
SHEET    4  CM 4 GLU f  59  LEU f  64 -1  O  LEU f  64   N  GLY f  48
LINK         O2G ANP S 600                MG    MG S 601     1555   1555  1.93
LINK         O2G ANP a 600                MG    MG a 601     1555   1555  1.93
LINK         OG1 THR K 176                MG    MG K 601     1555   1555  1.96
LINK        MG    MG L 601                 O3  SO4 L 630     1555   1555  2.00
LINK         O2G ANP K 600                MG    MG K 601     1555   1555  2.00
LINK         O2G ANP Y 600                MG    MG Y 601     1555   1555  2.00
LINK         OG1 THR I 176                MG    MG I 601     1555   1555  2.00
LINK         OG1 THR Y 176                MG    MG Y 601     1555   1555  2.02
LINK         O2G ANP C 600                MG    MG C 601     1555   1555  2.02
LINK         OG1 THR C 176                MG    MG C 601     1555   1555  2.02
LINK         OG1 THR S 176                MG    MG S 601     1555   1555  2.02
LINK         O2G ANP I 600                MG    MG I 601     1555   1555  2.03
LINK         O2G ANP A 600                MG    MG A 601     1555   1555  2.03
LINK         O2G ANP Q 600                MG    MG Q 601     1555   1555  2.04
LINK         OG1 THR B 176                MG    MG B 601     1555   1555  2.05
LINK         OG1 THR T 156                MG    MG T 601     1555   1555  2.05
LINK         O2G ANP J 600                MG    MG J 601     1555   1555  2.05
LINK         O2G ANP R 600                MG    MG R 601     1555   1555  2.05
LINK        MG    MG D 601                 O3  SO4 D 630     1555   1555  2.05
LINK         OG1 THR b 156                MG    MG b 601     1555   1555  2.05
LINK        MG    MG b 601                 O3  SO4 b 630     1555   1555  2.05
LINK         O2B ANP K 600                MG    MG K 601     1555   1555  2.07
LINK         O2G ANP Z 600                MG    MG Z 601     1555   1555  2.07
LINK         OG1 THR L 156                MG    MG L 601     1555   1555  2.07
LINK         O2G ANP B 600                MG    MG B 601     1555   1555  2.08
LINK         OG1 THR R 176                MG    MG R 601     1555   1555  2.09
LINK         O2B ANP S 600                MG    MG S 601     1555   1555  2.10
LINK         OG1 THR J 176                MG    MG J 601     1555   1555  2.10
LINK         OG1 THR D 156                MG    MG D 601     1555   1555  2.11
LINK         OG1 THR A 176                MG    MG A 601     1555   1555  2.11
LINK         OG1 THR Q 176                MG    MG Q 601     1555   1555  2.12
LINK         OG1 THR a 176                MG    MG a 601     1555   1555  2.13
LINK         O2B ANP Z 600                MG    MG Z 601     1555   1555  2.16
LINK         OG1 THR Z 176                MG    MG Z 601     1555   1555  2.17
LINK         O2B ANP R 600                MG    MG R 601     1555   1555  2.17
LINK         O2B ANP J 600                MG    MG J 601     1555   1555  2.17
LINK         O2B ANP I 600                MG    MG I 601     1555   1555  2.20
LINK         O2B ANP C 600                MG    MG C 601     1555   1555  2.20
LINK         O2B ANP a 600                MG    MG a 601     1555   1555  2.22
LINK        MG    MG T 601                 O3  SO4 T 630     1555   1555  2.22
LINK         O2B ANP B 600                MG    MG B 601     1555   1555  2.25
LINK         O2B ANP Q 600                MG    MG Q 601     1555   1555  2.25
LINK         O2B ADP b 600                MG    MG b 601     1555   1555  2.27
LINK         O2B ADP T 600                MG    MG T 601     1555   1555  2.28
LINK         O2B ADP L 600                MG    MG L 601     1555   1555  2.28
LINK         O2B ADP D 600                MG    MG D 601     1555   1555  2.29
LINK         O2B ANP A 600                MG    MG A 601     1555   1555  2.44
LINK         O2B ANP Y 600                MG    MG Y 601     1555   1555  2.46
CISPEP   1 ILE A  137    GLU A  138          0        23.86
CISPEP   2 GLY B   57    ASN B   58          0         2.96
CISPEP   3 ASP B  116    GLY B  117          0        -1.02
CISPEP   4 GLY B  216    ALA B  217          0         0.70
CISPEP   5 LYS C  314    GLY C  315          0        -1.40
CISPEP   6 VAL C  317    LYS C  318          0         4.44
CISPEP   7 SER D  120    ASN D  121          0         0.10
CISPEP   8 THR D  128    GLY D  129          0        -1.33
CISPEP   9 ASP D  200    LYS D  201          0         3.56
CISPEP  10 GLU D  432    GLY D  433          0        -2.60
CISPEP  11 GLY J   57    ASN J   58          0         2.87
CISPEP  12 ASP J  116    GLY J  117          0        -1.04
CISPEP  13 GLY J  216    ALA J  217          0         0.67
CISPEP  14 LYS K  314    GLY K  315          0        -1.35
CISPEP  15 VAL K  317    LYS K  318          0         4.47
CISPEP  16 SER L  120    ASN L  121          0         0.17
CISPEP  17 THR L  128    GLY L  129          0        -1.40
CISPEP  18 ASP L  200    LYS L  201          0         3.57
CISPEP  19 GLU L  432    GLY L  433          0        -1.30
CISPEP  20 GLY R   57    ASN R   58          0         2.98
CISPEP  21 ASP R  116    GLY R  117          0        -1.03
CISPEP  22 GLY R  216    ALA R  217          0         0.64
CISPEP  23 LYS S  314    GLY S  315          0        -1.38
CISPEP  24 VAL S  317    LYS S  318          0         4.48
CISPEP  25 SER T  120    ASN T  121          0         0.17
CISPEP  26 THR T  128    GLY T  129          0        -1.23
CISPEP  27 ASP T  200    LYS T  201          0         3.62
CISPEP  28 GLU T  432    GLY T  433          0        -2.50
CISPEP  29 GLY Z   57    ASN Z   58          0         2.98
CISPEP  30 ASP Z  116    GLY Z  117          0        -1.01
CISPEP  31 GLY Z  216    ALA Z  217          0         0.68
CISPEP  32 LYS a  314    GLY a  315          0        -1.36
CISPEP  33 VAL a  317    LYS a  318          0         4.47
CISPEP  34 SER b  120    ASN b  121          0         0.12
CISPEP  35 THR b  128    GLY b  129          0        -1.30
CISPEP  36 ASP b  200    LYS b  201          0         3.66
CISPEP  37 GLU b  432    GLY b  433          0        -1.96
SITE     1 AC1 14 GLN A 172  THR A 173  GLY A 174  LYS A 175
SITE     2 AC1 14 THR A 176  ALA A 177  GLU A 331  PHE A 360
SITE     3 AC1 14 ARG A 365  GLN A 433  LYS A 434  GLN A 435
SITE     4 AC1 14  MG A 601  ARG D 342
SITE     1 AC2  3 THR A 176  ASP A 261  ANP A 600
SITE     1 AC3 14 GLN B 172  THR B 173  GLY B 174  LYS B 175
SITE     2 AC3 14 THR B 176  ALA B 177  GLU B 331  PHE B 360
SITE     3 AC3 14 ARG B 365  GLN B 433  LYS B 434  GLN B 435
SITE     4 AC3 14  MG B 601  ARG E 342
SITE     1 AC4  2 THR B 176  ANP B 600
SITE     1 AC5 13 ARG C 171  GLN C 172  THR C 173  GLY C 174
SITE     2 AC5 13 LYS C 175  THR C 176  ALA C 177  PHE C 360
SITE     3 AC5 13 ARG C 365  GLN C 433  GLN C 435   MG C 601
SITE     4 AC5 13 TYR F 354
SITE     1 AC6  2 THR C 176  ANP C 600
SITE     1 AC7 14 ARG C 376  GLY D 150  ALA D 151  GLY D 152
SITE     2 AC7 14 VAL D 153  GLY D 154  LYS D 155  THR D 156
SITE     3 AC7 14 VAL D 157  TYR D 331  ALA D 407  THR D 411
SITE     4 AC7 14  MG D 601  SO4 D 630
SITE     1 AC8  4 THR D 156  GLU D 185  ADP D 600  SO4 D 630
SITE     1 AC9  7 ARG C 376  LYS D 155  ARG D 182  ASN D 243
SITE     2 AC9  7 ARG D 246  ADP D 600   MG D 601
SITE     1 BC1  6 GLY E 150  GLY E 152  VAL E 153  GLY E 154
SITE     2 BC1  6 LYS E 155  THR E 156
SITE     1 BC2  6 GLY F 152  VAL F 153  GLY F 154  LYS F 155
SITE     2 BC2  6 THR F 156  ARG F 182
SITE     1 BC3  5 SER G  81  ASP G  83  MET G 139  GLY G 140
SITE     2 BC3  5 VAL G 231
SITE     1 BC4  4 MET H  15  TYR H  63  SER H  65  ASP H  81
SITE     1 BC5 13 GLN I 172  THR I 173  GLY I 174  LYS I 175
SITE     2 BC5 13 THR I 176  ALA I 177  GLU I 331  PHE I 360
SITE     3 BC5 13 ARG I 365  GLN I 433  LYS I 434  GLN I 435
SITE     4 BC5 13  MG I 601
SITE     1 BC6  3 THR I 176  ASP I 261  ANP I 600
SITE     1 BC7 14 GLN J 172  THR J 173  GLY J 174  LYS J 175
SITE     2 BC7 14 THR J 176  ALA J 177  PHE J 360  ARG J 365
SITE     3 BC7 14 GLN J 433  LYS J 434  GLN J 435   MG J 601
SITE     4 BC7 14 ARG M 342  PRO M 346
SITE     1 BC8  3 THR J 176  GLN J 200  ANP J 600
SITE     1 BC9 14 ARG K 171  GLN K 172  THR K 173  GLY K 174
SITE     2 BC9 14 LYS K 175  THR K 176  ALA K 177  GLU K 331
SITE     3 BC9 14 PHE K 360  ARG K 365  GLN K 433  GLN K 435
SITE     4 BC9 14  MG K 601  TYR N 354
SITE     1 CC1  2 THR K 176  ANP K 600
SITE     1 CC2 14 ARG K 376  GLY L 150  ALA L 151  GLY L 152
SITE     2 CC2 14 VAL L 153  GLY L 154  LYS L 155  THR L 156
SITE     3 CC2 14 VAL L 157  TYR L 331  ALA L 407  THR L 411
SITE     4 CC2 14  MG L 601  SO4 L 630
SITE     1 CC3  4 THR L 156  GLU L 185  ADP L 600  SO4 L 630
SITE     1 CC4  7 ARG K 376  LYS L 155  ARG L 182  ASN L 243
SITE     2 CC4  7 ARG L 246  ADP L 600   MG L 601
SITE     1 CC5  6 GLY M 150  GLY M 152  VAL M 153  GLY M 154
SITE     2 CC5  6 LYS M 155  THR M 156
SITE     1 CC6  6 GLY N 152  VAL N 153  GLY N 154  LYS N 155
SITE     2 CC6  6 THR N 156  ARG N 182
SITE     1 CC7  2 SER O  81  ASP O  83
SITE     1 CC8  4 MET P  15  SER P  65  ASP P  81  THR P  82
SITE     1 CC9 13 GLN Q 172  THR Q 173  GLY Q 174  LYS Q 175
SITE     2 CC9 13 THR Q 176  ALA Q 177  GLU Q 331  PHE Q 360
SITE     3 CC9 13 ARG Q 365  GLN Q 433  GLN Q 435   MG Q 601
SITE     4 CC9 13 ARG T 342
SITE     1 DC1  3 THR Q 176  ASP Q 261  ANP Q 600
SITE     1 DC2 15 TYR R 150  GLN R 172  THR R 173  GLY R 174
SITE     2 DC2 15 LYS R 175  THR R 176  ALA R 177  PHE R 360
SITE     3 DC2 15 ARG R 365  GLN R 433  LYS R 434  GLN R 435
SITE     4 DC2 15  MG R 601  ARG U 342  PRO U 346
SITE     1 DC3  3 THR R 176  GLN R 200  ANP R 600
SITE     1 DC4 13 ARG S 171  GLN S 172  THR S 173  GLY S 174
SITE     2 DC4 13 LYS S 175  THR S 176  ALA S 177  PHE S 360
SITE     3 DC4 13 ARG S 365  GLN S 433  GLN S 435   MG S 601
SITE     4 DC4 13 TYR V 354
SITE     1 DC5  2 THR S 176  ANP S 600
SITE     1 DC6 13 ARG S 376  GLY T 150  ALA T 151  GLY T 152
SITE     2 DC6 13 VAL T 153  GLY T 154  LYS T 155  THR T 156
SITE     3 DC6 13 VAL T 157  TYR T 331  ALA T 407   MG T 601
SITE     4 DC6 13 SO4 T 630
SITE     1 DC7  4 THR T 156  GLU T 185  ADP T 600  SO4 T 630
SITE     1 DC8  7 ARG S 376  LYS T 155  ARG T 182  ASN T 243
SITE     2 DC8  7 ARG T 246  ADP T 600   MG T 601
SITE     1 DC9  6 GLY U 150  GLY U 152  VAL U 153  GLY U 154
SITE     2 DC9  6 LYS U 155  THR U 156
SITE     1 EC1  7 ARG R 376  GLY V 152  VAL V 153  GLY V 154
SITE     2 EC1  7 LYS V 155  THR V 156  ARG V 182
SITE     1 EC2  5 SER W  81  THR W  82  ASP W  83  GLY W 140
SITE     2 EC2  5 ASN W 234
SITE     1 EC3 13 GLN Y 172  THR Y 173  GLY Y 174  LYS Y 175
SITE     2 EC3 13 THR Y 176  ALA Y 177  GLU Y 331  PHE Y 360
SITE     3 EC3 13 ARG Y 365  GLN Y 433  LYS Y 434  GLN Y 435
SITE     4 EC3 13  MG Y 601
SITE     1 EC4  3 THR Y 176  ASP Y 261  ANP Y 600
SITE     1 EC5 15 TYR Z 150  GLN Z 172  THR Z 173  GLY Z 174
SITE     2 EC5 15 LYS Z 175  THR Z 176  ALA Z 177  PHE Z 360
SITE     3 EC5 15 ARG Z 365  GLN Z 433  LYS Z 434  GLN Z 435
SITE     4 EC5 15  MG Z 601  ARG c 342  PRO c 346
SITE     1 EC6  3 THR Z 176  GLN Z 200  ANP Z 600
SITE     1 EC7 14 ARG a 171  GLN a 172  THR a 173  GLY a 174
SITE     2 EC7 14 LYS a 175  THR a 176  ALA a 177  PHE a 360
SITE     3 EC7 14 ARG a 365  GLN a 433  LYS a 434  GLN a 435
SITE     4 EC7 14  MG a 601  TYR d 354
SITE     1 EC8  2 THR a 176  ANP a 600
SITE     1 EC9 12 ARG a 376  GLY b 150  ALA b 151  GLY b 152
SITE     2 EC9 12 GLY b 154  LYS b 155  THR b 156  VAL b 157
SITE     3 EC9 12 TYR b 331  ALA b 407   MG b 601  SO4 b 630
SITE     1 FC1  4 THR b 156  GLU b 185  ADP b 600  SO4 b 630
SITE     1 FC2  7 ARG a 376  LYS b 155  ARG b 182  ASN b 243
SITE     2 FC2  7 ARG b 246  ADP b 600   MG b 601
SITE     1 FC3  6 GLY c 150  GLY c 152  VAL c 153  GLY c 154
SITE     2 FC3  6 LYS c 155  THR c 156
SITE     1 FC4  7 ARG Z 376  GLY d 152  VAL d 153  GLY d 154
SITE     2 FC4  7 LYS d 155  THR d 156  ARG d 182
CRYST1  435.970  183.000  225.390  90.00 108.99  90.00 C 1 2 1      48
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.002294  0.000000  0.000789        0.00000
SCALE2      0.000000  0.005464  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004692        0.00000
      
PROCHECK
Go to PROCHECK summary
 References