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PDBsum entry 3hkz

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Transferase PDB id
3hkz
Jmol
Contents
Protein chains
836 a.a.
370 a.a.
1090 a.a.
264 a.a.
176 a.a.
89 a.a.
113 a.a.
74 a.a.
82 a.a.
92 a.a.
64 a.a.
43 a.a.
45 a.a.
Ligands
F3S ×2
Metals
_MG ×2
_ZN ×10
HEADER    TRANSFERASE                             26-MAY-09   3HKZ
TITLE     THE X-RAY CRYSTAL STRUCTURE OF RNA POLYMERASE FROM ARCHAEA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT A';
COMPND   3 CHAIN: A, I;
COMPND   4 EC: 2.7.7.6;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT A'';
COMPND   7 CHAIN: C, M;
COMPND   8 EC: 2.7.7.6;
COMPND   9 MOL_ID: 3;
COMPND  10 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT B;
COMPND  11 CHAIN: B, J;
COMPND  12 MOL_ID: 4;
COMPND  13 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT D;
COMPND  14 CHAIN: D, O;
COMPND  15 EC: 2.7.7.6;
COMPND  16 MOL_ID: 5;
COMPND  17 MOLECULE: DNA-DIRECTED RNA POLYMERASE, SUBUNIT E' (RPOE1);
COMPND  18 CHAIN: E, Q;
COMPND  19 EC: 2.7.7.6;
COMPND  20 MOL_ID: 6;
COMPND  21 MOLECULE: DNA-DIRECTED RNA POLYMERASE, SUBUNIT F (RPOF);
COMPND  22 CHAIN: F, R;
COMPND  23 SYNONYM: PUTATIVE UNCHARACTERIZED PROTEIN ORF-C20_042;
COMPND  24 EC: 2.7.7.6;
COMPND  25 MOL_ID: 7;
COMPND  26 MOLECULE: DNA-DIRECTED RNA POLYMERASE, SUBUNIT G (RPOG);
COMPND  27 CHAIN: G, S;
COMPND  28 EC: 2.7.7.6;
COMPND  29 MOL_ID: 8;
COMPND  30 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT H;
COMPND  31 CHAIN: H, T;
COMPND  32 EC: 2.7.7.6;
COMPND  33 MOL_ID: 9;
COMPND  34 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT K;
COMPND  35 CHAIN: K, U;
COMPND  36 EC: 2.7.7.6;
COMPND  37 MOL_ID: 10;
COMPND  38 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT L;
COMPND  39 CHAIN: L, V;
COMPND  40 EC: 2.7.7.6;
COMPND  41 MOL_ID: 11;
COMPND  42 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT N;
COMPND  43 CHAIN: N, W;
COMPND  44 EC: 2.7.7.6;
COMPND  45 MOL_ID: 12;
COMPND  46 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT P;
COMPND  47 CHAIN: P, X;
COMPND  48 EC: 2.7.7.6;
COMPND  49 MOL_ID: 13;
COMPND  50 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT 13;
COMPND  51 CHAIN: Y, Z
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE   3 ORGANISM_TAXID: 273057;
SOURCE   4 STRAIN: P2;
SOURCE   5 MOL_ID: 2;
SOURCE   6 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE   7 ORGANISM_TAXID: 273057;
SOURCE   8 STRAIN: P2;
SOURCE   9 MOL_ID: 3;
SOURCE  10 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE  11 ORGANISM_TAXID: 273057;
SOURCE  12 STRAIN: P2;
SOURCE  13 MOL_ID: 4;
SOURCE  14 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE  15 ORGANISM_TAXID: 273057;
SOURCE  16 STRAIN: P2;
SOURCE  17 MOL_ID: 5;
SOURCE  18 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE  19 ORGANISM_TAXID: 273057;
SOURCE  20 STRAIN: P2;
SOURCE  21 MOL_ID: 6;
SOURCE  22 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE  23 ORGANISM_TAXID: 273057;
SOURCE  24 STRAIN: P2;
SOURCE  25 MOL_ID: 7;
SOURCE  26 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE  27 ORGANISM_TAXID: 273057;
SOURCE  28 STRAIN: P2;
SOURCE  29 MOL_ID: 8;
SOURCE  30 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE  31 ORGANISM_TAXID: 273057;
SOURCE  32 STRAIN: P2;
SOURCE  33 MOL_ID: 9;
SOURCE  34 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE  35 ORGANISM_TAXID: 273057;
SOURCE  36 STRAIN: P2;
SOURCE  37 MOL_ID: 10;
SOURCE  38 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE  39 ORGANISM_TAXID: 273057;
SOURCE  40 STRAIN: P2;
SOURCE  41 MOL_ID: 11;
SOURCE  42 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE  43 ORGANISM_TAXID: 273057;
SOURCE  44 STRAIN: P2;
SOURCE  45 MOL_ID: 12;
SOURCE  46 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE  47 ORGANISM_TAXID: 273057;
SOURCE  48 STRAIN: P2;
SOURCE  49 MOL_ID: 13;
SOURCE  50 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE  51 ORGANISM_TAXID: 273057;
SOURCE  52 STRAIN: P2
KEYWDS    RNA POLYMERASE, ARCHAEA, SULFOLOBUS SOLFATARICUS, DNA-
KEYWDS   2 DIRECTED RNA POLYMERASE, METAL-BINDING,
KEYWDS   3 NUCLEOTIDYLTRANSFERASE, TRANSCRIPTION, TRANSFERASE, ZINC,
KEYWDS   4 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.S.MURAKAMI
REVDAT   1   09-JUN-09 3HKZ    0
JRNL        AUTH   A.HIRATA,B.J.KLEIN,K.S.MURAKAMI
JRNL        TITL   THE X-RAY CRYSTAL STRUCTURE OF RNA POLYMERASE FROM
JRNL        TITL 2 ARCHAEA.
JRNL        REF    NATURE                        V. 451   851 2008
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   18235446
JRNL        DOI    10.1038/NATURE06530
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0072
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.3
REMARK   3   NUMBER OF REFLECTIONS             : 100295
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.269
REMARK   3   R VALUE            (WORKING SET) : 0.265
REMARK   3   FREE R VALUE                     : 0.341
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 5323
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.49
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4969
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 54.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3640
REMARK   3   BIN FREE R VALUE SET COUNT          : 239
REMARK   3   BIN FREE R VALUE                    : 0.3830
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 53046
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 26
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 78.87
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.43000
REMARK   3    B22 (A**2) : 1.57000
REMARK   3    B33 (A**2) : -3.83000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -4.84000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.923
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.792
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 49.519
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.867
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.778
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 54012 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 72992 ; 1.612 ; 1.982
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  6636 ; 7.933 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2400 ;39.635 ;23.750
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES): 10044 ;23.339 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   448 ;18.865 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  8328 ; 0.109 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 39986 ; 0.006 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 33222 ; 0.743 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 54006 ; 1.418 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 20790 ; 1.580 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 18980 ; 3.044 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 13
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      4       A     879      2
REMARK   3           1     I      4       I     879      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3344 ; 0.030 ; 0.050
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3329 ; 0.040 ; 0.500
REMARK   3   TIGHT THERMAL      1    A (A**2):   3344 ; 0.050 ; 0.500
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3329 ; 0.060 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : C M
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     C     11       C     395      2
REMARK   3           1     M     11       M     395      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   2    A    (A):   1480 ; 0.350 ; 0.050
REMARK   3   MEDIUM POSITIONAL  2    A    (A):   1388 ; 0.590 ; 0.500
REMARK   3   TIGHT THERMAL      2    A (A**2):   1480 ; 0.350 ; 0.500
REMARK   3   MEDIUM THERMAL     2    A (A**2):   1388 ; 0.440 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 3
REMARK   3     CHAIN NAMES                    : B J
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     B      5       B    1119      2
REMARK   3           1     J      5       J    1119      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   3    A    (A):   4360 ; 0.030 ; 0.050
REMARK   3   MEDIUM POSITIONAL  3    A    (A):   4285 ; 0.040 ; 0.500
REMARK   3   TIGHT THERMAL      3    A (A**2):   4360 ; 0.050 ; 0.500
REMARK   3   MEDIUM THERMAL     3    A (A**2):   4285 ; 0.060 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 4
REMARK   3     CHAIN NAMES                    : D O
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     D      2       D     265      2
REMARK   3           1     O      2       O     265      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   4    A    (A):   1056 ; 0.030 ; 0.050
REMARK   3   MEDIUM POSITIONAL  4    A    (A):   1058 ; 0.030 ; 0.500
REMARK   3   TIGHT THERMAL      4    A (A**2):   1056 ; 0.040 ; 0.500
REMARK   3   MEDIUM THERMAL     4    A (A**2):   1058 ; 0.040 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 5
REMARK   3     CHAIN NAMES                    : E Q
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     E      1       E     180      2
REMARK   3           1     Q      1       Q     180      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   5    A    (A):    704 ; 0.340 ; 0.050
REMARK   3   MEDIUM POSITIONAL  5    A    (A):    698 ; 0.580 ; 0.500
REMARK   3   TIGHT THERMAL      5    A (A**2):    704 ; 0.240 ; 0.500
REMARK   3   MEDIUM THERMAL     5    A (A**2):    698 ; 0.320 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 6
REMARK   3     CHAIN NAMES                    : F R
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     F      1       F      89      2
REMARK   3           1     R      1       R      89      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   6    A    (A):    356 ; 0.410 ; 0.050
REMARK   3   MEDIUM POSITIONAL  6    A    (A):    339 ; 0.700 ; 0.500
REMARK   3   TIGHT THERMAL      6    A (A**2):    356 ; 0.180 ; 0.500
REMARK   3   MEDIUM THERMAL     6    A (A**2):    339 ; 0.260 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 7
REMARK   3     CHAIN NAMES                    : G S
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     G      5       G     117      2
REMARK   3           1     S      5       S     117      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   7    A    (A):    452 ; 0.310 ; 0.050
REMARK   3   MEDIUM POSITIONAL  7    A    (A):    433 ; 0.530 ; 0.500
REMARK   3   TIGHT THERMAL      7    A (A**2):    452 ; 0.290 ; 0.500
REMARK   3   MEDIUM THERMAL     7    A (A**2):    433 ; 0.380 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 8
REMARK   3     CHAIN NAMES                    : H T
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     H      9       H      82      2
REMARK   3           1     T      9       T      82      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   8    A    (A):    296 ; 0.320 ; 0.050
REMARK   3   MEDIUM POSITIONAL  8    A    (A):    316 ; 0.560 ; 0.500
REMARK   3   TIGHT THERMAL      8    A (A**2):    296 ; 0.270 ; 0.500
REMARK   3   MEDIUM THERMAL     8    A (A**2):    316 ; 0.380 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 9
REMARK   3     CHAIN NAMES                    : K U
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     K     11       K      92      2
REMARK   3           1     U     11       U      92      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   9    A    (A):    328 ; 0.280 ; 0.050
REMARK   3   MEDIUM POSITIONAL  9    A    (A):    331 ; 0.540 ; 0.500
REMARK   3   TIGHT THERMAL      9    A (A**2):    328 ; 0.340 ; 0.500
REMARK   3   MEDIUM THERMAL     9    A (A**2):    331 ; 0.570 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 10
REMARK   3     CHAIN NAMES                    : L V
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     L      1       L      92      2
REMARK   3           1     V      1       V      92      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  10    A    (A):    368 ; 0.340 ; 0.050
REMARK   3   MEDIUM POSITIONAL 10    A    (A):    355 ; 0.480 ; 0.500
REMARK   3   TIGHT THERMAL     10    A (A**2):    368 ; 0.440 ; 0.500
REMARK   3   MEDIUM THERMAL    10    A (A**2):    355 ; 0.510 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 11
REMARK   3     CHAIN NAMES                    : N W
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     N      1       N      64      2
REMARK   3           1     W      1       W      64      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  11    A    (A):    256 ; 0.030 ; 0.050
REMARK   3   MEDIUM POSITIONAL 11    A    (A):    258 ; 0.030 ; 0.500
REMARK   3   TIGHT THERMAL     11    A (A**2):    256 ; 0.040 ; 0.500
REMARK   3   MEDIUM THERMAL    11    A (A**2):    258 ; 0.040 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 12
REMARK   3     CHAIN NAMES                    : P X
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     P      6       P      48      2
REMARK   3           1     X      6       X      48      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  12    A    (A):    172 ; 0.030 ; 0.050
REMARK   3   MEDIUM POSITIONAL 12    A    (A):    174 ; 0.030 ; 0.500
REMARK   3   TIGHT THERMAL     12    A (A**2):    172 ; 0.040 ; 0.500
REMARK   3   MEDIUM THERMAL    12    A (A**2):    174 ; 0.040 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 13
REMARK   3     CHAIN NAMES                    : Y Z
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     Y     38       Y      82      2
REMARK   3           1     Z     38       Z      82      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  13    A    (A):    180 ; 0.480 ; 0.050
REMARK   3   MEDIUM POSITIONAL 13    A    (A):    212 ; 0.770 ; 0.500
REMARK   3   TIGHT THERMAL     13    A (A**2):    180 ; 0.190 ; 0.500
REMARK   3   MEDIUM THERMAL    13    A (A**2):    212 ; 0.280 ; 2.000
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3HKZ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAY-09.
REMARK 100 THE RCSB ID CODE IS RCSB053262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU 200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5414
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 105621
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1R9T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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      100.61750
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIDECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D, E, F, G, H, K,
REMARK 350                    AND CHAINS: L, N, P, Y
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: TRIDECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, M, J, O, Q, R, S, T, U,
REMARK 350                    AND CHAINS: V, W, X, Z
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     SER A     2
REMARK 465     GLU A     3
REMARK 465     ASP A    31
REMARK 465     VAL A    32
REMARK 465     TYR A    33
REMARK 465     ASP A    34
REMARK 465     GLU A    35
REMARK 465     ASP A    36
REMARK 465     GLY A    37
REMARK 465     THR A    38
REMARK 465     PRO A    39
REMARK 465     ILE A    40
REMARK 465     GLU A    41
REMARK 465     GLY A    42
REMARK 465     SER A    43
REMARK 465     VAL A    44
REMARK 465     LYS A   157
REMARK 465     LEU A   158
REMARK 465     GLU A   159
REMARK 465     LYS A   160
REMARK 465     PRO A   161
REMARK 465     TYR A   162
REMARK 465     ASN A   163
REMARK 465     PHE A   164
REMARK 465     TYR A   165
REMARK 465     GLU A   166
REMARK 465     GLU A   167
REMARK 465     ARG A   168
REMARK 465     LYS A   169
REMARK 465     GLU A   170
REMARK 465     GLY A   171
REMARK 465     VAL A   172
REMARK 465     ALA A   173
REMARK 465     ILE A   223
REMARK 465     MET A   224
REMARK 465     ILE A   225
REMARK 465     GLU A   226
REMARK 465     SER A   227
REMARK 465     GLY A   228
REMARK 465     ILE A   229
REMARK 465     ARG A   230
REMARK 465     ALA A   231
REMARK 465     ALA A   880
REMARK 465     MET C     1
REMARK 465     GLU C     2
REMARK 465     GLY C     3
REMARK 465     MET C     4
REMARK 465     ILE C     5
REMARK 465     ASP C     6
REMARK 465     GLU C     7
REMARK 465     LYS C     8
REMARK 465     ASP C     9
REMARK 465     LYS C    10
REMARK 465     LEU C    87
REMARK 465     ARG C    88
REMARK 465     THR C    89
REMARK 465     PHE C    90
REMARK 465     HIS C    91
REMARK 465     PHE C    92
REMARK 465     ALA C    93
REMARK 465     GLY C    94
REMARK 465     ILE C    95
REMARK 465     ARG C    96
REMARK 465     GLU C    97
REMARK 465     LEU C    98
REMARK 465     ASN C    99
REMARK 465     VAL C   100
REMARK 465     THR C   101
REMARK 465     MET B     1
REMARK 465     ALA B     2
REMARK 465     SER B     3
REMARK 465     ASN B     4
REMARK 465     ARG B   502
REMARK 465     ARG B   503
REMARK 465     VAL B   504
REMARK 465     THR B   505
REMARK 465     GLU B   506
REMARK 465     GLY B   507
REMARK 465     GLY B   508
REMARK 465     GLU B   509
REMARK 465     ASP B   510
REMARK 465     GLN B   511
REMARK 465     ASN B   512
REMARK 465     GLU B   513
REMARK 465     TYR B   514
REMARK 465     PHE B   819
REMARK 465     LEU B   820
REMARK 465     GLN B   821
REMARK 465     GLU B   822
REMARK 465     PHE B   823
REMARK 465     LYS B   824
REMARK 465     GLU B   825
REMARK 465     LEU B   826
REMARK 465     SER B   827
REMARK 465     PRO B   828
REMARK 465     GLU B   829
REMARK 465     GLN B   830
REMARK 465     GLY B  1120
REMARK 465     LEU B  1121
REMARK 465     SER B  1122
REMARK 465     GLY B  1123
REMARK 465     GLY B  1124
REMARK 465     MET D     1
REMARK 465     THR E   154
REMARK 465     GLY E   155
REMARK 465     ARG E   156
REMARK 465     LEU E   157
REMARK 465     ASP F    90
REMARK 465     THR F    91
REMARK 465     ASN F    92
REMARK 465     LYS F    93
REMARK 465     THR F    94
REMARK 465     TYR F    95
REMARK 465     THR F    96
REMARK 465     SER F    97
REMARK 465     GLU F    98
REMARK 465     ASP F    99
REMARK 465     ILE F   100
REMARK 465     GLN F   101
REMARK 465     LYS F   102
REMARK 465     ILE F   103
REMARK 465     ILE F   104
REMARK 465     ASP F   105
REMARK 465     ILE F   106
REMARK 465     ILE F   107
REMARK 465     ARG F   108
REMARK 465     LYS F   109
REMARK 465     TYR F   110
REMARK 465     ILE F   111
REMARK 465     LYS F   112
REMARK 465     SER F   113
REMARK 465     MET G     1
REMARK 465     MET G     2
REMARK 465     GLU G     3
REMARK 465     SER G     4
REMARK 465     LEU G   118
REMARK 465     ASN G   119
REMARK 465     ILE G   120
REMARK 465     MET G   121
REMARK 465     ASP G   122
REMARK 465     HIS G   123
REMARK 465     VAL G   124
REMARK 465     TYR G   125
REMARK 465     PHE G   126
REMARK 465     CYS G   127
REMARK 465     VAL G   128
REMARK 465     LYS G   129
REMARK 465     LYS G   130
REMARK 465     ASN G   131
REMARK 465     ASN G   132
REMARK 465     MET H     1
REMARK 465     ARG H     2
REMARK 465     GLY H     3
REMARK 465     SER H     4
REMARK 465     SER H     5
REMARK 465     ASN H     6
REMARK 465     LYS H     7
REMARK 465     LYS H     8
REMARK 465     SER H    83
REMARK 465     GLY H    84
REMARK 465     MET K     1
REMARK 465     GLY K     2
REMARK 465     LEU K     3
REMARK 465     GLU K     4
REMARK 465     ARG K     5
REMARK 465     ASP K     6
REMARK 465     GLU K     7
REMARK 465     ILE K     8
REMARK 465     LEU K     9
REMARK 465     SER K    10
REMARK 465     ARG K    93
REMARK 465     LYS K    94
REMARK 465     SER K    95
REMARK 465     PRO N    65
REMARK 465     ILE N    66
REMARK 465     MET P     1
REMARK 465     ALA P     2
REMARK 465     VAL P     3
REMARK 465     TYR P     4
REMARK 465     ARG P     5
REMARK 465     MET Y     1
REMARK 465     VAL Y     2
REMARK 465     SER Y     3
REMARK 465     GLY Y     4
REMARK 465     MET Y     5
REMARK 465     SER Y     6
REMARK 465     THR Y     7
REMARK 465     ASP Y     8
REMARK 465     GLU Y     9
REMARK 465     GLU Y    10
REMARK 465     LYS Y    11
REMARK 465     GLU Y    12
REMARK 465     GLY Y    13
REMARK 465     THR Y    14
REMARK 465     SER Y    15
REMARK 465     ASP Y    16
REMARK 465     GLU Y    17
REMARK 465     GLU Y    18
REMARK 465     VAL Y    19
REMARK 465     ASN Y    20
REMARK 465     GLU Y    21
REMARK 465     GLU Y    22
REMARK 465     LYS Y    23
REMARK 465     GLU Y    24
REMARK 465     VAL Y    25
REMARK 465     GLU Y    26
REMARK 465     GLU Y    27
REMARK 465     THR Y    28
REMARK 465     SER Y    29
REMARK 465     GLU Y    30
REMARK 465     ASP Y    31
REMARK 465     GLU Y    32
REMARK 465     PHE Y    33
REMARK 465     PRO Y    34
REMARK 465     LYS Y    35
REMARK 465     LEU Y    36
REMARK 465     SER Y    37
REMARK 465     LYS Y    83
REMARK 465     ALA Y    84
REMARK 465     LYS Y    85
REMARK 465     LYS Y    86
REMARK 465     ALA Y    87
REMARK 465     VAL Y    88
REMARK 465     SER Y    89
REMARK 465     LYS Y    90
REMARK 465     LYS Y    91
REMARK 465     VAL Y    92
REMARK 465     LYS Y    93
REMARK 465     LYS Y    94
REMARK 465     THR Y    95
REMARK 465     LYS Y    96
REMARK 465     LYS Y    97
REMARK 465     LYS Y    98
REMARK 465     GLU Y    99
REMARK 465     LYS Y   100
REMARK 465     SER Y   101
REMARK 465     VAL Y   102
REMARK 465     GLU Y   103
REMARK 465     GLY Y   104
REMARK 465     MET I     1
REMARK 465     SER I     2
REMARK 465     GLU I     3
REMARK 465     ASP I    31
REMARK 465     VAL I    32
REMARK 465     TYR I    33
REMARK 465     ASP I    34
REMARK 465     GLU I    35
REMARK 465     ASP I    36
REMARK 465     GLY I    37
REMARK 465     THR I    38
REMARK 465     PRO I    39
REMARK 465     ILE I    40
REMARK 465     GLU I    41
REMARK 465     GLY I    42
REMARK 465     SER I    43
REMARK 465     VAL I    44
REMARK 465     LYS I   157
REMARK 465     LEU I   158
REMARK 465     GLU I   159
REMARK 465     LYS I   160
REMARK 465     PRO I   161
REMARK 465     TYR I   162
REMARK 465     ASN I   163
REMARK 465     PHE I   164
REMARK 465     TYR I   165
REMARK 465     GLU I   166
REMARK 465     GLU I   167
REMARK 465     ARG I   168
REMARK 465     LYS I   169
REMARK 465     GLU I   170
REMARK 465     GLY I   171
REMARK 465     VAL I   172
REMARK 465     ALA I   173
REMARK 465     ILE I   223
REMARK 465     MET I   224
REMARK 465     ILE I   225
REMARK 465     GLU I   226
REMARK 465     SER I   227
REMARK 465     GLY I   228
REMARK 465     ILE I   229
REMARK 465     ARG I   230
REMARK 465     ALA I   231
REMARK 465     ALA I   880
REMARK 465     MET M     1
REMARK 465     GLU M     2
REMARK 465     GLY M     3
REMARK 465     MET M     4
REMARK 465     ILE M     5
REMARK 465     ASP M     6
REMARK 465     GLU M     7
REMARK 465     LYS M     8
REMARK 465     ASP M     9
REMARK 465     LYS M    10
REMARK 465     LEU M    87
REMARK 465     ARG M    88
REMARK 465     THR M    89
REMARK 465     PHE M    90
REMARK 465     HIS M    91
REMARK 465     PHE M    92
REMARK 465     ALA M    93
REMARK 465     GLY M    94
REMARK 465     ILE M    95
REMARK 465     ARG M    96
REMARK 465     GLU M    97
REMARK 465     LEU M    98
REMARK 465     ASN M    99
REMARK 465     VAL M   100
REMARK 465     THR M   101
REMARK 465     MET J     1
REMARK 465     ALA J     2
REMARK 465     SER J     3
REMARK 465     ASN J     4
REMARK 465     ARG J   502
REMARK 465     ARG J   503
REMARK 465     VAL J   504
REMARK 465     THR J   505
REMARK 465     GLU J   506
REMARK 465     GLY J   507
REMARK 465     GLY J   508
REMARK 465     GLU J   509
REMARK 465     ASP J   510
REMARK 465     GLN J   511
REMARK 465     ASN J   512
REMARK 465     GLU J   513
REMARK 465     TYR J   514
REMARK 465     PHE J   819
REMARK 465     LEU J   820
REMARK 465     GLN J   821
REMARK 465     GLU J   822
REMARK 465     PHE J   823
REMARK 465     LYS J   824
REMARK 465     GLU J   825
REMARK 465     LEU J   826
REMARK 465     SER J   827
REMARK 465     PRO J   828
REMARK 465     GLU J   829
REMARK 465     GLN J   830
REMARK 465     GLY J  1120
REMARK 465     LEU J  1121
REMARK 465     SER J  1122
REMARK 465     GLY J  1123
REMARK 465     GLY J  1124
REMARK 465     MET O     1
REMARK 465     THR Q   154
REMARK 465     GLY Q   155
REMARK 465     ARG Q   156
REMARK 465     LEU Q   157
REMARK 465     ASP R    90
REMARK 465     THR R    91
REMARK 465     ASN R    92
REMARK 465     LYS R    93
REMARK 465     THR R    94
REMARK 465     TYR R    95
REMARK 465     THR R    96
REMARK 465     SER R    97
REMARK 465     GLU R    98
REMARK 465     ASP R    99
REMARK 465     ILE R   100
REMARK 465     GLN R   101
REMARK 465     LYS R   102
REMARK 465     ILE R   103
REMARK 465     ILE R   104
REMARK 465     ASP R   105
REMARK 465     ILE R   106
REMARK 465     ILE R   107
REMARK 465     ARG R   108
REMARK 465     LYS R   109
REMARK 465     TYR R   110
REMARK 465     ILE R   111
REMARK 465     LYS R   112
REMARK 465     SER R   113
REMARK 465     MET S     1
REMARK 465     MET S     2
REMARK 465     GLU S     3
REMARK 465     SER S     4
REMARK 465     LEU S   118
REMARK 465     ASN S   119
REMARK 465     ILE S   120
REMARK 465     MET S   121
REMARK 465     ASP S   122
REMARK 465     HIS S   123
REMARK 465     VAL S   124
REMARK 465     TYR S   125
REMARK 465     PHE S   126
REMARK 465     CYS S   127
REMARK 465     VAL S   128
REMARK 465     LYS S   129
REMARK 465     LYS S   130
REMARK 465     ASN S   131
REMARK 465     ASN S   132
REMARK 465     MET T     1
REMARK 465     ARG T     2
REMARK 465     GLY T     3
REMARK 465     SER T     4
REMARK 465     SER T     5
REMARK 465     ASN T     6
REMARK 465     LYS T     7
REMARK 465     LYS T     8
REMARK 465     SER T    83
REMARK 465     GLY T    84
REMARK 465     MET U     1
REMARK 465     GLY U     2
REMARK 465     LEU U     3
REMARK 465     GLU U     4
REMARK 465     ARG U     5
REMARK 465     ASP U     6
REMARK 465     GLU U     7
REMARK 465     ILE U     8
REMARK 465     LEU U     9
REMARK 465     SER U    10
REMARK 465     ARG U    93
REMARK 465     LYS U    94
REMARK 465     SER U    95
REMARK 465     PRO W    65
REMARK 465     ILE W    66
REMARK 465     MET X     1
REMARK 465     ALA X     2
REMARK 465     VAL X     3
REMARK 465     TYR X     4
REMARK 465     ARG X     5
REMARK 465     MET Z     1
REMARK 465     VAL Z     2
REMARK 465     SER Z     3
REMARK 465     GLY Z     4
REMARK 465     MET Z     5
REMARK 465     SER Z     6
REMARK 465     THR Z     7
REMARK 465     ASP Z     8
REMARK 465     GLU Z     9
REMARK 465     GLU Z    10
REMARK 465     LYS Z    11
REMARK 465     GLU Z    12
REMARK 465     GLY Z    13
REMARK 465     THR Z    14
REMARK 465     SER Z    15
REMARK 465     ASP Z    16
REMARK 465     GLU Z    17
REMARK 465     GLU Z    18
REMARK 465     VAL Z    19
REMARK 465     ASN Z    20
REMARK 465     GLU Z    21
REMARK 465     GLU Z    22
REMARK 465     LYS Z    23
REMARK 465     GLU Z    24
REMARK 465     VAL Z    25
REMARK 465     GLU Z    26
REMARK 465     GLU Z    27
REMARK 465     THR Z    28
REMARK 465     SER Z    29
REMARK 465     GLU Z    30
REMARK 465     ASP Z    31
REMARK 465     GLU Z    32
REMARK 465     PHE Z    33
REMARK 465     PRO Z    34
REMARK 465     LYS Z    35
REMARK 465     LEU Z    36
REMARK 465     SER Z    37
REMARK 465     LYS Z    83
REMARK 465     ALA Z    84
REMARK 465     LYS Z    85
REMARK 465     LYS Z    86
REMARK 465     ALA Z    87
REMARK 465     VAL Z    88
REMARK 465     SER Z    89
REMARK 465     LYS Z    90
REMARK 465     LYS Z    91
REMARK 465     VAL Z    92
REMARK 465     LYS Z    93
REMARK 465     LYS Z    94
REMARK 465     THR Z    95
REMARK 465     LYS Z    96
REMARK 465     LYS Z    97
REMARK 465     LYS Z    98
REMARK 465     GLU Z    99
REMARK 465     LYS Z   100
REMARK 465     SER Z   101
REMARK 465     VAL Z   102
REMARK 465     GLU Z   103
REMARK 465     GLY Z   104
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     ILE G  58    CG1  CG2  CD1
REMARK 470     ILE S  58    CG1  CG2  CD1
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   SG   CYS N    45    ZN    ZN  N  1001              1.58
REMARK 500   SG   CYS J  1064    ZN    ZN  J  2001              1.62
REMARK 500   SG   CYS O   209    FE1   F3S O  1001              1.69
REMARK 500   O    VAL I   875     N    GLY I   877              2.08
REMARK 500   O    LEU A   841     N    GLY A   843              2.10
REMARK 500   O    ILE I     9     O    VAL M   363              2.10
REMARK 500   O    VAL A   875     N    GLY A   877              2.10
REMARK 500   OH   TYR A    91     O    GLN A   153              2.12
REMARK 500   OH   TYR A   818     OE2  GLU C   348              2.12
REMARK 500   O    LYS M   114     N    VAL M   116              2.13
REMARK 500   O    PRO J   800     N    VAL J   802              2.14
REMARK 500   O    TRP A   206     N    ILE A   208              2.16
REMARK 500   NH1  ARG J    88     O    GLU J   854              2.18
REMARK 500   O    LEU I   841     N    GLY I   843              2.18
REMARK 500   OH   TYR I    91     O    GLN I   153              2.18
REMARK 500   OG1  THR M   127     O    TYR M   130              2.19
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    CYS A  98   CA  -  CB  -  SG  ANGL. DEV. =   8.0 DEGREES
REMARK 500    LEU A 239   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES
REMARK 500    LEU A 464   CA  -  CB  -  CG  ANGL. DEV. =  15.7 DEGREES
REMARK 500    LEU C  54   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES
REMARK 500    LEU B1045   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES
REMARK 500    CYS I  98   CA  -  CB  -  SG  ANGL. DEV. =   7.4 DEGREES
REMARK 500    LEU I 239   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES
REMARK 500    LEU I 464   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES
REMARK 500    LEU J  23   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES
REMARK 500    LEU T  42   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES
REMARK 500    CYS W  10   CA  -  CB  -  SG  ANGL. DEV. =   6.6 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    LYS A   7       71.97   -158.66
REMARK 500    ILE A  27      101.89     46.71
REMARK 500    PRO A  47      -50.15   -121.11
REMARK 500    LEU A  49       54.78   -105.97
REMARK 500    GLU A  53      145.90     68.13
REMARK 500    PRO A  54       87.96    -54.59
REMARK 500    GLN A  56      -38.97    -10.69
REMARK 500    CYS A  58      -95.10   -119.49
REMARK 500    PRO A  59       54.27    -90.54
REMARK 500    THR A  64     -109.83    -58.33
REMARK 500    GLU A  76       87.40     58.43
REMARK 500    PRO A  80       93.98    -33.52
REMARK 500    ALA A  96     -150.80   -107.30
REMARK 500    THR A  97      131.98     68.61
REMARK 500    ARG A  99      -10.30     79.35
REMARK 500    ARG A 100      -29.54   -142.22
REMARK 500    CYS A 101     -141.62   -103.76
REMARK 500    ARG A 103      -91.90     55.48
REMARK 500    LYS A 105     -148.91   -150.48
REMARK 500    ILE A 106     -126.24   -136.99
REMARK 500    TYR A 118       48.09    -78.85
REMARK 500    ILE A 121      -75.75    -47.33
REMARK 500    LYS A 142      -82.95   -105.27
REMARK 500    ALA A 143      -77.82     69.21
REMARK 500    VAL A 145       38.35   -173.82
REMARK 500    HIS A 148     -175.82     61.48
REMARK 500    ASN A 150     -139.35    -71.44
REMARK 500    GLU A 151     -151.91   -155.15
REMARK 500    LYS A 155      161.08    -38.59
REMARK 500    GLU A 185      -34.09    -30.88
REMARK 500    ILE A 194        0.62    -60.00
REMARK 500    THR A 200       -5.56     66.84
REMARK 500    THR A 201      -31.87   -139.37
REMARK 500    MET A 207       -3.87    -37.98
REMARK 500    THR A 218       -0.36    -58.38
REMARK 500    ARG A 220       43.67   -154.34
REMARK 500    LEU A 235       -0.96    -55.23
REMARK 500    HIS A 237      -73.86    -60.04
REMARK 500    ALA A 255     -110.66   -147.15
REMARK 500    GLN A 259       29.81    -74.41
REMARK 500    HIS A 272      -42.53   -136.19
REMARK 500    PHE A 277      -71.98    -90.55
REMARK 500    PRO A 285      114.58    -37.72
REMARK 500    SER A 287      118.20   -175.42
REMARK 500    ARG A 296       74.82   -101.97
REMARK 500    LEU A 298      -52.25    -29.54
REMARK 500    LYS A 303      -79.59    -83.58
REMARK 500    LEU A 313      -62.32    -90.61
REMARK 500    PHE A 320       -0.97     76.48
REMARK 500    SER A 322      134.17   -178.20
REMARK 500    ILE A 332      116.21    107.82
REMARK 500    PRO A 355     -176.54    -49.78
REMARK 500    TRP A 356      -83.71     58.57
REMARK 500    TRP A 372      -80.98    -48.13
REMARK 500    PRO A 373       91.70    -67.06
REMARK 500    ALA A 375       67.77   -158.65
REMARK 500    ASN A 376       82.50    -55.18
REMARK 500    TYR A 377      145.67    130.35
REMARK 500    VAL A 378       69.23   -157.28
REMARK 500    ARG A 384      106.32    -53.27
REMARK 500    ASP A 387      178.53    -58.49
REMARK 500    LEU A 388      -24.91   -147.07
REMARK 500    TYR A 390     -161.39   -115.32
REMARK 500    VAL A 391      103.18     68.76
REMARK 500    LYS A 392      -82.35    -55.50
REMARK 500    ASP A 393     -101.30     22.28
REMARK 500    ARG A 394      -76.59     68.58
REMARK 500    PRO A 403      114.78    -29.04
REMARK 500    LEU A 425       51.03   -112.70
REMARK 500    HIS A 426      109.89    163.37
REMARK 500    LEU A 447      -33.22    -29.79
REMARK 500    ASN A 454       66.89     81.58
REMARK 500    VAL A 482      -77.30    -65.87
REMARK 500    ARG A 490      -65.84    -91.75
REMARK 500    ALA A 499      -88.45   -100.83
REMARK 500    GLN A 500      -78.62   -136.93
REMARK 500    LEU A 508      -57.97    100.18
REMARK 500    THR A 514      -80.04    -55.00
REMARK 500    LEU A 515       88.98     60.55
REMARK 500    ILE A 524       80.67    -63.41
REMARK 500    LEU A 525       43.30   -157.14
REMARK 500    ALA A 528     -110.11    -67.72
REMARK 500    ASP A 529       19.01    -63.83
REMARK 500    VAL A 530      107.77    -47.53
REMARK 500    ILE A 532       -9.79     89.93
REMARK 500    ASP A 533      107.99    -40.47
REMARK 500    LEU A 534      124.35    -12.05
REMARK 500    PRO A 537      132.43    -28.87
REMARK 500    ALA A 541     -124.20    -54.63
REMARK 500    ARG A 543     -175.63     54.42
REMARK 500    SER A 569       84.94    -66.20
REMARK 500    LYS A 576      -57.17     52.98
REMARK 500    SER A 584     -173.08    -69.37
REMARK 500    TYR A 585      106.41     48.24
REMARK 500    GLU A 595      142.37     59.24
REMARK 500    ASP A 599     -161.61   -173.37
REMARK 500    LYS A 601       -9.39    -57.86
REMARK 500    GLN A 606      105.97    -54.31
REMARK 500    GLN A 607      -90.21    -71.37
REMARK 500    PRO A 608     -101.93      7.71
REMARK 500    GLU A 609       43.79   -146.70
REMARK 500    GLU A 618       51.52    -96.28
REMARK 500    ASP A 621        4.93    -55.34
REMARK 500    TRP A 626      -75.01    -54.41
REMARK 500    GLU A 640       -7.74    -59.25
REMARK 500    PHE A 644      137.56     79.82
REMARK 500    THR A 645     -159.70   -179.50
REMARK 500    LEU A 653     -118.02    -98.57
REMARK 500    ASP A 655     -133.35     47.07
REMARK 500    ASN A 681       49.59    -98.25
REMARK 500    PRO A 686     -146.44    -87.56
REMARK 500    PRO A 688       96.95    -38.94
REMARK 500    LEU A 707       34.71    -89.44
REMARK 500    PRO A 721       13.54    -46.52
REMARK 500    ARG A 730      -13.47     74.34
REMARK 500    ALA A 733      -78.18    -16.35
REMARK 500    THR A 741      -77.85    -39.07
REMARK 500    MET A 746      132.67     42.02
REMARK 500    GLN A 749      116.32     57.03
REMARK 500    GLN A 750       68.55   -110.90
REMARK 500    ARG A 753       -5.63     58.98
REMARK 500    ILE A 757       81.31    -68.46
REMARK 500    LYS A 758     -168.11    -73.10
REMARK 500    MET A 762       79.04     50.65
REMARK 500    THR A 763       89.65     42.41
REMARK 500    ARG A 764      -21.65   -175.67
REMARK 500    THR A 765      -53.36     64.49
REMARK 500    PRO A 767        4.61    -63.34
REMARK 500    TYR A 772       76.94     57.28
REMARK 500    ARG A 779       14.11     47.81
REMARK 500    PHE A 781      105.75     70.26
REMARK 500    PHE A 786       -9.87    -53.71
REMARK 500    LEU A 806        4.93    -63.79
REMARK 500    VAL A 807      -46.33   -133.78
REMARK 500    ARG A 821      -38.09    -36.78
REMARK 500    ASN A 825      -89.01    -68.50
REMARK 500    ALA A 826      -64.94    -13.15
REMARK 500    SER A 828      -60.17   -141.02
REMARK 500    ASP A 829       17.75    -51.11
REMARK 500    SER A 840     -112.54   -146.64
REMARK 500    LEU A 841     -142.66    -68.96
REMARK 500    TYR A 842      -36.40      8.30
REMARK 500    ASP A 852      -17.13     59.31
REMARK 500    SER A 860     -161.37   -109.49
REMARK 500    ALA A 861      -70.97    -98.95
REMARK 500    LYS A 864       38.08    -71.30
REMARK 500    THR A 865      104.33    120.93
REMARK 500    VAL A 866       80.93    -69.86
REMARK 500    VAL A 875      -92.57   -106.91
REMARK 500    VAL A 876      -54.86     17.37
REMARK 500    TYR C  12        8.29    -69.99
REMARK 500    LYS C  27       57.99    -69.97
REMARK 500    ILE C  28       77.81    -28.82
REMARK 500    VAL C  29       36.58    -96.25
REMARK 500    ASP C  31      -67.27     98.35
REMARK 500    ASN C  38       34.20    -76.13
REMARK 500    THR C  44       91.82    -69.08
REMARK 500    ARG C  45      102.28    -47.00
REMARK 500    ILE C  48     -103.65    -61.07
REMARK 500    LYS C  50      -49.38     -7.82
REMARK 500    GLU C  58      -30.61    -35.91
REMARK 500    SER C  60      -78.59   -108.49
REMARK 500    PRO C  66     -163.28   -125.02
REMARK 500    ALA C  69       63.41   -107.56
REMARK 500    ALA C  75       40.07    -84.56
REMARK 500    GLN C  76      -36.99   -156.91
REMARK 500    LEU C 104      -75.62     93.37
REMARK 500    GLU C 109      -36.13    -36.89
REMARK 500    ASP C 112      -75.92    -81.81
REMARK 500    ALA C 113     -117.32    126.41
REMARK 500    LYS C 114      146.53     87.54
REMARK 500    LYS C 115       16.94    -60.14
REMARK 500    THR C 119       78.71     62.33
REMARK 500    THR C 127     -111.11     -2.74
REMARK 500    ASP C 128      -33.26   -161.95
REMARK 500    TYR C 130       33.79    -74.09
REMARK 500    ALA C 137      -30.02   -142.68
REMARK 500    LEU C 144     -123.88    -86.94
REMARK 500    GLU C 145       65.96     20.05
REMARK 500    ALA C 161     -117.27    -87.15
REMARK 500    SER C 162       48.66   -157.92
REMARK 500    SER C 164      -57.59   -124.83
REMARK 500    ASN C 171      -46.98   -132.83
REMARK 500    VAL C 181       74.51     59.89
REMARK 500    ILE C 188     -107.27    -77.60
REMARK 500    ARG C 190     -162.35    170.95
REMARK 500    LEU C 191     -103.05     13.01
REMARK 500    LYS C 192       16.88   -169.28
REMARK 500    LEU C 193       38.30     28.30
REMARK 500    ASP C 195      -73.52   -139.99
REMARK 500    PHE C 196       86.29     44.67
REMARK 500    SER C 201     -151.51   -107.80
REMARK 500    ASP C 203      -43.11     79.53
REMARK 500    ASN C 209       46.02   -143.53
REMARK 500    PHE C 210      -86.63    -65.36
REMARK 500    ALA C 211      129.42     -9.04
REMARK 500    ASP C 214       16.34   -149.79
REMARK 500    ALA C 217     -146.99     50.51
REMARK 500    ALA C 218       61.80     37.93
REMARK 500    ARG C 223      -32.58   -135.56
REMARK 500    LYS C 225       32.73    -74.05
REMARK 500    ILE C 226      -40.65   -133.32
REMARK 500    THR C 229       29.20   -155.24
REMARK 500    LYS C 232      -68.22    -95.07
REMARK 500    LYS C 235      -25.35   -170.56
REMARK 500    LYS C 238      108.39     89.40
REMARK 500    ARG C 239      150.15     90.62
REMARK 500    VAL C 264       99.19    -42.18
REMARK 500    VAL C 272      115.19    -29.82
REMARK 500    THR C 274     -122.24    -96.59
REMARK 500    ASN C 275      -22.40    160.70
REMARK 500    GLU C 279      -66.96   -107.83
REMARK 500    ARG C 290      -77.82    -53.59
REMARK 500    SER C 298       51.66    -67.57
REMARK 500    LYS C 299      -47.62   -173.27
REMARK 500    ALA C 302       -8.59    -47.91
REMARK 500    GLN C 304      -15.04   -148.27
REMARK 500    LEU C 306      119.77     28.75
REMARK 500    MET C 320       23.83    -79.86
REMARK 500    ILE C 325      153.74    -49.19
REMARK 500    ARG C 331      -67.31    -16.24
REMARK 500    GLU C 337      -55.46   -157.06
REMARK 500    LYS C 338       14.05   -145.67
REMARK 500    GLU C 348      -94.28     54.55
REMARK 500    THR C 350      -78.23   -134.45
REMARK 500    ALA C 359      -67.61    -90.12
REMARK 500    ARG C 360        6.00    -55.00
REMARK 500    ASP C 362      147.31     45.56
REMARK 500    VAL C 363      -42.83   -135.84
REMARK 500    GLU C 364      100.53     11.80
REMARK 500    GLU C 365     -127.15    -59.50
REMARK 500    PHE C 366      -56.56   -132.90
REMARK 500    LYS C 367      -83.42     47.72
REMARK 500    MET C 390     -163.11     32.35
REMARK 500    ARG C 391       18.25    147.59
REMARK 500    THR B   6     -162.07   -123.74
REMARK 500    GLU B   9      -72.89    -64.36
REMARK 500    LYS B  21      -96.85   -150.50
REMARK 500    LEU B  23     -125.00     14.51
REMARK 500    ARG B  25       11.09   -151.93
REMARK 500    HIS B  27      -62.94    -91.08
REMARK 500    SER B  30      -41.03    173.07
REMARK 500    ARG B  36      -70.39   -108.62
REMARK 500    LEU B  39      -61.27     71.20
REMARK 500    ASP B  44       58.20   -115.02
REMARK 500    GLN B  46     -179.35     62.68
REMARK 500    ILE B  49      131.62    -35.46
REMARK 500    THR B  51       15.39     45.79
REMARK 500    ARG B  71       78.87     74.91
REMARK 500    SER B  73       70.15     38.09
REMARK 500    ASP B  74       -3.96   -176.88
REMARK 500    ARG B  75       92.29     52.14
REMARK 500    GLU B  84      -66.36   -102.47
REMARK 500    TYR B  92       65.14     39.05
REMARK 500    TRP B  97     -101.28    -52.92
REMARK 500    LEU B  98      128.41     73.37
REMARK 500    VAL B 103       70.33   -153.05
REMARK 500    GLU B 104       47.76    -80.44
REMARK 500    ASN B 105      -40.63    131.77
REMARK 500    GLU B 108     -155.52   -162.89
REMARK 500    ALA B 109      -85.70     46.03
REMARK 500    GLU B 110      121.99     60.17
REMARK 500    GLU B 112       75.72     89.07
REMARK 500    GLU B 113       88.80    -66.33
REMARK 500    LYS B 124        6.98     40.35
REMARK 500    GLN B 132       59.98   -115.78
REMARK 500    LEU B 135      -64.33    -28.39
REMARK 500    ASN B 155       47.65     28.45
REMARK 500    GLU B 158       88.48     93.42
REMARK 500    ILE B 161       95.25    -66.66
REMARK 500    LEU B 167      -88.31    -62.95
REMARK 500    ALA B 168      138.54   -170.09
REMARK 500    ASN B 170     -132.62     76.87
REMARK 500    ARG B 171      140.27     26.13
REMARK 500    ASN B 182      -35.00     94.26
REMARK 500    THR B 184      -81.52    -61.80
REMARK 500    SER B 192      -59.36   -120.31
REMARK 500    THR B 193     -173.97    177.33
REMARK 500    ALA B 194      -47.73   -161.59
REMARK 500    TYR B 196      -95.35   -132.15
REMARK 500    ARG B 197     -146.83   -113.06
REMARK 500    PHE B 210      108.45     65.44
REMARK 500    ALA B 216      -72.16     69.56
REMARK 500    PHE B 223      -56.39    -21.89
REMARK 500    MET B 227       37.50    -81.45
REMARK 500    ARG B 228      -45.44   -141.91
REMARK 500    LEU B 233      -78.57    -78.38
REMARK 500    GLU B 247      -23.53     57.84
REMARK 500    GLU B 257       22.80    -72.14
REMARK 500    SER B 261        5.36    -61.05
REMARK 500    VAL B 276     -129.68   -109.26
REMARK 500    LYS B 281      150.72    -40.90
REMARK 500    ILE B 292       39.00    -68.41
REMARK 500    ILE B 293      -42.62   -137.47
REMARK 500    PHE B 297       84.44    153.59
REMARK 500    PRO B 299       24.96    -62.89
REMARK 500    HIS B 300     -151.07    -57.96
REMARK 500    THR B 303       -8.20   -155.86
REMARK 500    ASP B 307       48.79    -73.51
REMARK 500    TYR B 317        3.86    -66.78
REMARK 500    SER B 320       44.17    -70.94
REMARK 500    LYS B 321      -30.79   -156.12
REMARK 500    LEU B 325      -22.99    174.45
REMARK 500    GLU B 331      130.06     66.28
REMARK 500    PRO B 332      134.59    -30.49
REMARK 500    LYS B 335       33.09    -94.68
REMARK 500    TYR B 338       34.01    -67.92
REMARK 500    ALA B 339       -4.44   -144.94
REMARK 500    ALA B 346      -66.60    -29.60
REMARK 500    ASP B 348        0.32    -65.37
REMARK 500    ARG B 355      -55.44    -26.79
REMARK 500    LYS B 371      -83.53    -92.41
REMARK 500    SER B 372      -75.09     18.25
REMARK 500    ARG B 377      120.54     82.80
REMARK 500    LYS B 378       37.31    168.76
REMARK 500    LEU B 379       51.75   -102.34
REMARK 500    LYS B 382       10.64    -55.36
REMARK 500    PRO B 387      108.04    -58.41
REMARK 500    HIS B 396       31.32    -84.45
REMARK 500    ALA B 397       16.33   -154.38
REMARK 500    ASN B 402     -128.35    -13.04
REMARK 500    TRP B 403     -106.91    147.96
REMARK 500    VAL B 404      -86.91     44.45
REMARK 500    THR B 417      105.02    -52.03
REMARK 500    ASN B 418      142.88     60.54
REMARK 500    LEU B 433     -137.42     60.32
REMARK 500    ALA B 434      -50.79   -125.36
REMARK 500    ARG B 435       88.27     64.50
REMARK 500    PRO B 438       61.50   -100.36
REMARK 500    PHE B 440      -54.27   -135.36
REMARK 500    GLU B 441       29.20    -70.91
REMARK 500    ALA B 442       17.28   -147.23
REMARK 500    LEU B 445      108.29    -44.15
REMARK 500    THR B 448     -136.98    -62.53
REMARK 500    GLN B 449      -20.14     57.91
REMARK 500    ARG B 452      -62.46   -130.23
REMARK 500    GLU B 457      101.09    -56.73
REMARK 500    ASN B 463        2.04    -68.01
REMARK 500    MET B 473     -137.93     14.14
REMARK 500    ALA B 474       58.62   -161.95
REMARK 500    GLN B 475      170.28     65.40
REMARK 500    GLU B 482      -81.98    -51.25
REMARK 500    ARG B 483      -68.28     -3.18
REMARK 500    GLU B 486        2.51    -60.57
REMARK 500    GLU B 499      -14.70    -48.43
REMARK 500    TYR B 530      117.37    164.18
REMARK 500    GLU B 548      -34.24   -135.87
REMARK 500    ASP B 551       31.63    -94.39
REMARK 500    VAL B 559     -100.97    -87.09
REMARK 500    THR B 560      162.78     67.86
REMARK 500    PHE B 562      -34.46   -132.91
REMARK 500    CYS B 570      -94.52   -118.60
REMARK 500    ASP B 571      145.05     25.59
REMARK 500    ARG B 574      105.97    169.77
REMARK 500    PRO B 587     -129.89    -88.26
REMARK 500    LEU B 588      105.68   -169.60
REMARK 500    VAL B 589      -70.15   -101.00
REMARK 500    GLU B 598      128.28     80.18
REMARK 500    ALA B 601       -9.33    -56.99
REMARK 500    ILE B 602     -167.39     60.19
REMARK 500    PHE B 604      -51.76    -19.45
REMARK 500    ASP B 605      -26.25    -34.64
REMARK 500    ALA B 618      -51.10    141.77
REMARK 500    PRO B 635     -149.78    -80.60
REMARK 500    PRO B 645        7.63    -60.12
REMARK 500    GLU B 659       51.00    -55.92
REMARK 500    HIS B 660       -5.58   -166.68
REMARK 500    SER B 663      -79.62     -4.57
REMARK 500    SER B 670        5.93    -62.11
REMARK 500    ALA B 681      133.68   -170.51
REMARK 500    ALA B 682       -7.97    -55.52
REMARK 500    TYR B 684       -4.38    -48.43
REMARK 500    ARG B 691       85.76     29.18
REMARK 500    PRO B 701       98.83    -69.77
REMARK 500    VAL B 703       95.10     67.26
REMARK 500    LEU B 708       15.82    -60.79
REMARK 500    ASP B 709      -55.75   -125.10
REMARK 500    ALA B 718       17.91   -148.50
REMARK 500    PHE B 729      140.13   -172.01
REMARK 500    THR B 730      -14.08     49.77
REMARK 500    GLU B 735       92.26     62.34
REMARK 500    ASP B 736       85.00     13.94
REMARK 500    SER B 752     -162.89   -119.92
REMARK 500    SER B 759      158.34    166.05
REMARK 500    VAL B 763      105.73    -55.41
REMARK 500    GLN B 769     -126.42     77.27
REMARK 500    GLU B 770      123.06     78.98
REMARK 500    ILE B 773       71.86   -113.25
REMARK 500    MET B 775      107.25    -34.74
REMARK 500    GLU B 777     -147.84   -138.99
REMARK 500    VAL B 780       -6.99   -143.13
REMARK 500    ARG B 781     -113.79   -150.70
REMARK 500    TYR B 783     -137.02   -122.30
REMARK 500    LYS B 784       97.53   -167.68
REMARK 500    ARG B 790      -70.20     15.38
REMARK 500    GLU B 793     -147.02    -83.76
REMARK 500    PRO B 800     -163.79      2.26
REMARK 500    GLU B 801       49.18    -13.51
REMARK 500    GLU B 803      107.81    -59.81
REMARK 500    VAL B 814      132.11   -178.35
REMARK 500    THR B 835      -39.63     59.85
REMARK 500    ALA B 856      -37.81    -34.08
REMARK 500    LYS B 860       67.52    -65.08
REMARK 500    LEU B 869      106.19    -51.21
REMARK 500    ILE B 888      103.97    -56.16
REMARK 500    VAL B 901      -30.14    -35.13
REMARK 500    PRO B 912      -17.88    -45.43
REMARK 500    LEU B 915      -80.60    -72.86
REMARK 500    MET B 919       65.91     28.35
REMARK 500    LEU B 921     -161.51    -65.05
REMARK 500    TYR B 932       81.25    -67.75
REMARK 500    ALA B 933      -43.36    179.61
REMARK 500    PRO B 944       34.13    -61.49
REMARK 500    PHE B 945       16.15    175.42
REMARK 500    TYR B 946      151.47     87.41
REMARK 500    GLU B 951      -27.84    -33.27
REMARK 500    ASP B 965       44.40   -100.87
REMARK 500    ALA B 966        3.68     47.43
REMARK 500    ASP B 972       79.45    -65.06
REMARK 500    THR B 975      -44.51   -136.70
REMARK 500    ARG B 982     -176.37     62.66
REMARK 500    HIS B 995       54.77    -98.90
REMARK 500    LEU B1001      145.07    157.73
REMARK 500    ALA B1003       46.44    -87.74
REMARK 500    ALA B1005      -67.75    -99.86
REMARK 500    ARG B1014       -5.04     69.82
REMARK 500    GLU B1023       79.38     62.18
REMARK 500    GLU B1030      -78.01      7.46
REMARK 500    ASP B1034      -32.12    -37.01
REMARK 500    ARG B1048      -20.62   -164.04
REMARK 500    LEU B1050      -35.56   -145.48
REMARK 500    SER B1053      -48.34   -146.44
REMARK 500    ASP B1054      -67.38   -131.90
REMARK 500    ARG B1055      -46.97     67.84
REMARK 500    THR B1056      121.11      0.35
REMARK 500    TYR B1066      -99.31   -108.01
REMARK 500    ASP B1071      143.48     29.68
REMARK 500    LYS B1072       48.66    -71.68
REMARK 500    LYS B1074       26.37     47.46
REMARK 500    TYR B1077       50.27     36.22
REMARK 500    PRO B1080        5.80    -52.06
REMARK 500    ASP B1084      -37.28     68.87
REMARK 500    SER B1086      -35.04     73.94
REMARK 500    ASN B1087      148.92     63.49
REMARK 500    ILE B1108       47.73     72.00
REMARK 500    VAL B1114     -139.26    -78.02
REMARK 500    GLU B1116     -155.91   -128.02
REMARK 500    ASP B1117      -93.41   -133.99
REMARK 500    LYS B1118        7.83    156.50
REMARK 500    HIS D   7      162.84    169.18
REMARK 500    LYS D   8      120.99    179.31
REMARK 500    ASP D   9     -134.35   -132.08
REMARK 500    THR D  11      -62.78   -132.93
REMARK 500    GLU D  23        4.91    -58.72
REMARK 500    SER D  32      -71.60    -57.00
REMARK 500    LEU D  34      -99.24   -104.16
REMARK 500    TYR D  35        0.24    -62.52
REMARK 500    ASP D  42      -70.25   -105.53
REMARK 500    TYR D  54      153.97    -45.61
REMARK 500    ASP D  55      -59.60    -28.73
REMARK 500    GLU D  70      -72.23    -24.32
REMARK 500    PRO D  79      -21.85    -37.67
REMARK 500    GLU D  87      151.96     77.53
REMARK 500    CYS D  89       56.98   -109.19
REMARK 500    THR D  94     -144.69    -80.53
REMARK 500    LYS D  95      120.63   -174.35
REMARK 500    PRO D 103      -74.63    -70.93
REMARK 500    ASN D 104       39.16   -149.41
REMARK 500    SER D 116      -25.66     76.90
REMARK 500    GLU D 117      -66.31     66.19
REMARK 500    ASP D 127        6.89   -163.48
REMARK 500    THR D 135      116.62     13.94
REMARK 500    ALA D 143     -152.56    -84.49
REMARK 500    GLU D 152      -89.03    -31.53
REMARK 500    ALA D 154      -22.37     62.87
REMARK 500    SER D 162       26.86   -167.36
REMARK 500    GLU D 177      -74.61    -51.85
REMARK 500    ALA D 179      -31.97    -34.38
REMARK 500    LYS D 191       58.48   -100.37
REMARK 500    ASP D 192       73.14     63.69
REMARK 500    LEU D 195       21.72    -77.81
REMARK 500    SER D 196      154.98    -49.34
REMARK 500    LEU D 201        0.32    -67.00
REMARK 500    LEU D 205      -80.71     27.35
REMARK 500    CYS D 206      -90.00     46.01
REMARK 500    GLU D 207       12.93     82.36
REMARK 500    GLU D 223      108.06    -52.60
REMARK 500    ASP D 224       32.50     70.96
REMARK 500    GLU D 257      -70.44    -32.31
REMARK 500    GLU E  17       32.82    -86.62
REMARK 500    PRO E  21      130.10    -32.82
REMARK 500    GLU E  29       -9.21    -59.65
REMARK 500    GLN E  32        7.28    -69.22
REMARK 500    ILE E  38     -153.39   -119.83
REMARK 500    LEU E  39      -74.18    166.64
REMARK 500    LYS E  40      -49.91    135.50
REMARK 500    LEU E  49     -103.08   -117.19
REMARK 500    LYS E  52       -2.59    -52.23
REMARK 500    PHE E  61      133.34    -34.81
REMARK 500    ALA E  65     -153.04    -62.32
REMARK 500    THR E  66      111.79   -161.82
REMARK 500    VAL E  81       98.12    -64.32
REMARK 500    GLN E  82       82.00     92.69
REMARK 500    GLU E  88      152.69    137.09
REMARK 500    GLN E 112       50.22    -95.57
REMARK 500    ILE E 113      -58.61   -120.99
REMARK 500    ASP E 115       96.41    -68.91
REMARK 500    ASP E 116     -123.40    173.95
REMARK 500    LEU E 118       68.69   -110.53
REMARK 500    ASN E 122      -92.28    -70.80
REMARK 500    GLU E 130       40.60   -142.64
REMARK 500    LYS E 131      -50.42   -163.80
REMARK 500    LYS E 133       72.99     54.09
REMARK 500    VAL E 135       76.64   -100.00
REMARK 500    VAL E 142     -160.41   -100.64
REMARK 500    ARG E 143       84.65   -167.24
REMARK 500    ALA E 144     -160.37   -117.97
REMARK 500    ILE E 147      -57.47   -122.93
REMARK 500    ARG E 165       34.44    -95.97
REMARK 500    PRO E 167      123.51    -39.10
REMARK 500    TYR E 168       53.12     72.33
REMARK 500    LYS E 179       76.37   -102.98
REMARK 500    SER F   2      -34.97   -133.22
REMARK 500    SER F   3     -106.75    -64.42
REMARK 500    VAL F   4      -30.96   -139.06
REMARK 500    VAL F   7      -75.60    -83.08
REMARK 500    SER F  30     -111.44   -151.32
REMARK 500    SER F  31     -131.42   -155.15
REMARK 500    LEU F  33       64.47   -104.21
REMARK 500    LEU F  34      -36.99   -163.75
REMARK 500    SER F  43      -18.07   -167.57
REMARK 500    GLU F  57      -76.92    -55.48
REMARK 500    SER F  60        8.04    -65.34
REMARK 500    SER F  64     -103.09    -98.67
REMARK 500    ALA F  73       34.53    -97.33
REMARK 500    SER F  74      -47.71   -156.16
REMARK 500    CYS F  76       79.40     52.76
REMARK 500    PRO F  77     -179.61    -67.15
REMARK 500    SER F  80       11.20    -69.32
REMARK 500    SER F  85      -19.21    -48.46
REMARK 500    CYS G  13     -166.48   -112.52
REMARK 500    ARG G  20      108.34    -45.90
REMARK 500    SER G  27      119.03   -160.12
REMARK 500    CYS G  33     -101.75   -109.83
REMARK 500    ASN G  34       51.04   -102.69
REMARK 500    ASN G  47      157.02     63.38
REMARK 500    ILE G  48     -117.95   -122.56
REMARK 500    PRO G  64      103.36    -52.59
REMARK 500    SER G  65      139.84    -34.37
REMARK 500    HIS G  68      -56.07     12.76
REMARK 500    VAL G  78      114.46   -163.68
REMARK 500    GLU G  80      -66.02   -160.58
REMARK 500    LEU G  81      -37.53   -141.44
REMARK 500    ASN G  87       66.24   -111.37
REMARK 500    ASN G  88       -4.46     47.09
REMARK 500    SER G  97      -83.63    -40.25
REMARK 500    TYR G  99       90.62     65.60
REMARK 500    LEU G 101      -19.80     63.93
REMARK 500    ASN G 108       47.13    -59.05
REMARK 500    ASP H  10      102.68     58.71
REMARK 500    ARG H  12       25.26    -51.93
REMARK 500    ILE H  13      -41.19   -131.08
REMARK 500    TYR H  15     -113.88     75.14
REMARK 500    VAL H  17      102.16    -36.19
REMARK 500    ILE H  25      -47.19     32.14
REMARK 500    ALA H  28      -99.69    -67.96
REMARK 500    TYR H  29        0.85    -56.24
REMARK 500    PRO H  43      -62.34     -8.43
REMARK 500    TRP H  44      112.52     97.51
REMARK 500    SER H  48       20.10    -73.51
REMARK 500    PRO H  50       -8.53    -53.12
REMARK 500    ASN H  56       97.70    -26.00
REMARK 500    PRO H  59       60.77    -58.73
REMARK 500    TYR H  72       11.60   -142.71
REMARK 500    GLU H  74      130.10    162.92
REMARK 500    ARG H  79     -127.82   -153.44
REMARK 500    TYR H  80      -37.12   -172.57
REMARK 500    VAL H  81      135.45     74.70
REMARK 500    LEU K  13       56.08     73.50
REMARK 500    PHE K  19      -70.22    -66.78
REMARK 500    ARG K  26      116.35    -14.73
REMARK 500    LEU K  27      124.77     94.41
REMARK 500    GLN K  42      -50.62    -16.25
REMARK 500    ALA K  47      111.41      1.72
REMARK 500    LEU K  50      124.10    -31.22
REMARK 500    ILE K  51       84.23     -0.74
REMARK 500    ASP K  52       65.24   -151.50
REMARK 500    SER K  58     -137.67   -141.13
REMARK 500    VAL K  61      160.92    -10.98
REMARK 500    ILE K  62      -24.90     87.06
REMARK 500    ARG K  71       35.21    -65.41
REMARK 500    PRO K  75       42.53    -80.04
REMARK 500    LEU L   6     -124.36    -85.93
REMARK 500    GLU L   9      106.87   -160.57
REMARK 500    SER L  10      -79.17     49.41
REMARK 500    ASP L  21     -151.82   -120.43
REMARK 500    ILE L  28      -73.10    -58.16
REMARK 500    ARG L  34       56.24    -96.01
REMARK 500    SER L  36       88.29    -10.60
REMARK 500    PRO L  46      -99.36    -33.66
REMARK 500    PRO L  48      -63.63     -9.62
REMARK 500    LEU L  49       76.29    -69.32
REMARK 500    SER L  50      108.61    166.13
REMARK 500    ASP L  60       60.56   -115.76
REMARK 500    SER L  62      -67.39    -12.07
REMARK 500    LEU L  90       48.00    -82.97
REMARK 500    THR L  91      -45.10   -136.87
REMARK 500    LEU N   2      170.84     67.71
REMARK 500    ARG N   6      135.72     71.17
REMARK 500    THR N   9      -72.51    -64.55
REMARK 500    ILE N  14      -70.73   -135.07
REMARK 500    GLN N  19       33.22    -69.15
REMARK 500    SER N  20      -14.82   -140.39
REMARK 500    PHE N  21      -72.40    -71.98
REMARK 500    THR N  23      -70.46    -54.45
REMARK 500    ALA N  27       52.70    -94.11
REMARK 500    GLU N  29      112.16     26.86
REMARK 500    LYS N  41      -88.78    -95.68
REMARK 500    ASP N  54       80.94     52.17
REMARK 500    HIS N  61       68.06    -69.73
REMARK 500    TYR N  62      -72.19   -153.25
REMARK 500    THR N  63      -91.09     90.85
REMARK 500    LYS P  11      -53.26     72.02
REMARK 500    PHE P  13       49.48    -63.23
REMARK 500    LEU P  18       13.43    -67.33
REMARK 500    VAL P  20       58.46    -91.86
REMARK 500    VAL P  24       34.18    -95.84
REMARK 500    ARG P  25     -129.10   -101.74
REMARK 500    CYS P  26     -144.01   -155.30
REMARK 500    TYR P  28      -68.10     58.20
REMARK 500    ILE P  34      116.68     13.19
REMARK 500    TRP Y  51      -37.33    -38.16
REMARK 500    LEU Y  55      -79.76   -127.53
REMARK 500    ASN Y  56     -136.01   -166.18
REMARK 500    ILE Y  59      -50.81     66.98
REMARK 500    LYS Y  66      -23.51    -37.28
REMARK 500    ASP Y  70      -45.60    -26.34
REMARK 500    LYS Y  73       23.82    -74.86
REMARK 500    TYR Y  75       45.11    -84.00
REMARK 500    LYS Y  77      143.19     77.22
REMARK 500    ASP Y  79     -153.55    -92.03
REMARK 500    SER Y  80     -148.21    -83.88
REMARK 500    ARG Y  81       57.84   -116.49
REMARK 500    LYS I   7       70.46   -160.70
REMARK 500    SER I  23      165.20    -49.79
REMARK 500    ILE I  27      101.27     45.82
REMARK 500    ARG I  48       30.73    -98.49
REMARK 500    LEU I  49       53.94   -108.47
REMARK 500    GLU I  53      147.23     67.07
REMARK 500    PRO I  54       89.02    -54.99
REMARK 500    GLN I  56      -39.25    -10.07
REMARK 500    CYS I  58      -93.73   -119.42
REMARK 500    PRO I  59       53.31    -90.84
REMARK 500    THR I  64     -108.92    -56.26
REMARK 500    GLU I  76       86.64     57.93
REMARK 500    PRO I  80       93.05    -34.67
REMARK 500    ALA I  96     -145.39   -103.48
REMARK 500    THR I  97      133.38     65.17
REMARK 500    ARG I  99      -11.96     80.92
REMARK 500    ARG I 100      -27.66   -141.03
REMARK 500    CYS I 101     -144.32   -105.44
REMARK 500    ARG I 103      -93.28     53.29
REMARK 500    LYS I 105     -150.30   -150.78
REMARK 500    ILE I 106     -127.52   -135.50
REMARK 500    TYR I 118       47.24    -77.45
REMARK 500    ILE I 121      -73.37    -51.61
REMARK 500    LYS I 142      -79.01   -106.25
REMARK 500    ALA I 143      -77.79     66.00
REMARK 500    VAL I 145       36.91   -171.53
REMARK 500    HIS I 148     -176.89     59.83
REMARK 500    ASN I 150     -139.88    -68.82
REMARK 500    GLU I 151     -150.84   -155.10
REMARK 500    LYS I 155      159.31    -37.83
REMARK 500    GLU I 185      -31.93    -33.03
REMARK 500    ILE I 194       -1.27    -57.70
REMARK 500    THR I 200       -4.26     64.95
REMARK 500    THR I 201      -32.32   -138.49
REMARK 500    MET I 207       -2.12    -40.19
REMARK 500    PRO I 216      168.77    -49.61
REMARK 500    THR I 218       -1.56    -54.89
REMARK 500    ARG I 220       43.39   -156.81
REMARK 500    LEU I 235       -2.34    -53.37
REMARK 500    HIS I 237      -75.50    -59.12
REMARK 500    ALA I 255     -110.78   -146.78
REMARK 500    GLN I 259       29.11    -76.01
REMARK 500    HIS I 272      -42.94   -135.33
REMARK 500    PHE I 277      -71.67    -93.16
REMARK 500    PRO I 285      113.29    -37.27
REMARK 500    SER I 287      120.26   -176.15
REMARK 500    LEU I 298      -53.20    -28.31
REMARK 500    LYS I 303      -77.16    -80.62
REMARK 500    SER I 322      134.97   -175.55
REMARK 500    ILE I 332      117.50    105.80
REMARK 500    PRO I 355     -178.45    -51.94
REMARK 500    TRP I 356      -80.76     61.13
REMARK 500    TRP I 372      -82.71    -48.02
REMARK 500    PRO I 373       91.28    -68.17
REMARK 500    ALA I 375       66.43   -156.49
REMARK 500    ASN I 376       83.24    -57.26
REMARK 500    TYR I 377      148.21    129.49
REMARK 500    VAL I 378       68.20   -158.59
REMARK 500    ARG I 384      105.50    -54.69
REMARK 500    ASP I 387      177.85    -58.65
REMARK 500    LEU I 388      -21.82   -149.55
REMARK 500    TYR I 390     -163.29   -112.87
REMARK 500    VAL I 391      101.32     70.63
REMARK 500    LYS I 392      -83.96    -53.02
REMARK 500    ASP I 393     -103.67     23.69
REMARK 500    ARG I 394      -75.36     69.13
REMARK 500    PRO I 403      115.41    -30.59
REMARK 500    HIS I 426      112.67    164.46
REMARK 500    LEU I 447      -28.32    -35.29
REMARK 500    ASN I 454       63.36     86.29
REMARK 500    ASP I 458        8.94    -69.56
REMARK 500    VAL I 482      -81.81    -58.19
REMARK 500    ARG I 490      -66.32    -92.83
REMARK 500    ALA I 499      -92.21    -99.27
REMARK 500    GLN I 500      -74.50   -137.10
REMARK 500    LEU I 508      -56.08     97.45
REMARK 500    THR I 514      -79.04    -57.89
REMARK 500    LEU I 515       89.25     59.05
REMARK 500    ILE I 524       83.73    -63.78
REMARK 500    LEU I 525       43.56   -159.44
REMARK 500    ALA I 528     -114.85    -63.03
REMARK 500    ASP I 529       20.07    -61.78
REMARK 500    VAL I 530      108.50    -47.89
REMARK 500    ILE I 532       -9.11     90.12
REMARK 500    ASP I 533      106.78    -40.50
REMARK 500    LEU I 534      126.92    -11.65
REMARK 500    PRO I 537      130.25    -26.99
REMARK 500    ALA I 541     -127.40    -58.38
REMARK 500    ARG I 543     -174.21     53.95
REMARK 500    LYS I 558       26.12    -79.58
REMARK 500    SER I 569       84.56    -69.48
REMARK 500    LYS I 576      -60.89     53.32
REMARK 500    SER I 584     -172.21    -67.98
REMARK 500    TYR I 585      108.15     46.38
REMARK 500    GLU I 595      144.49     55.51
REMARK 500    ASP I 599     -163.62   -172.77
REMARK 500    GLN I 606      106.34    -49.84
REMARK 500    GLN I 607      -91.74    -73.26
REMARK 500    PRO I 608     -100.27      9.95
REMARK 500    GLU I 609       40.74   -146.97
REMARK 500    SER I 610      153.80    -48.89
REMARK 500    LYS I 617      -71.68    -66.33
REMARK 500    GLU I 618       54.02    -93.28
REMARK 500    ASP I 621        7.86    -58.63
REMARK 500    TRP I 626      -72.12    -51.89
REMARK 500    PHE I 644      136.90     78.69
REMARK 500    THR I 645     -160.78   -178.71
REMARK 500    LEU I 653     -119.79    -98.25
REMARK 500    ASP I 655     -130.73     47.72
REMARK 500    ASN I 681       49.37    -98.43
REMARK 500    PRO I 686     -146.40    -86.72
REMARK 500    PRO I 688       96.39    -39.48
REMARK 500    LEU I 707       34.46    -90.39
REMARK 500    ARG I 708      -30.83   -132.06
REMARK 500    PRO I 721       11.68    -45.31
REMARK 500    ARG I 730      -17.07     72.08
REMARK 500    ALA I 733      -82.35    -18.15
REMARK 500    THR I 741      -80.39    -38.51
REMARK 500    MET I 746      134.99     42.24
REMARK 500    GLN I 749      118.70     55.84
REMARK 500    GLN I 750       73.19   -113.37
REMARK 500    ARG I 753       -0.15     56.20
REMARK 500    ILE I 757       81.81    -69.12
REMARK 500    LYS I 758     -169.14    -73.49
REMARK 500    ARG I 759      156.64    -48.28
REMARK 500    MET I 762       76.12     55.70
REMARK 500    THR I 763       87.45     45.03
REMARK 500    ARG I 764      -18.65   -177.59
REMARK 500    THR I 765      -53.06     64.96
REMARK 500    TYR I 772       74.52     56.78
REMARK 500    ARG I 779       14.15     49.75
REMARK 500    PHE I 781      103.87     67.91
REMARK 500    LEU I 806        5.38    -65.72
REMARK 500    VAL I 807      -45.25   -134.19
REMARK 500    ARG I 821      -35.37    -36.15
REMARK 500    ASN I 825     -100.52    -64.75
REMARK 500    ALA I 826      -69.11     -3.04
REMARK 500    SER I 828      -55.37   -144.87
REMARK 500    ASP I 829       15.26    -54.44
REMARK 500    SER I 840     -113.52   -148.22
REMARK 500    LEU I 841     -141.15    -68.75
REMARK 500    TYR I 842      -34.96      5.27
REMARK 500    ASP I 852      -19.55     60.15
REMARK 500    ASP I 853      -60.59    -96.59
REMARK 500    SER I 860     -162.36   -109.73
REMARK 500    ALA I 861      -73.98    -97.96
REMARK 500    LYS I 864       35.00    -67.04
REMARK 500    THR I 865      109.22    122.62
REMARK 500    ASP I 867      -48.16    -29.24
REMARK 500    VAL I 875      -89.73   -108.57
REMARK 500    VAL I 876      -56.17     15.81
REMARK 500    TYR M  12       21.53    -68.24
REMARK 500    LEU M  13       26.03   -151.58
REMARK 500    LEU M  24      -73.89    -34.08
REMARK 500    ILE M  28       75.46    -35.40
REMARK 500    VAL M  29       40.70   -100.13
REMARK 500    ASP M  31      -62.58     99.10
REMARK 500    ASN M  38       -7.83    -58.69
REMARK 500    THR M  44       98.85    -29.92
REMARK 500    ARG M  45       38.47    -78.43
REMARK 500    ILE M  48     -114.43    -78.29
REMARK 500    LYS M  50      -44.48    -26.63
REMARK 500    LEU M  54      -15.61    -37.20
REMARK 500    GLU M  58      -30.17    -39.47
REMARK 500    PRO M  66     -151.09   -126.21
REMARK 500    ALA M  74      -78.52    -63.12
REMARK 500    THR M  83        5.69    -68.93
REMARK 500    LEU M 104      -57.80    113.47
REMARK 500    ASP M 112      -96.55   -103.76
REMARK 500    ALA M 113      -91.61    135.79
REMARK 500    LYS M 114      118.86     64.24
REMARK 500    LYS M 115       40.65    -36.53
REMARK 500    VAL M 116       95.33   -171.36
REMARK 500    THR M 119       43.06     79.26
REMARK 500    THR M 127      -90.43     -2.16
REMARK 500    ASP M 128      -71.08   -173.10
REMARK 500    ALA M 137      -53.56   -140.77
REMARK 500    LEU M 144     -130.86    -81.92
REMARK 500    GLU M 145       37.42     39.99
REMARK 500    TYR M 146       72.20    -46.44
REMARK 500    ALA M 161       52.55    -66.99
REMARK 500    ASP M 170     -178.97    -68.55
REMARK 500    VAL M 179      109.50   -162.45
REMARK 500    VAL M 181       78.03     48.78
REMARK 500    LYS M 186       56.10   -149.72
REMARK 500    ILE M 188      -58.71   -127.79
REMARK 500    ARG M 190      141.29     72.95
REMARK 500    LEU M 191     -109.70     39.69
REMARK 500    LYS M 192      -43.06   -150.29
REMARK 500    LEU M 193      -24.37     59.78
REMARK 500    ASP M 195      -97.55    -84.50
REMARK 500    PHE M 196       39.68     80.98
REMARK 500    SER M 201     -139.69    -91.26
REMARK 500    ASP M 203      -35.50     85.59
REMARK 500    THR M 205       64.19   -162.31
REMARK 500    PHE M 210     -131.92    -81.90
REMARK 500    ALA M 211       88.26     23.54
REMARK 500    ASN M 212     -136.31    -71.58
REMARK 500    ILE M 213      -26.07     54.49
REMARK 500    ALA M 217     -140.20     43.89
REMARK 500    ALA M 218       80.66     36.46
REMARK 500    LYS M 232      -62.80   -121.30
REMARK 500    LYS M 235      -49.38   -174.44
REMARK 500    LYS M 238      145.28     69.63
REMARK 500    ARG M 239      118.22     73.94
REMARK 500    ASP M 247       50.03     22.64
REMARK 500    GLU M 248       80.64   -156.51
REMARK 500    VAL M 261       14.00    -68.12
REMARK 500    THR M 274     -162.63   -125.07
REMARK 500    ASN M 275       12.99   -158.60
REMARK 500    ILE M 277     -169.64    -71.25
REMARK 500    ARG M 278      -32.40     53.91
REMARK 500    GLU M 279      -96.30    -76.24
REMARK 500    ILE M 280      -43.11    -23.06
REMARK 500    GLU M 281      -85.33    -57.11
REMARK 500    GLU M 282        0.26    -64.80
REMARK 500    ILE M 297      -60.14   -128.63
REMARK 500    SER M 298      -46.54    -28.13
REMARK 500    GLN M 304      -35.26   -179.71
REMARK 500    LEU M 306      130.50     -6.09
REMARK 500    THR M 323      -15.49     64.55
REMARK 500    GLU M 337      -68.05   -171.83
REMARK 500    LYS M 338       28.54   -154.97
REMARK 500    GLU M 348     -104.14     67.72
REMARK 500    THR M 350      -61.41   -138.77
REMARK 500    VAL M 351      -47.32    -23.86
REMARK 500    LYS M 352      -73.50    -75.43
REMARK 500    HIS M 353      -63.06    -26.47
REMARK 500    ASP M 362     -179.43     61.44
REMARK 500    VAL M 363      -69.19   -147.65
REMARK 500    GLU M 364       87.54     55.28
REMARK 500    GLU M 365     -115.28    -60.42
REMARK 500    PHE M 366      -64.83   -140.95
REMARK 500    LYS M 367      -89.44     51.55
REMARK 500    LYS M 380       35.77    -83.11
REMARK 500    MET M 390     -159.16     62.88
REMARK 500    ARG M 391       21.20    156.11
REMARK 500    THR J   6     -161.81   -123.43
REMARK 500    GLU J   9      -73.95    -63.29
REMARK 500    LYS J  21      -94.84   -152.09
REMARK 500    LEU J  23     -123.01     12.57
REMARK 500    ARG J  25        9.73   -159.88
REMARK 500    SER J  30      -48.75    174.74
REMARK 500    ARG J  36      -73.58   -109.11
REMARK 500    LEU J  39      -60.47     71.29
REMARK 500    ASP J  44       55.46   -112.89
REMARK 500    GLN J  46     -177.43     62.78
REMARK 500    ILE J  49      134.14    -36.34
REMARK 500    THR J  51       15.86     44.03
REMARK 500    ARG J  71       81.05     71.32
REMARK 500    SER J  73       70.68     38.75
REMARK 500    ASP J  74       -2.90   -175.27
REMARK 500    ARG J  75       90.76     51.41
REMARK 500    GLU J  84      -62.61   -102.78
REMARK 500    TYR J  92       67.05     38.81
REMARK 500    TRP J  97     -103.60    -49.19
REMARK 500    LEU J  98      123.92     72.19
REMARK 500    VAL J 103       72.93   -152.71
REMARK 500    GLU J 104       45.90    -79.13
REMARK 500    ASN J 105      -39.41    131.62
REMARK 500    GLU J 108     -155.53   -160.80
REMARK 500    ALA J 109      -85.63     46.65
REMARK 500    GLU J 110      120.91     60.92
REMARK 500    GLU J 112       72.15     92.50
REMARK 500    GLU J 113       89.80    -62.04
REMARK 500    LYS J 124       13.18     39.49
REMARK 500    GLN J 132       54.72   -116.31
REMARK 500    ASN J 155       49.30     34.85
REMARK 500    GLU J 158       87.24     89.63
REMARK 500    ILE J 161       97.78    -68.16
REMARK 500    LEU J 167      -87.39    -62.32
REMARK 500    ASN J 170     -134.02     75.17
REMARK 500    ARG J 171      142.85     27.81
REMARK 500    THR J 176      111.26   -161.22
REMARK 500    THR J 179      151.23    -40.84
REMARK 500    ASN J 182      -36.37     93.76
REMARK 500    THR J 184      -81.96    -61.83
REMARK 500    THR J 193     -172.65    177.71
REMARK 500    ALA J 194      -50.26   -161.98
REMARK 500    TYR J 196      -94.37   -133.94
REMARK 500    ARG J 197     -146.38   -113.79
REMARK 500    PHE J 210      107.56     67.52
REMARK 500    ALA J 216      -72.44     70.78
REMARK 500    PHE J 223      -57.11    -24.43
REMARK 500    MET J 227       40.96    -82.11
REMARK 500    ARG J 228      -44.62   -146.66
REMARK 500    LEU J 233      -75.49    -79.38
REMARK 500    GLU J 247      -24.78     57.00
REMARK 500    GLU J 257       23.59    -72.33
REMARK 500    SER J 261        4.80    -60.90
REMARK 500    VAL J 276     -129.95   -109.04
REMARK 500    LYS J 288       30.18    -86.16
REMARK 500    ILE J 292       36.97    -65.79
REMARK 500    ILE J 293      -43.63   -136.79
REMARK 500    PHE J 297       85.35    153.93
REMARK 500    PRO J 299       25.68    -63.24
REMARK 500    HIS J 300     -150.69    -60.82
REMARK 500    THR J 303       -7.32   -156.95
REMARK 500    ASP J 307       48.33    -74.42
REMARK 500    TYR J 317        5.43    -69.74
REMARK 500    SER J 320       46.48    -70.58
REMARK 500    LYS J 321      -34.51   -156.77
REMARK 500    LEU J 325      -27.52    163.89
REMARK 500    LEU J 327       67.66   -119.98
REMARK 500    GLU J 331      126.69     66.16
REMARK 500    PRO J 332      137.74    -26.83
REMARK 500    LYS J 335       33.92    -94.74
REMARK 500    TYR J 338       37.63    -68.78
REMARK 500    ALA J 339       -1.73   -148.87
REMARK 500    ALA J 346      -62.94    -29.45
REMARK 500    ASP J 348        0.46    -64.53
REMARK 500    ARG J 355      -56.03    -28.42
REMARK 500    LYS J 371      -82.21    -89.50
REMARK 500    SER J 372      -73.99     18.12
REMARK 500    ARG J 377      123.05     80.06
REMARK 500    LYS J 378       33.33    168.08
REMARK 500    LEU J 379       52.50    -97.99
REMARK 500    LYS J 382       11.15    -58.49
REMARK 500    PRO J 387      105.42    -56.73
REMARK 500    HIS J 396       34.55    -85.92
REMARK 500    ALA J 397       10.61   -153.17
REMARK 500    ASN J 402     -131.87    -14.09
REMARK 500    TRP J 403     -105.41    150.94
REMARK 500    VAL J 404      -82.95     42.69
REMARK 500    THR J 417      108.04    -54.55
REMARK 500    ASN J 418      143.46     57.10
REMARK 500    LEU J 433     -138.15     59.38
REMARK 500    ARG J 435       87.54     64.13
REMARK 500    PHE J 440      -52.29   -131.80
REMARK 500    GLU J 441       32.70    -73.75
REMARK 500    ALA J 442       15.52   -148.72
REMARK 500    THR J 448     -137.11    -64.95
REMARK 500    GLN J 449      -20.76     58.95
REMARK 500    ARG J 452      -62.76   -132.64
REMARK 500    GLU J 457       95.16    -49.97
REMARK 500    ASN J 463        6.10    -68.48
REMARK 500    MET J 473     -136.64     13.56
REMARK 500    ALA J 474       57.24   -163.33
REMARK 500    GLN J 475      171.40     66.23
REMARK 500    GLU J 482      -81.03    -50.72
REMARK 500    ARG J 483      -65.34     -6.71
REMARK 500    GLU J 486        0.65    -56.63
REMARK 500    GLU J 499      -15.63    -49.20
REMARK 500    TYR J 530      116.66    162.77
REMARK 500    LYS J 546       13.20    -67.79
REMARK 500    GLU J 548      -31.31   -134.14
REMARK 500    ASP J 551       33.65    -92.57
REMARK 500    GLU J 552       19.25   -140.53
REMARK 500    VAL J 559     -101.87    -87.39
REMARK 500    THR J 560      163.54     69.08
REMARK 500    PHE J 562      -36.07   -131.05
REMARK 500    CYS J 570      -94.20   -119.49
REMARK 500    ASP J 571      145.81     23.48
REMARK 500    ARG J 574      104.16    167.25
REMARK 500    PRO J 587     -128.84    -90.85
REMARK 500    LEU J 588      106.87   -169.50
REMARK 500    VAL J 589      -71.53   -101.39
REMARK 500    THR J 590      -48.02    -29.22
REMARK 500    GLU J 598      127.61     77.87
REMARK 500    ALA J 601       -9.35    -56.80
REMARK 500    ILE J 602     -167.93     61.01
REMARK 500    PHE J 604      -50.26    -19.47
REMARK 500    ASP J 605      -26.04    -35.48
REMARK 500    ALA J 618      -54.75    141.23
REMARK 500    ASP J 632       32.19    -99.16
REMARK 500    PRO J 635     -149.72    -79.47
REMARK 500    LEU J 640     -162.36   -103.23
REMARK 500    PRO J 645        5.62    -58.27
REMARK 500    GLU J 659       51.10    -57.58
REMARK 500    HIS J 660       -5.76   -169.15
REMARK 500    SER J 663      -81.42     -1.63
REMARK 500    SER J 670        6.35    -65.24
REMARK 500    ALA J 682       -7.61    -52.07
REMARK 500    TYR J 684       -7.89    -44.88
REMARK 500    ARG J 691       82.36     33.25
REMARK 500    PRO J 701       97.53    -69.72
REMARK 500    VAL J 703       96.41     67.99
REMARK 500    LEU J 708       21.54    -63.94
REMARK 500    ASP J 709      -61.69   -128.44
REMARK 500    ALA J 718       23.95   -146.90
REMARK 500    PHE J 729      136.85   -174.27
REMARK 500    THR J 730      -14.19     50.91
REMARK 500    GLU J 735       89.94     61.05
REMARK 500    ASP J 736       81.91     18.22
REMARK 500    SER J 752     -162.77   -116.57
REMARK 500    SER J 759      160.72    163.68
REMARK 500    VAL J 763      104.72    -56.57
REMARK 500    GLN J 769     -126.95     78.88
REMARK 500    GLU J 770      124.89     79.25
REMARK 500    ILE J 773       74.07   -114.77
REMARK 500    MET J 775      107.93    -34.87
REMARK 500    GLU J 777     -148.89   -139.12
REMARK 500    VAL J 780       -4.92   -144.12
REMARK 500    ARG J 781     -117.14   -152.37
REMARK 500    TYR J 783     -136.75   -122.78
REMARK 500    LYS J 784       99.43   -168.19
REMARK 500    ARG J 790      -66.19     13.18
REMARK 500    GLU J 793     -148.73    -79.51
REMARK 500    PRO J 800     -154.36     -1.88
REMARK 500    GLU J 801       47.39    -20.22
REMARK 500    GLU J 803      108.94    -57.55
REMARK 500    LYS J 813     -169.82   -118.90
REMARK 500    VAL J 814      137.51   -174.19
REMARK 500    THR J 835      -40.88     61.35
REMARK 500    LYS J 860       71.61    -69.39
REMARK 500    LEU J 869      106.37    -52.45
REMARK 500    PRO J 872      102.81    -57.76
REMARK 500    ILE J 888      100.91    -50.75
REMARK 500    VAL J 901      -29.84    -35.91
REMARK 500    PRO J 912      -17.30    -45.55
REMARK 500    LEU J 915      -82.00    -75.36
REMARK 500    MET J 919       58.09     29.51
REMARK 500    LEU J 921     -160.72    -67.65
REMARK 500    TYR J 932       80.31    -67.42
REMARK 500    ALA J 933      -47.35   -177.52
REMARK 500    PRO J 944       35.53    -62.64
REMARK 500    PHE J 945       14.18    172.99
REMARK 500    TYR J 946      153.74     87.69
REMARK 500    GLU J 951      -28.29    -33.92
REMARK 500    ASP J 965       42.19    -98.84
REMARK 500    ALA J 966        3.26     47.15
REMARK 500    ASP J 972       75.74    -57.31
REMARK 500    THR J 975      -44.38   -137.11
REMARK 500    ARG J 982     -172.80     57.60
REMARK 500    HIS J 995       53.39   -103.62
REMARK 500    LEU J1001      149.07    155.88
REMARK 500    ALA J1003       48.60    -84.89
REMARK 500    ALA J1005      -66.53    -98.49
REMARK 500    ARG J1014       -4.05     68.83
REMARK 500    PRO J1016      149.10    -39.56
REMARK 500    GLU J1023       78.18     61.73
REMARK 500    GLU J1030      -71.36      7.64
REMARK 500    ASP J1034      -38.39    -34.20
REMARK 500    ARG J1048      -21.06   -161.78
REMARK 500    LEU J1050      -34.74   -145.65
REMARK 500    SER J1053      -50.45   -147.15
REMARK 500    ASP J1054      -70.03   -133.06
REMARK 500    ARG J1055      -49.05     69.93
REMARK 500    THR J1056      122.69      3.43
REMARK 500    TYR J1066      -97.71   -105.64
REMARK 500    ASP J1071      142.64     27.99
REMARK 500    LYS J1072       49.09    -71.25
REMARK 500    LYS J1074       27.01     48.48
REMARK 500    TYR J1077       48.67     37.39
REMARK 500    PRO J1080        4.06    -50.71
REMARK 500    ASP J1084      -37.73     68.74
REMARK 500    SER J1086      -34.28     72.00
REMARK 500    ASN J1087      152.10     64.69
REMARK 500    ILE J1108       47.80     72.94
REMARK 500    VAL J1114     -142.27    -77.20
REMARK 500    GLU J1116     -158.26   -127.74
REMARK 500    ASP J1117      -97.33   -131.38
REMARK 500    LYS J1118        7.95    162.32
REMARK 500    HIS O   7      157.99    166.50
REMARK 500    LYS O   8      121.92   -175.75
REMARK 500    ASP O   9     -135.39   -131.96
REMARK 500    THR O  11      -63.58   -135.23
REMARK 500    GLU O  23        2.08    -61.14
REMARK 500    SER O  32      -74.12    -59.79
REMARK 500    LEU O  34     -103.03   -100.70
REMARK 500    TYR O  35       -3.78    -59.94
REMARK 500    ASP O  42      -69.27   -104.81
REMARK 500    TYR O  54      154.02    -46.59
REMARK 500    ASP O  55      -59.50    -26.40
REMARK 500    GLU O  70      -70.71    -25.49
REMARK 500    PRO O  79      -24.56    -39.19
REMARK 500    GLU O  87      151.56     78.66
REMARK 500    CYS O  89       56.58   -109.02
REMARK 500    THR O  94     -146.61    -80.95
REMARK 500    LYS O  95      119.72   -174.80
REMARK 500    PRO O 103      -73.62    -70.09
REMARK 500    ASN O 104       38.24   -148.60
REMARK 500    SER O 116      -24.81     78.67
REMARK 500    GLU O 117      -68.24     66.81
REMARK 500    PRO O 119        0.61    -65.92
REMARK 500    SER O 125       99.85   -163.90
REMARK 500    ASP O 127        5.59   -161.23
REMARK 500    THR O 135      115.27     16.37
REMARK 500    ALA O 143     -150.37    -80.71
REMARK 500    GLU O 152      -84.89    -35.49
REMARK 500    ALA O 154      -25.14     64.39
REMARK 500    SER O 162       29.55   -172.85
REMARK 500    GLU O 177      -74.95    -54.34
REMARK 500    ALA O 179      -32.81    -33.35
REMARK 500    LYS O 191       57.86    -96.44
REMARK 500    ASP O 192       71.19     65.00
REMARK 500    LEU O 195       21.97    -78.31
REMARK 500    LEU O 205      -81.82     27.19
REMARK 500    CYS O 206      -91.77     47.84
REMARK 500    GLU O 207       12.33     84.69
REMARK 500    GLU O 223      108.58    -55.46
REMARK 500    LEU O 256      -70.79    -56.48
REMARK 500    GLU O 257      -69.79    -29.34
REMARK 500    ASN Q  16      -45.20    -25.15
REMARK 500    GLU Q  17       57.42   -113.39
REMARK 500    ARG Q  31      -71.00    -77.67
REMARK 500    GLN Q  32       13.48    -53.88
REMARK 500    ILE Q  38     -108.48   -107.27
REMARK 500    LEU Q  39      -81.41    127.97
REMARK 500    LYS Q  40      -66.08    156.03
REMARK 500    ASP Q  41      -72.31    -56.40
REMARK 500    LEU Q  49      -85.56    -92.22
REMARK 500    GLU Q  56      100.47    -37.40
REMARK 500    ALA Q  65     -135.35    -86.80
REMARK 500    THR Q  66      138.76   -175.66
REMARK 500    VAL Q  81        9.30    -60.01
REMARK 500    GLN Q  82       89.06   -160.15
REMARK 500    GLN Q 112       72.62   -105.86
REMARK 500    ILE Q 113      -54.19   -136.04
REMARK 500    ASP Q 116      -99.67   -164.15
REMARK 500    ASN Q 122      -77.61    -82.15
REMARK 500    GLU Q 130      -45.29   -135.15
REMARK 500    LYS Q 133       71.14     43.69
REMARK 500    ILE Q 147      -36.78   -133.75
REMARK 500    ALA Q 150       77.89   -160.25
REMARK 500    PRO Q 167      131.11    -34.10
REMARK 500    LYS Q 179       69.98   -103.02
REMARK 500    SER R   2     -151.15    -87.13
REMARK 500    SER R   3     -120.33     66.89
REMARK 500    VAL R   4      -71.18   -145.10
REMARK 500    VAL R   7     -103.75    -69.97
REMARK 500    ILE R  25       31.27    -77.08
REMARK 500    SER R  30     -101.11   -142.12
REMARK 500    ASN R  32      -79.01     -7.09
REMARK 500    ASN R  42       64.75    -67.86
REMARK 500    SER R  43      -47.22   -165.63
REMARK 500    ASP R  48     -125.15   -143.23
REMARK 500    ALA R  49     -101.21    -75.04
REMARK 500    GLU R  50       48.37    -81.18
REMARK 500    SER R  51      -57.43   -127.70
REMARK 500    SER R  60       11.85    -64.73
REMARK 500    SER R  64     -121.86    -73.68
REMARK 500    ASP R  67      -71.74    -69.21
REMARK 500    ALA R  73       21.15    -77.88
REMARK 500    SER R  74      -57.10   -147.54
REMARK 500    CYS R  76       63.32     36.77
REMARK 500    PRO R  77      170.76    -55.73
REMARK 500    THR R  78      -72.75   -111.61
REMARK 500    SER R  80       18.79    -69.06
REMARK 500    SER S  22       34.53    -72.64
REMARK 500    ASN S  25       75.46     50.78
REMARK 500    CYS S  33     -115.88   -121.24
REMARK 500    ASN S  34       63.67   -107.50
REMARK 500    ILE S  46        0.37    -68.24
REMARK 500    ASN S  47      127.00     65.82
REMARK 500    ILE S  48     -138.64   -107.20
REMARK 500    PRO S  64       86.58    -59.75
REMARK 500    SER S  65      144.55    -25.48
REMARK 500    GLU S  80      -97.26   -172.31
REMARK 500    ASN S  87       69.17   -105.54
REMARK 500    ASN S  88       -1.74     48.15
REMARK 500    SER S  97      -79.32    -32.26
REMARK 500    TYR S  99       96.46     61.05
REMARK 500    LEU S 101      -38.69     63.65
REMARK 500    LEU S 102       17.36    -65.66
REMARK 500    VAL S 103       40.28    -96.29
REMARK 500    ILE S 105       68.30    -63.39
REMARK 500    ASN S 108       47.44    -56.88
REMARK 500    ASP T  10       89.42     74.73
REMARK 500    ARG T  12       21.21    -68.30
REMARK 500    TYR T  15      -83.22    102.24
REMARK 500    VAL T  17      106.77    -53.10
REMARK 500    LYS T  19       97.71    -51.74
REMARK 500    HIS T  20     -157.50    -68.04
REMARK 500    GLU T  21      114.72    161.35
REMARK 500    ALA T  28      -88.21    -59.40
REMARK 500    TYR T  29       34.75    -60.85
REMARK 500    PRO T  43      -27.93     -8.79
REMARK 500    TRP T  44      152.81     67.21
REMARK 500    SER T  54     -111.51    -80.10
REMARK 500    ASN T  56       66.54    -67.55
REMARK 500    PRO T  59      107.51    -57.32
REMARK 500    TYR T  72      -59.96   -132.61
REMARK 500    ARG T  79     -136.92   -138.88
REMARK 500    TYR T  80      -51.02   -162.51
REMARK 500    VAL T  81      128.90     74.38
REMARK 500    ASP U  12     -159.82    -73.53
REMARK 500    LEU U  13       67.86     19.16
REMARK 500    HIS U  14     -106.86    -69.16
REMARK 500    PHE U  15      -66.65     -2.39
REMARK 500    ASN U  16      -77.38    -43.27
REMARK 500    PHE U  19      -77.46    -57.18
REMARK 500    ILE U  20      -68.97     -7.91
REMARK 500    TRP U  23       49.43   -106.91
REMARK 500    ASN U  25       80.53    -56.92
REMARK 500    ARG U  26       98.02     34.83
REMARK 500    LEU U  27      113.08     73.48
REMARK 500    ARG U  34      -20.30    -31.65
REMARK 500    ALA U  38      -72.08    -77.59
REMARK 500    ARG U  39      -12.03    -49.32
REMARK 500    LEU U  41      -72.41    -64.86
REMARK 500    GLN U  42      -41.76    -22.11
REMARK 500    ALA U  44        3.59    -57.43
REMARK 500    ALA U  47      119.26     41.62
REMARK 500    LEU U  50      134.03    -34.52
REMARK 500    ILE U  51       89.14     -7.20
REMARK 500    ASP U  52       78.70   -165.09
REMARK 500    SER U  57      -71.66   -119.35
REMARK 500    SER U  58     -111.92    -96.47
REMARK 500    THR U  59      117.34    160.39
REMARK 500    VAL U  61      175.89     15.79
REMARK 500    ILE U  62      -45.58     61.03
REMARK 500    ILE U  64       33.72    -88.72
REMARK 500    ARG U  70      -72.76    -48.93
REMARK 500    ARG U  71      -21.94    -39.84
REMARK 500    PRO U  75       42.25    -84.89
REMARK 500    SER U  91      -78.24    -70.62
REMARK 500    ARG V   4      120.38   -173.19
REMARK 500    LEU V   6      -75.43    -89.49
REMARK 500    SER V  10      -65.34     60.60
REMARK 500    TYR V  12      138.50    179.55
REMARK 500    ASP V  21     -133.08   -139.95
REMARK 500    ILE V  28      -83.53    -56.43
REMARK 500    LEU V  32       36.09    -89.70
REMARK 500    SER V  36        8.78     58.56
REMARK 500    PHE V  40      133.55   -170.74
REMARK 500    TYR V  44     -165.15   -172.00
REMARK 500    PRO V  46      -60.87    -27.85
REMARK 500    HIS V  47      132.87    177.30
REMARK 500    PRO V  48      -34.46    -34.40
REMARK 500    LEU V  49       44.25    -75.97
REMARK 500    ASP V  51       31.29    -84.79
REMARK 500    ASP V  60       49.11   -100.36
REMARK 500    LYS V  66      -29.46    -35.22
REMARK 500    LEU V  70      -36.09    -37.03
REMARK 500    LEU V  90       60.27   -105.76
REMARK 500    THR V  91      -47.98   -152.16
REMARK 500    LEU W   2      168.99     68.65
REMARK 500    ARG W   6      134.09     68.38
REMARK 500    THR W   9      -72.74    -62.09
REMARK 500    ILE W  14      -71.18   -132.28
REMARK 500    GLN W  19       31.60    -69.02
REMARK 500    PHE W  21      -72.48    -71.34
REMARK 500    ALA W  27       54.72    -91.93
REMARK 500    GLU W  29      111.58     28.07
REMARK 500    LYS W  41      -88.40    -99.36
REMARK 500    ASP W  54       79.51     53.40
REMARK 500    HIS W  61       66.37    -68.52
REMARK 500    TYR W  62      -70.70   -152.71
REMARK 500    THR W  63      -93.08     88.58
REMARK 500    LYS X  11      -52.77     68.65
REMARK 500    PHE X  13       50.52    -63.24
REMARK 500    LEU X  18       15.19    -67.63
REMARK 500    LYS X  19       48.38    -89.14
REMARK 500    VAL X  24       32.74    -93.06
REMARK 500    ARG X  25     -126.52    -99.88
REMARK 500    CYS X  26     -146.77   -157.49
REMARK 500    TYR X  28      -71.65     57.99
REMARK 500    CYS X  29      122.99    -38.86
REMARK 500    ILE X  34      117.60     14.49
REMARK 500    GLN Z  39       25.10     83.25
REMARK 500    LEU Z  55     -146.17   -142.45
REMARK 500    ASN Z  56     -163.83   -126.19
REMARK 500    ILE Z  59      -30.29    100.13
REMARK 500    ASN Z  71       -8.86    -58.34
REMARK 500    LYS Z  77      135.11    122.43
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 PHE B  945     TYR B  946                  142.44
REMARK 500 PHE G   40     ASP G   41                  148.78
REMARK 500 ARG K   26     LEU K   27                  149.49
REMARK 500 LYS M   27     ILE M   28                 -148.67
REMARK 500 PHE J  945     TYR J  946                  141.65
REMARK 500 THR U   59     ASP U   60                 -149.53
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 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: (11X,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     ARG A 103        24.3      L          L   OUTSIDE RANGE
REMARK 500     VAL A 104        24.8      L          L   OUTSIDE RANGE
REMARK 500     TRP A 372        24.9      L          L   OUTSIDE RANGE
REMARK 500     CYS A 575        24.4      L          L   OUTSIDE RANGE
REMARK 500     ARG A 759        23.4      L          L   OUTSIDE RANGE
REMARK 500     ASP C 214        24.8      L          L   OUTSIDE RANGE
REMARK 500     ASP B 571        22.4      L          L   OUTSIDE RANGE
REMARK 500     VAL B 589        24.9      L          L   OUTSIDE RANGE
REMARK 500     TYR B 946        24.4      L          L   OUTSIDE RANGE
REMARK 500     HIS B1002        23.8      L          L   OUTSIDE RANGE
REMARK 500     THR G  79        24.6      L          L   OUTSIDE RANGE
REMARK 500     ILE H  25        25.0      L          L   OUTSIDE RANGE
REMARK 500     ILE H  82        24.4      L          L   OUTSIDE RANGE
REMARK 500     THR N  63        22.1      L          L   OUTSIDE RANGE
REMARK 500     ARG I 103        24.0      L          L   OUTSIDE RANGE
REMARK 500     VAL I 104        24.9      L          L   OUTSIDE RANGE
REMARK 500     LEU I 284        24.9      L          L   OUTSIDE RANGE
REMARK 500     THR I 510        24.5      L          L   OUTSIDE RANGE
REMARK 500     CYS I 575        24.4      L          L   OUTSIDE RANGE
REMARK 500     ARG I 759        22.4      L          L   OUTSIDE RANGE
REMARK 500     LYS I 864        24.0      L          L   OUTSIDE RANGE
REMARK 500     ARG M 190        25.0      L          L   OUTSIDE RANGE
REMARK 500     ASP J 571        22.7      L          L   OUTSIDE RANGE
REMARK 500     VAL J 589        24.8      L          L   OUTSIDE RANGE
REMARK 500     TYR J 680        24.7      L          L   OUTSIDE RANGE
REMARK 500     HIS J1002        23.9      L          L   OUTSIDE RANGE
REMARK 500     LYS Q   3        24.9      L          L   OUTSIDE RANGE
REMARK 500     ARG U  26        24.6      L          L   OUTSIDE RANGE
REMARK 500     ASP U  60        23.8      L          L   OUTSIDE RANGE
REMARK 500     VAL U  61        24.3      L          L   OUTSIDE RANGE
REMARK 500     THR W  63        23.3      L          L   OUTSIDE RANGE
REMARK 500     ILE Z  59        24.9      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                              ZN A1001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  58   SG
REMARK 620 2 CYS A  68   SG   51.5
REMARK 620 3 HIS A  71   NE2  94.7  62.9
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1002  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  98   SG
REMARK 620 2 CYS A 146   SG   99.5
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A1003  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 458   OD2
REMARK 620 2 ASP A 460   OD1 106.9
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B2001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1061   SG
REMARK 620 2 CYS B1079   SG  116.5
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN N1001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N   7   SG
REMARK 620 2 CYS N  10   SG  119.8
REMARK 620 3 CYS N  44   SG  145.9  94.0
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN P1001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS P   9   SG
REMARK 620 2 THR P  12   OG1  95.1
REMARK 620 3 CYS P  26   SG   90.0 167.2
REMARK 620 4 CYS P  29   SG   95.8  68.3  99.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN I1002  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I  98   SG
REMARK 620 2 CYS I 146   SG   88.5
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG I1003  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 456   OD1
REMARK 620 2 ASP I 456   OD2  54.3
REMARK 620 3 ASP I 458   OD2 117.2  94.9
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN J2001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J1061   SG
REMARK 620 2 CYS J1079   SG  116.8
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN W1001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS W   7   SG
REMARK 620 2 CYS W  44   SG  163.9
REMARK 620 3 CYS W  45   SG   71.4 105.9
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN X1001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS X   9   SG
REMARK 620 2 THR X  12   OG1 106.3
REMARK 620 3 CYS X  26   SG   82.3 170.3
REMARK 620 4 CYS X  29   SG  108.6  78.8 103.0
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1002
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1003
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2001
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S D 1001
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 1001
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 1001
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 1001
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 1002
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 1003
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 2001
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S O 1001
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN W 1001
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN X 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PMZ   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF THE SULFOLOBUS SOLFATARICUS RNA
REMARK 900 POLYMERASE, 11-SUBUNIT STRUCTURE
REMARK 900 RELATED ID: 2PA8   RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF THE D/L SUBCOMPLEX OF THE
REMARK 900 SULFOLOBUS SOLFATARICUS RNA POLYMERASE
REMARK 900 RELATED ID: 2WAQ   RELATED DB: PDB
REMARK 900 THE COMPLETE STRUCTURE OF THE ARCHAEAL 13-SUBUNIT DNA-
REMARK 900 DIRECTED RNA POLYMERASE
DBREF  3HKZ A    1   880  UNP    Q980R2   RPOA1_SULSO      1    880
DBREF  3HKZ C    4   395  UNP    P58192   RPOA2_SULSO      1    392
DBREF  3HKZ D    1   265  UNP    P95989   RPOD_SULSO       1    265
DBREF  3HKZ E    1   180  UNP    Q980A3   Q980A3_SULSO     1    180
DBREF  3HKZ F    1   113  UNP    Q9UXD9   Q9UXD9_SULSO     1    113
DBREF  3HKZ G    1   132  UNP    Q980L5   Q980L5_SULSO     1    132
DBREF  3HKZ H    1    84  UNP    Q980Q9   RPOH_SULSO       1     84
DBREF  3HKZ K    1    95  UNP    Q97ZJ9   RPOK_SULSO       1     95
DBREF  3HKZ L    1    92  UNP    Q980K0   RPOL_SULSO       1     92
DBREF  3HKZ N    1    66  UNP    Q980Z8   RPON_SULSO       1     66
DBREF  3HKZ P    1    48  UNP    Q97ZX7   RPOP_SULSO       1     48
DBREF  3HKZ Y    1   104  UNP    Q980B8   Q980B8_SULSO     1    104
DBREF  3HKZ I    1   880  UNP    Q980R2   RPOA1_SULSO      1    880
DBREF  3HKZ M    4   395  UNP    P58192   RPOA2_SULSO      1    392
DBREF  3HKZ O    1   265  UNP    P95989   RPOD_SULSO       1    265
DBREF  3HKZ Q    1   180  UNP    Q980A3   Q980A3_SULSO     1    180
DBREF  3HKZ R    1   113  UNP    Q9UXD9   Q9UXD9_SULSO     1    113
DBREF  3HKZ S    1   132  UNP    Q980L5   Q980L5_SULSO     1    132
DBREF  3HKZ T    1    84  UNP    Q980Q9   RPOH_SULSO       1     84
DBREF  3HKZ U    1    95  UNP    Q97ZJ9   RPOK_SULSO       1     95
DBREF  3HKZ V    1    92  UNP    Q980K0   RPOL_SULSO       1     92
DBREF  3HKZ W    1    66  UNP    Q980Z8   RPON_SULSO       1     66
DBREF  3HKZ X    1    48  UNP    Q97ZX7   RPOP_SULSO       1     48
DBREF  3HKZ Z    1   104  UNP    Q980B8   Q980B8_SULSO     1    104
DBREF  3HKZ B    1  1124  PDB    3HKZ     3HKZ             1   1124
DBREF  3HKZ J    1  1124  PDB    3HKZ     3HKZ             1   1124
SEQADV 3HKZ MET C    1  UNP  P58192              EXPRESSION TAG
SEQADV 3HKZ GLU C    2  UNP  P58192              EXPRESSION TAG
SEQADV 3HKZ GLY C    3  UNP  P58192              EXPRESSION TAG
SEQADV 3HKZ MET M    1  UNP  P58192              EXPRESSION TAG
SEQADV 3HKZ GLU M    2  UNP  P58192              EXPRESSION TAG
SEQADV 3HKZ GLY M    3  UNP  P58192              EXPRESSION TAG
SEQRES   1 A  880  MET SER GLU LYS ASN ILE LYS GLY ILE LYS PHE GLY ILE
SEQRES   2 A  880  LEU SER PRO ASP GLU ILE ARG LYS MET SER VAL THR ALA
SEQRES   3 A  880  ILE ILE THR PRO ASP VAL TYR ASP GLU ASP GLY THR PRO
SEQRES   4 A  880  ILE GLU GLY SER VAL MET ASP PRO ARG LEU GLY VAL ILE
SEQRES   5 A  880  GLU PRO GLY GLN LYS CYS PRO THR CYS GLY ASN THR LEU
SEQRES   6 A  880  GLY ASN CYS PRO GLY HIS PHE GLY HIS ILE GLU LEU VAL
SEQRES   7 A  880  ARG PRO VAL ILE HIS VAL GLY LEU VAL LYS HIS ILE TYR
SEQRES   8 A  880  GLU PHE LEU LYS ALA THR CYS ARG ARG CYS GLY ARG VAL
SEQRES   9 A  880  LYS ILE SER GLU ASP GLU ILE GLU LYS TYR SER ARG ILE
SEQRES  10 A  880  TYR ASN ALA ILE LYS LYS ARG TRP PRO SER ALA ALA ARG
SEQRES  11 A  880  ARG LEU THR GLU TYR VAL LYS LYS THR ALA MET LYS ALA
SEQRES  12 A  880  GLN VAL CYS PRO HIS CYS ASN GLU LYS GLN TYR LYS ILE
SEQRES  13 A  880  LYS LEU GLU LYS PRO TYR ASN PHE TYR GLU GLU ARG LYS
SEQRES  14 A  880  GLU GLY VAL ALA LYS LEU THR PRO SER ASP ILE ARG GLU
SEQRES  15 A  880  ARG LEU GLU LYS ILE PRO ASP SER ASP VAL GLU ILE LEU
SEQRES  16 A  880  GLY TYR ASP PRO THR THR SER ARG PRO GLU TRP MET ILE
SEQRES  17 A  880  LEU THR VAL LEU PRO VAL PRO PRO ILE THR ILE ARG PRO
SEQRES  18 A  880  SER ILE MET ILE GLU SER GLY ILE ARG ALA GLU ASP ASP
SEQRES  19 A  880  LEU THR HIS LYS LEU VAL ASP ILE VAL ARG ILE ASN GLU
SEQRES  20 A  880  ARG LEU LYS GLU SER ILE ASP ALA GLY ALA PRO GLN LEU
SEQRES  21 A  880  ILE ILE GLU ASP LEU TRP ASP LEU LEU GLN TYR HIS VAL
SEQRES  22 A  880  ALA THR TYR PHE ASP ASN GLU ILE PRO GLY LEU PRO PRO
SEQRES  23 A  880  SER LYS HIS ARG SER GLY ARG PRO LEU ARG THR LEU ALA
SEQRES  24 A  880  GLN ARG LEU LYS GLY LYS GLU GLY ARG PHE ARG GLY ASN
SEQRES  25 A  880  LEU SER GLY LYS ARG VAL ASP PHE SER SER ARG THR VAL
SEQRES  26 A  880  ILE SER PRO ASP PRO ASN ILE SER ILE ASP GLU VAL GLY
SEQRES  27 A  880  VAL PRO GLU ILE ILE ALA LYS THR LEU THR VAL PRO GLU
SEQRES  28 A  880  ARG ILE THR PRO TRP ASN ILE GLU LYS LEU ARG GLN PHE
SEQRES  29 A  880  VAL ILE ASN GLY PRO ASP LYS TRP PRO GLY ALA ASN TYR
SEQRES  30 A  880  VAL ILE ARG PRO ASP GLY ARG ARG ILE ASP LEU ARG TYR
SEQRES  31 A  880  VAL LYS ASP ARG LYS GLU LEU ALA SER THR LEU ALA PRO
SEQRES  32 A  880  GLY TYR ILE ILE GLU ARG HIS LEU ILE ASP GLY ASP ILE
SEQRES  33 A  880  VAL LEU PHE ASN ARG GLN PRO SER LEU HIS ARG ILE SER
SEQRES  34 A  880  MET MET ALA HIS ARG VAL ARG VAL LEU LYS GLY LEU THR
SEQRES  35 A  880  PHE ARG LEU ASN LEU LEU VAL CYS PRO PRO TYR ASN ALA
SEQRES  36 A  880  ASP PHE ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN
SEQRES  37 A  880  SER GLU GLU ALA ILE ALA GLU ALA LYS GLU ILE MET LEU
SEQRES  38 A  880  VAL HIS LYS ASN ILE ILE THR PRO ARG TYR GLY GLY PRO
SEQRES  39 A  880  ILE ILE GLY ALA ALA GLN ASP TYR ILE SER GLY ALA TYR
SEQRES  40 A  880  LEU LEU THR VAL LYS THR THR LEU LEU THR LYS GLU GLU
SEQRES  41 A  880  ALA GLN GLN ILE LEU GLY VAL ALA ASP VAL LYS ILE ASP
SEQRES  42 A  880  LEU GLY GLU PRO ALA ILE LEU ALA PRO ARG GLU TYR TYR
SEQRES  43 A  880  THR GLY LYS GLN VAL ILE SER ALA PHE LEU PRO LYS ASP
SEQRES  44 A  880  PHE ASN PHE HIS GLY GLN ALA ASN VAL SER SER GLY PRO
SEQRES  45 A  880  ARG LEU CYS LYS ASN GLU ASP CYS PRO HIS ASP SER TYR
SEQRES  46 A  880  VAL VAL ILE LYS ASN GLY ILE LEU LEU GLU GLY VAL PHE
SEQRES  47 A  880  ASP LYS LYS ALA ILE GLY ASN GLN GLN PRO GLU SER ILE
SEQRES  48 A  880  LEU HIS TRP LEU ILE LYS GLU TYR SER ASP GLU TYR GLY
SEQRES  49 A  880  LYS TRP LEU MET ASP ASN LEU PHE ARG VAL PHE ILE ARG
SEQRES  50 A  880  PHE VAL GLU LEU GLN GLY PHE THR MET ARG LEU GLU ASP
SEQRES  51 A  880  VAL SER LEU GLY ASP ASP VAL LYS LYS GLU ILE TYR ASN
SEQRES  52 A  880  GLU ILE ASP ARG ALA LYS VAL GLU VAL ASP ASN LEU ILE
SEQRES  53 A  880  GLN LYS TYR LYS ASN GLY GLU LEU GLU PRO ILE PRO GLY
SEQRES  54 A  880  ARG THR LEU GLU GLU SER LEU GLU ASN TYR ILE LEU ASP
SEQRES  55 A  880  THR LEU ASP LYS LEU ARG SER THR ALA GLY ASP ILE ALA
SEQRES  56 A  880  SER LYS TYR LEU ASP PRO PHE ASN PHE ALA TYR VAL MET
SEQRES  57 A  880  ALA ARG THR GLY ALA ARG GLY SER VAL LEU ASN ILE THR
SEQRES  58 A  880  GLN MET ALA ALA MET LEU GLY GLN GLN SER VAL ARG GLY
SEQRES  59 A  880  GLU ARG ILE LYS ARG GLY TYR MET THR ARG THR LEU PRO
SEQRES  60 A  880  HIS PHE LYS PRO TYR ASP ILE SER PRO GLU ALA ARG GLY
SEQRES  61 A  880  PHE ILE TYR SER SER PHE ARG THR GLY LEU LYS PRO THR
SEQRES  62 A  880  GLU LEU PHE PHE HIS ALA ALA GLY GLY ARG GLU GLY LEU
SEQRES  63 A  880  VAL ASP THR ALA VAL ARG THR SER GLN SER GLY TYR MET
SEQRES  64 A  880  GLN ARG ARG LEU ILE ASN ALA LEU SER ASP LEU ARG ALA
SEQRES  65 A  880  GLU TYR ASP GLY THR VAL ARG SER LEU TYR GLY GLU VAL
SEQRES  66 A  880  VAL GLN VAL ALA TYR GLY ASP ASP GLY VAL PHE PRO MET
SEQRES  67 A  880  TYR SER ALA HIS GLY LYS THR VAL ASP VAL ASN ARG ILE
SEQRES  68 A  880  PHE GLU ARG VAL VAL GLY TRP LYS ALA
SEQRES   1 C  395  MET GLU GLY MET ILE ASP GLU LYS ASP LYS PRO TYR LEU
SEQRES   2 C  395  GLU GLU LYS VAL LYS GLN ALA SER ASN ILE LEU PRO GLN
SEQRES   3 C  395  LYS ILE VAL ASP ASP LEU LYS ASN LEU ILE LEU ASN LYS
SEQRES   4 C  395  GLU ILE ILE VAL THR ARG ASP GLU ILE ASP LYS ILE PHE
SEQRES   5 C  395  ASP LEU ALA ILE LYS GLU TYR SER GLU GLY LEU ILE ALA
SEQRES   6 C  395  PRO GLY GLU ALA ILE GLY ILE VAL ALA ALA GLN SER VAL
SEQRES   7 C  395  GLY GLU PRO GLY THR GLN MET THR LEU ARG THR PHE HIS
SEQRES   8 C  395  PHE ALA GLY ILE ARG GLU LEU ASN VAL THR LEU GLY LEU
SEQRES   9 C  395  PRO ARG LEU ILE GLU ILE VAL ASP ALA LYS LYS VAL PRO
SEQRES  10 C  395  SER THR PRO MET MET THR ILE TYR LEU THR ASP GLU TYR
SEQRES  11 C  395  LYS ARG ASP ARG ASP LYS ALA LEU GLU VAL ALA ARG LYS
SEQRES  12 C  395  LEU GLU TYR THR LYS ILE GLU ASN VAL VAL SER SER THR
SEQRES  13 C  395  SER ILE ASP ILE ALA SER MET SER ILE ILE LEU GLN LEU
SEQRES  14 C  395  ASP ASN GLU MET LEU LYS ASP LYS GLY VAL THR VAL ASP
SEQRES  15 C  395  ASP VAL LYS LYS ALA ILE GLY ARG LEU LYS LEU GLY ASP
SEQRES  16 C  395  PHE MET ILE GLU GLU SER GLU ASP SER THR LEU ASN ILE
SEQRES  17 C  395  ASN PHE ALA ASN ILE ASP SER ILE ALA ALA LEU PHE LYS
SEQRES  18 C  395  LEU ARG ASP LYS ILE LEU ASN THR LYS ILE LYS GLY ILE
SEQRES  19 C  395  LYS GLY ILE LYS ARG ALA ILE VAL GLN LYS LYS GLY ASP
SEQRES  20 C  395  GLU TYR ILE ILE LEU THR ASP GLY SER ASN LEU SER GLY
SEQRES  21 C  395  VAL LEU SER VAL LYS GLY VAL ASP VAL ALA LYS VAL GLU
SEQRES  22 C  395  THR ASN ASN ILE ARG GLU ILE GLU GLU VAL PHE GLY ILE
SEQRES  23 C  395  GLU ALA ALA ARG GLU ILE ILE ILE ARG GLU ILE SER LYS
SEQRES  24 C  395  VAL LEU ALA GLU GLN GLY LEU ASP VAL ASP ILE ARG HIS
SEQRES  25 C  395  ILE LEU LEU ILE ALA ASP VAL MET THR ARG THR GLY ILE
SEQRES  26 C  395  VAL ARG GLN ILE GLY ARG HIS GLY VAL THR GLY GLU LYS
SEQRES  27 C  395  ASN SER VAL LEU ALA ARG ALA ALA PHE GLU VAL THR VAL
SEQRES  28 C  395  LYS HIS LEU LEU ASP ALA ALA ALA ARG GLY ASP VAL GLU
SEQRES  29 C  395  GLU PHE LYS GLY VAL VAL GLU ASN ILE ILE ILE GLY HIS
SEQRES  30 C  395  PRO ILE LYS LEU GLY THR GLY MET VAL GLU LEU THR MET
SEQRES  31 C  395  ARG PRO ILE LEU ARG
SEQRES   1 B 1124  MET ALA SER ASN LEU THR ILE ASP GLU ARG TRP ARG VAL
SEQRES   2 B 1124  ILE GLU ALA TYR PHE LYS SER LYS GLY LEU VAL ARG GLN
SEQRES   3 B 1124  HIS LEU ASP SER TYR ASN ASP PHE VAL ARG ASN LYS LEU
SEQRES   4 B 1124  GLN GLU ILE ILE ASP GLU GLN GLY GLU ILE PRO THR GLU
SEQRES   5 B 1124  ILE PRO GLY LEU LYS VAL ARG LEU GLY LYS ILE ARG ILE
SEQRES   6 B 1124  GLY LYS PRO ARG VAL ARG GLU SER ASP ARG GLY GLU ARG
SEQRES   7 B 1124  GLU ILE SER PRO MET GLU ALA ARG LEU ARG ASN LEU THR
SEQRES   8 B 1124  TYR ALA ALA PRO LEU TRP LEU THR MET ILE PRO VAL GLU
SEQRES   9 B 1124  ASN ASN ILE GLU ALA GLU PRO GLU GLU VAL TYR ILE GLY
SEQRES  10 B 1124  ASP LEU PRO ILE MET LEU LYS SER ALA ILE ASP PRO ILE
SEQRES  11 B 1124  SER GLN TYR THR LEU ASP LYS LEU ILE GLU ILE GLY GLU
SEQRES  12 B 1124  ASP PRO LYS ASP PRO GLY GLY TYR PHE ILE VAL ASN GLY
SEQRES  13 B 1124  SER GLU ARG VAL ILE VAL THR GLN GLU ASP LEU ALA PRO
SEQRES  14 B 1124  ASN ARG VAL LEU VAL ASP THR GLY LYS THR GLY SER ASN
SEQRES  15 B 1124  ILE THR HIS THR ALA LYS ILE ILE SER SER THR ALA GLY
SEQRES  16 B 1124  TYR ARG VAL PRO VAL THR ILE GLU ARG LEU LYS ASP GLY
SEQRES  17 B 1124  THR PHE HIS VAL SER PHE PRO ALA VAL PRO GLY LYS ILE
SEQRES  18 B 1124  PRO PHE VAL ILE LEU MET ARG ALA LEU GLY ILE LEU THR
SEQRES  19 B 1124  ASP ARG ASP ILE VAL TYR ALA VAL SER LEU ASP PRO GLU
SEQRES  20 B 1124  VAL GLN ASN GLU LEU PHE PRO SER LEU GLU GLN ALA SER
SEQRES  21 B 1124  SER ILE ALA ASN VAL ASP ASP ALA LEU ASP PHE ILE GLY
SEQRES  22 B 1124  SER ARG VAL ALA ILE GLY GLN LYS ARG GLU ASN ARG ILE
SEQRES  23 B 1124  GLU LYS ALA GLN GLN ILE ILE ASP LYS TYR PHE LEU PRO
SEQRES  24 B 1124  HIS LEU GLY THR SER ALA GLU ASP ARG LYS LYS LYS ALA
SEQRES  25 B 1124  TYR TYR LEU ALA TYR ALA ILE SER LYS VAL ILE GLU LEU
SEQRES  26 B 1124  TYR LEU GLY ARG ARG GLU PRO ASP ASP LYS ASP HIS TYR
SEQRES  27 B 1124  ALA ASN LYS ARG LEU ARG LEU ALA GLY ASP LEU PHE ALA
SEQRES  28 B 1124  SER LEU PHE ARG VAL ALA PHE LYS ALA PHE VAL LYS ASP
SEQRES  29 B 1124  LEU THR TYR GLN LEU GLU LYS SER LYS VAL ARG GLY ARG
SEQRES  30 B 1124  LYS LEU ALA LEU LYS ALA LEU VAL ARG PRO ASP ILE VAL
SEQRES  31 B 1124  THR GLU ARG ILE ARG HIS ALA LEU ALA THR GLY ASN TRP
SEQRES  32 B 1124  VAL GLY GLY ARG THR GLY VAL SER GLN LEU LEU ASP ARG
SEQRES  33 B 1124  THR ASN TRP LEU SER MET LEU SER HIS LEU ARG ARG VAL
SEQRES  34 B 1124  ILE SER SER LEU ALA ARG GLY GLN PRO ASN PHE GLU ALA
SEQRES  35 B 1124  ARG ASP LEU HIS GLY THR GLN TRP GLY ARG MET CYS PRO
SEQRES  36 B 1124  PHE GLU THR PRO GLU GLY PRO ASN SER GLY LEU VAL LYS
SEQRES  37 B 1124  ASN LEU ALA LEU MET ALA GLN ILE ALA VAL GLY ILE ASN
SEQRES  38 B 1124  GLU ARG ILE VAL GLU LYS THR LEU TYR GLU MET GLY VAL
SEQRES  39 B 1124  VAL PRO VAL GLU GLU VAL ILE ARG ARG VAL THR GLU GLY
SEQRES  40 B 1124  GLY GLU ASP GLN ASN GLU TYR LEU LYS TRP SER LYS VAL
SEQRES  41 B 1124  ILE LEU ASN GLY ARG LEU ILE GLY TYR TYR GLN ASP GLY
SEQRES  42 B 1124  GLY GLU LEU ALA ASN LYS ILE ARG GLU ARG ARG ARG LYS
SEQRES  43 B 1124  GLY GLU ILE SER ASP GLU VAL ASN VAL GLY HIS ILE VAL
SEQRES  44 B 1124  THR ASP PHE ILE ASN GLU VAL HIS VAL ASN CYS ASP SER
SEQRES  45 B 1124  GLY ARG VAL ARG ARG PRO LEU ILE ILE VAL SER ASN GLY
SEQRES  46 B 1124  ASN PRO LEU VAL THR ILE GLU ASP ILE GLU LYS LEU GLU
SEQRES  47 B 1124  SER GLY ALA ILE THR PHE ASP ASP LEU VAL ARG GLN GLY
SEQRES  48 B 1124  LYS ILE GLU TYR LEU ASP ALA GLU GLU GLU GLU ASN ALA
SEQRES  49 B 1124  TYR VAL ALA LEU GLU PRO ASN ASP LEU THR PRO ASP HIS
SEQRES  50 B 1124  THR HIS LEU GLU ILE TRP SER PRO ALA ILE LEU GLY ILE
SEQRES  51 B 1124  THR ALA SER ILE ILE PRO TYR PRO GLU HIS ASN GLN SER
SEQRES  52 B 1124  PRO ARG ASN THR TYR GLN SER ALA MET ALA LYS GLN ALA
SEQRES  53 B 1124  LEU GLY LEU TYR ALA ALA ASN TYR GLN LEU ARG THR ASP
SEQRES  54 B 1124  THR ARG ALA HIS LEU LEU HIS TYR PRO GLN ARG PRO LEU
SEQRES  55 B 1124  VAL GLN THR ARG ALA LEU ASP ILE ILE GLY TYR THR ASN
SEQRES  56 B 1124  ARG PRO ALA GLY ASN ASN ALA ILE LEU ALA VAL MET SER
SEQRES  57 B 1124  PHE THR GLY TYR ASN MET GLU ASP SER ILE ILE MET ASN
SEQRES  58 B 1124  ARG SER SER VAL GLU ARG GLY MET TYR ARG SER THR PHE
SEQRES  59 B 1124  PHE ARG LEU TYR SER THR GLU GLU VAL LYS TYR PRO GLY
SEQRES  60 B 1124  GLY GLN GLU ASP LYS ILE VAL MET PRO GLU ALA GLY VAL
SEQRES  61 B 1124  ARG GLY TYR LYS GLY LYS GLU TYR TYR ARG LEU LEU GLU
SEQRES  62 B 1124  ASP ASN GLY VAL VAL SER PRO GLU VAL GLU VAL LYS GLY
SEQRES  63 B 1124  GLY ASP VAL LEU ILE GLY LYS VAL SER PRO PRO ARG PHE
SEQRES  64 B 1124  LEU GLN GLU PHE LYS GLU LEU SER PRO GLU GLN ALA LYS
SEQRES  65 B 1124  ARG ASP THR SER ILE VAL THR ARG HIS GLY GLU MET GLY
SEQRES  66 B 1124  ILE VAL ASP LEU VAL LEU ILE THR GLU THR ALA GLU GLY
SEQRES  67 B 1124  ASN LYS LEU VAL LYS VAL ARG VAL ARG ASP LEU ARG ILE
SEQRES  68 B 1124  PRO THR ILE GLY ASP LYS PHE ALA SER ARG HIS GLY GLN
SEQRES  69 B 1124  LYS GLY VAL ILE GLY MET LEU ILE PRO GLN VAL ASP MET
SEQRES  70 B 1124  PRO TYR THR VAL LYS GLY VAL VAL PRO ASP ILE ILE LEU
SEQRES  71 B 1124  ASN PRO HIS ALA LEU PRO SER ARG MET THR LEU GLY GLN
SEQRES  72 B 1124  ILE MET GLU GLY ILE ALA GLY LYS TYR ALA ALA LEU SER
SEQRES  73 B 1124  GLY ASN ILE VAL ASP ALA THR PRO PHE TYR LYS THR PRO
SEQRES  74 B 1124  ILE GLU GLN LEU GLN ASN GLU ILE LEU ARG TYR GLY TYR
SEQRES  75 B 1124  LEU PRO ASP ALA THR GLU VAL VAL TYR ASP GLY ARG THR
SEQRES  76 B 1124  GLY GLN LYS ILE LYS SER ARG ILE TYR PHE GLY VAL VAL
SEQRES  77 B 1124  TYR TYR GLN LYS LEU HIS HIS MET VAL ALA ASP LYS LEU
SEQRES  78 B 1124  HIS ALA ARG ALA ARG GLY PRO VAL GLN ILE LEU THR ARG
SEQRES  79 B 1124  GLN PRO THR GLU GLY ARG ALA ARG GLU GLY GLY LEU ARG
SEQRES  80 B 1124  PHE GLY GLU MET GLU ARG ASP CYS LEU ILE GLY PHE GLY
SEQRES  81 B 1124  THR ALA MET LEU LEU LYS ASP ARG LEU LEU ASP ASN SER
SEQRES  82 B 1124  ASP ARG THR MET ILE TYR VAL CYS ASP GLN CYS GLY TYR
SEQRES  83 B 1124  ILE GLY TRP TYR ASP LYS ASN LYS ASN LYS TYR VAL CYS
SEQRES  84 B 1124  PRO ILE HIS GLY ASP LYS SER ASN LEU PHE PRO VAL THR
SEQRES  85 B 1124  VAL SER TYR ALA PHE LYS LEU LEU ILE GLN GLU LEU MET
SEQRES  86 B 1124  SER MET ILE ILE SER PRO ARG LEU VAL LEU GLU ASP LYS
SEQRES  87 B 1124  VAL GLY LEU SER GLY GLY
SEQRES   1 D  265  MET SER ILE ASN LEU LEU HIS LYS ASP ASP THR ARG ILE
SEQRES   2 D  265  ASP LEU VAL PHE GLU GLY TYR PRO LEU GLU PHE VAL ASN
SEQRES   3 D  265  ALA ILE ARG ARG ALA SER MET LEU TYR VAL PRO ILE MET
SEQRES   4 D  265  ALA VAL ASP ASP VAL TYR PHE ILE GLU ASN ASN SER PRO
SEQRES   5 D  265  LEU TYR ASP GLU ILE LEU ALA HIS ARG LEU ALA LEU ILE
SEQRES   6 D  265  PRO PHE MET SER GLU GLU ALA LEU ASP THR TYR ARG TRP
SEQRES   7 D  265  PRO GLU GLU CYS ILE GLU CYS THR GLU ASN CYS GLU LYS
SEQRES   8 D  265  CYS TYR THR LYS ILE TYR ILE GLU ALA GLU ALA PRO ASN
SEQRES   9 D  265  GLU PRO ARG MET ILE TYR SER LYS ASP ILE LYS SER GLU
SEQRES  10 D  265  ASP PRO SER VAL VAL PRO ILE SER GLY ASP ILE PRO ILE
SEQRES  11 D  265  VAL LEU LEU GLY THR ASN GLN LYS ILE SER LEU GLU ALA
SEQRES  12 D  265  ARG LEU ARG LEU GLY TYR GLY LYS GLU HIS ALA LYS PHE
SEQRES  13 D  265  ILE PRO VAL SER LEU SER VAL VAL ARG TYR TYR PRO LYS
SEQRES  14 D  265  VAL GLU ILE LEU ALA ASN CYS GLU LYS ALA VAL ASN VAL
SEQRES  15 D  265  CYS PRO GLU GLY VAL PHE GLU LEU LYS ASP GLY LYS LEU
SEQRES  16 D  265  SER VAL LYS ASN GLU LEU SER CYS THR LEU CYS GLU GLU
SEQRES  17 D  265  CYS LEU ARG TYR CYS ASN GLY SER ILE ARG ILE SER PHE
SEQRES  18 D  265  VAL GLU ASP LYS TYR ILE LEU GLU ILE GLU SER VAL GLY
SEQRES  19 D  265  SER LEU LYS PRO GLU ARG ILE LEU LEU GLU ALA GLY LYS
SEQRES  20 D  265  SER ILE ILE ARG LYS ILE GLU GLU LEU GLU LYS LYS LEU
SEQRES  21 D  265  VAL GLU VAL VAL LYS
SEQRES   1 E  180  MET TYR LYS LEU ILE LYS ALA ARG SER ILE VAL ARG ILE
SEQRES   2 E  180  PRO PRO ASN GLU PHE GLY LYS PRO LEU ASN GLU ILE ALA
SEQRES   3 E  180  LEU ASN GLU LEU ARG GLN GLN TYR GLN GLU LYS ILE LEU
SEQRES   4 E  180  LYS ASP LEU GLY LEU VAL LEU ALA ILE LEU ASN VAL LYS
SEQRES   5 E  180  THR SER GLU GLU GLY ILE LEU VAL PHE GLY ASP GLY ALA
SEQRES   6 E  180  THR TYR HIS GLU VAL GLU PHE ASP MET ILE THR TYR VAL
SEQRES   7 E  180  PRO VAL VAL GLN GLU VAL VAL GLU GLY GLU VAL LEU GLN
SEQRES   8 E  180  VAL ASP ASN TYR GLY ILE PHE VAL ASN LEU GLY PRO MET
SEQRES   9 E  180  ASP GLY LEU VAL HIS ILE SER GLN ILE THR ASP ASP THR
SEQRES  10 E  180  LEU LYS TYR ASP ASN VAL ARG GLY ILE ILE PHE GLY GLU
SEQRES  11 E  180  LYS SER LYS LYS VAL ILE GLN LYS GLY ASP LYS VAL ARG
SEQRES  12 E  180  ALA ARG VAL ILE SER VAL ALA SER THR VAL THR GLY ARG
SEQRES  13 E  180  LEU PRO ARG ILE ALA LEU THR MET ARG GLN PRO TYR LEU
SEQRES  14 E  180  GLY LYS LEU GLU TRP ILE THR GLN THR LYS LYS
SEQRES   1 F  113  MET SER SER VAL TYR ILE VAL GLU GLU HIS TYR ILE PRO
SEQRES   2 F  113  TYR SER VAL ALA LYS LYS LEU LEU THR ASP VAL ILE ARG
SEQRES   3 F  113  SER GLY GLY SER SER ASN LEU LEU GLN ARG THR TYR ASP
SEQRES   4 F  113  TYR LEU ASN SER VAL GLU LYS CYS ASP ALA GLU SER ALA
SEQRES   5 F  113  GLN LYS VAL ILE GLU GLU LEU SER ASN ILE VAL SER ARG
SEQRES   6 F  113  GLU ASP VAL ARG ALA ILE LEU ALA SER ILE CYS PRO THR
SEQRES   7 F  113  THR SER ASP GLU VAL ARG SER ILE LEU VAL MET ASP THR
SEQRES   8 F  113  ASN LYS THR TYR THR SER GLU ASP ILE GLN LYS ILE ILE
SEQRES   9 F  113  ASP ILE ILE ARG LYS TYR ILE LYS SER
SEQRES   1 G  132  MET MET GLU SER VAL ALA GLN GLU ILE ILE LEU SER CYS
SEQRES   2 G  132  GLU ILE ASN SER ILE GLU ARG GLY SER LEU LYS ASN LEU
SEQRES   3 G  132  SER MET VAL ASN MET SER CYS ASN GLY PHE ASN VAL SER
SEQRES   4 G  132  PHE ASP ILE ILE ASP SER ILE ASN ILE PHE SER GLN LYS
SEQRES   5 G  132  GLU LYS VAL LYS VAL ILE ILE SER LYS ASN ARG PRO SER
SEQRES   6 G  132  TYR SER HIS ASP ASP PHE CYS GLY HIS GLY TYR ILE VAL
SEQRES   7 G  132  THR GLU LEU LYS ASP SER SER LEU ASN ASN GLY ASN LYS
SEQRES   8 G  132  TYR THR THR ILE ILE SER LEU TYR GLY LEU LEU VAL LYS
SEQRES   9 G  132  ILE ILE SER ASN LYS GLU SER PHE LEU ARG THR SER GLN
SEQRES  10 G  132  LEU ASN ILE MET ASP HIS VAL TYR PHE CYS VAL LYS LYS
SEQRES  11 G  132  ASN ASN
SEQRES   1 H   84  MET ARG GLY SER SER ASN LYS LYS ILE ASP PRO ARG ILE
SEQRES   2 H   84  HIS TYR LEU VAL PRO LYS HIS GLU VAL LEU ASN ILE ASP
SEQRES   3 H   84  GLU ALA TYR LYS ILE LEU LYS GLU LEU GLY ILE ARG PRO
SEQRES   4 H   84  GLU GLN LEU PRO TRP ILE ARG ALA SER ASP PRO VAL ALA
SEQRES   5 H   84  ARG SER ILE ASN ALA LYS PRO GLY ASP ILE ILE ARG ILE
SEQRES   6 H   84  ILE ARG LYS SER GLN LEU TYR GLY GLU VAL VAL SER TYR
SEQRES   7 H   84  ARG TYR VAL ILE SER GLY
SEQRES   1 K   95  MET GLY LEU GLU ARG ASP GLU ILE LEU SER GLN ASP LEU
SEQRES   2 K   95  HIS PHE ASN GLU VAL PHE ILE SER LEU TRP GLN ASN ARG
SEQRES   3 K   95  LEU THR ARG TYR GLU ILE ALA ARG VAL ILE SER ALA ARG
SEQRES   4 K   95  ALA LEU GLN LEU ALA MET GLY ALA PRO ALA LEU ILE ASP
SEQRES   5 K   95  ILE ASN ASN LEU SER SER THR ASP VAL ILE SER ILE ALA
SEQRES   6 K   95  GLU GLU GLU PHE ARG ARG GLY VAL LEU PRO ILE THR ILE
SEQRES   7 K   95  ARG ARG ARG LEU PRO ASN GLY LYS ILE ILE LEU LEU SER
SEQRES   8 K   95  LEU ARG LYS SER
SEQRES   1 L   92  MET GLU ILE ARG ILE LEU LYS SER GLU SER ASN TYR LEU
SEQRES   2 L   92  GLU LEU GLU ILE GLU GLY GLU ASP HIS THR LEU GLY ASN
SEQRES   3 L   92  LEU ILE ALA GLY THR LEU ARG ARG ILE SER GLY VAL SER
SEQRES   4 L   92  PHE ALA SER TYR TYR GLN PRO HIS PRO LEU SER ASP LYS
SEQRES   5 L   92  ILE ILE VAL LYS ILE LEU THR ASP GLY SER ILE THR PRO
SEQRES   6 L   92  LYS ASP ALA LEU LEU LYS ALA ILE GLU ASN ILE ARG GLY
SEQRES   7 L   92  MET THR SER HIS TYR ILE ASP GLU ILE LYS GLY LEU THR
SEQRES   8 L   92  LYS
SEQRES   1 N   66  MET LEU ILE PRO ILE ARG CYS PHE THR CYS GLY SER LEU
SEQRES   2 N   66  ILE ALA ASP LYS TRP GLN SER PHE ILE THR ARG VAL ASN
SEQRES   3 N   66  ALA GLY GLU ASN PRO GLY LYS VAL LEU ASP ASP LEU GLY
SEQRES   4 N   66  VAL LYS ARG TYR CYS CYS ARG ARG MET LEU LEU SER HIS
SEQRES   5 N   66  VAL ASP ILE ILE ASN GLU VAL ILE HIS TYR THR ARG PRO
SEQRES   6 N   66  ILE
SEQRES   1 P   48  MET ALA VAL TYR ARG CYS GLY LYS CYS TRP LYS THR PHE
SEQRES   2 P   48  THR ASP GLU GLN LEU LYS VAL LEU PRO GLY VAL ARG CYS
SEQRES   3 P   48  PRO TYR CYS GLY TYR LYS ILE ILE PHE MET VAL ARG LYS
SEQRES   4 P   48  PRO THR ILE LYS ILE VAL LYS ALA ILE
SEQRES   1 Y  104  MET VAL SER GLY MET SER THR ASP GLU GLU LYS GLU GLY
SEQRES   2 Y  104  THR SER ASP GLU GLU VAL ASN GLU GLU LYS GLU VAL GLU
SEQRES   3 Y  104  GLU THR SER GLU ASP GLU PHE PRO LYS LEU SER ILE GLN
SEQRES   4 Y  104  ASP ILE GLU LEU LEU MET ARG ASN THR GLU ILE TRP ASP
SEQRES   5 Y  104  ASN LEU LEU ASN GLY LYS ILE THR LEU GLU GLU ALA LYS
SEQRES   6 Y  104  LYS LEU PHE GLU ASP ASN TYR LYS GLU TYR GLU LYS ARG
SEQRES   7 Y  104  ASP SER ARG ARG LYS ALA LYS LYS ALA VAL SER LYS LYS
SEQRES   8 Y  104  VAL LYS LYS THR LYS LYS LYS GLU LYS SER VAL GLU GLY
SEQRES   1 I  880  MET SER GLU LYS ASN ILE LYS GLY ILE LYS PHE GLY ILE
SEQRES   2 I  880  LEU SER PRO ASP GLU ILE ARG LYS MET SER VAL THR ALA
SEQRES   3 I  880  ILE ILE THR PRO ASP VAL TYR ASP GLU ASP GLY THR PRO
SEQRES   4 I  880  ILE GLU GLY SER VAL MET ASP PRO ARG LEU GLY VAL ILE
SEQRES   5 I  880  GLU PRO GLY GLN LYS CYS PRO THR CYS GLY ASN THR LEU
SEQRES   6 I  880  GLY ASN CYS PRO GLY HIS PHE GLY HIS ILE GLU LEU VAL
SEQRES   7 I  880  ARG PRO VAL ILE HIS VAL GLY LEU VAL LYS HIS ILE TYR
SEQRES   8 I  880  GLU PHE LEU LYS ALA THR CYS ARG ARG CYS GLY ARG VAL
SEQRES   9 I  880  LYS ILE SER GLU ASP GLU ILE GLU LYS TYR SER ARG ILE
SEQRES  10 I  880  TYR ASN ALA ILE LYS LYS ARG TRP PRO SER ALA ALA ARG
SEQRES  11 I  880  ARG LEU THR GLU TYR VAL LYS LYS THR ALA MET LYS ALA
SEQRES  12 I  880  GLN VAL CYS PRO HIS CYS ASN GLU LYS GLN TYR LYS ILE
SEQRES  13 I  880  LYS LEU GLU LYS PRO TYR ASN PHE TYR GLU GLU ARG LYS
SEQRES  14 I  880  GLU GLY VAL ALA LYS LEU THR PRO SER ASP ILE ARG GLU
SEQRES  15 I  880  ARG LEU GLU LYS ILE PRO ASP SER ASP VAL GLU ILE LEU
SEQRES  16 I  880  GLY TYR ASP PRO THR THR SER ARG PRO GLU TRP MET ILE
SEQRES  17 I  880  LEU THR VAL LEU PRO VAL PRO PRO ILE THR ILE ARG PRO
SEQRES  18 I  880  SER ILE MET ILE GLU SER GLY ILE ARG ALA GLU ASP ASP
SEQRES  19 I  880  LEU THR HIS LYS LEU VAL ASP ILE VAL ARG ILE ASN GLU
SEQRES  20 I  880  ARG LEU LYS GLU SER ILE ASP ALA GLY ALA PRO GLN LEU
SEQRES  21 I  880  ILE ILE GLU ASP LEU TRP ASP LEU LEU GLN TYR HIS VAL
SEQRES  22 I  880  ALA THR TYR PHE ASP ASN GLU ILE PRO GLY LEU PRO PRO
SEQRES  23 I  880  SER LYS HIS ARG SER GLY ARG PRO LEU ARG THR LEU ALA
SEQRES  24 I  880  GLN ARG LEU LYS GLY LYS GLU GLY ARG PHE ARG GLY ASN
SEQRES  25 I  880  LEU SER GLY LYS ARG VAL ASP PHE SER SER ARG THR VAL
SEQRES  26 I  880  ILE SER PRO ASP PRO ASN ILE SER ILE ASP GLU VAL GLY
SEQRES  27 I  880  VAL PRO GLU ILE ILE ALA LYS THR LEU THR VAL PRO GLU
SEQRES  28 I  880  ARG ILE THR PRO TRP ASN ILE GLU LYS LEU ARG GLN PHE
SEQRES  29 I  880  VAL ILE ASN GLY PRO ASP LYS TRP PRO GLY ALA ASN TYR
SEQRES  30 I  880  VAL ILE ARG PRO ASP GLY ARG ARG ILE ASP LEU ARG TYR
SEQRES  31 I  880  VAL LYS ASP ARG LYS GLU LEU ALA SER THR LEU ALA PRO
SEQRES  32 I  880  GLY TYR ILE ILE GLU ARG HIS LEU ILE ASP GLY ASP ILE
SEQRES  33 I  880  VAL LEU PHE ASN ARG GLN PRO SER LEU HIS ARG ILE SER
SEQRES  34 I  880  MET MET ALA HIS ARG VAL ARG VAL LEU LYS GLY LEU THR
SEQRES  35 I  880  PHE ARG LEU ASN LEU LEU VAL CYS PRO PRO TYR ASN ALA
SEQRES  36 I  880  ASP PHE ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN
SEQRES  37 I  880  SER GLU GLU ALA ILE ALA GLU ALA LYS GLU ILE MET LEU
SEQRES  38 I  880  VAL HIS LYS ASN ILE ILE THR PRO ARG TYR GLY GLY PRO
SEQRES  39 I  880  ILE ILE GLY ALA ALA GLN ASP TYR ILE SER GLY ALA TYR
SEQRES  40 I  880  LEU LEU THR VAL LYS THR THR LEU LEU THR LYS GLU GLU
SEQRES  41 I  880  ALA GLN GLN ILE LEU GLY VAL ALA ASP VAL LYS ILE ASP
SEQRES  42 I  880  LEU GLY GLU PRO ALA ILE LEU ALA PRO ARG GLU TYR TYR
SEQRES  43 I  880  THR GLY LYS GLN VAL ILE SER ALA PHE LEU PRO LYS ASP
SEQRES  44 I  880  PHE ASN PHE HIS GLY GLN ALA ASN VAL SER SER GLY PRO
SEQRES  45 I  880  ARG LEU CYS LYS ASN GLU ASP CYS PRO HIS ASP SER TYR
SEQRES  46 I  880  VAL VAL ILE LYS ASN GLY ILE LEU LEU GLU GLY VAL PHE
SEQRES  47 I  880  ASP LYS LYS ALA ILE GLY ASN GLN GLN PRO GLU SER ILE
SEQRES  48 I  880  LEU HIS TRP LEU ILE LYS GLU TYR SER ASP GLU TYR GLY
SEQRES  49 I  880  LYS TRP LEU MET ASP ASN LEU PHE ARG VAL PHE ILE ARG
SEQRES  50 I  880  PHE VAL GLU LEU GLN GLY PHE THR MET ARG LEU GLU ASP
SEQRES  51 I  880  VAL SER LEU GLY ASP ASP VAL LYS LYS GLU ILE TYR ASN
SEQRES  52 I  880  GLU ILE ASP ARG ALA LYS VAL GLU VAL ASP ASN LEU ILE
SEQRES  53 I  880  GLN LYS TYR LYS ASN GLY GLU LEU GLU PRO ILE PRO GLY
SEQRES  54 I  880  ARG THR LEU GLU GLU SER LEU GLU ASN TYR ILE LEU ASP
SEQRES  55 I  880  THR LEU ASP LYS LEU ARG SER THR ALA GLY ASP ILE ALA
SEQRES  56 I  880  SER LYS TYR LEU ASP PRO PHE ASN PHE ALA TYR VAL MET
SEQRES  57 I  880  ALA ARG THR GLY ALA ARG GLY SER VAL LEU ASN ILE THR
SEQRES  58 I  880  GLN MET ALA ALA MET LEU GLY GLN GLN SER VAL ARG GLY
SEQRES  59 I  880  GLU ARG ILE LYS ARG GLY TYR MET THR ARG THR LEU PRO
SEQRES  60 I  880  HIS PHE LYS PRO TYR ASP ILE SER PRO GLU ALA ARG GLY
SEQRES  61 I  880  PHE ILE TYR SER SER PHE ARG THR GLY LEU LYS PRO THR
SEQRES  62 I  880  GLU LEU PHE PHE HIS ALA ALA GLY GLY ARG GLU GLY LEU
SEQRES  63 I  880  VAL ASP THR ALA VAL ARG THR SER GLN SER GLY TYR MET
SEQRES  64 I  880  GLN ARG ARG LEU ILE ASN ALA LEU SER ASP LEU ARG ALA
SEQRES  65 I  880  GLU TYR ASP GLY THR VAL ARG SER LEU TYR GLY GLU VAL
SEQRES  66 I  880  VAL GLN VAL ALA TYR GLY ASP ASP GLY VAL PHE PRO MET
SEQRES  67 I  880  TYR SER ALA HIS GLY LYS THR VAL ASP VAL ASN ARG ILE
SEQRES  68 I  880  PHE GLU ARG VAL VAL GLY TRP LYS ALA
SEQRES   1 M  395  MET GLU GLY MET ILE ASP GLU LYS ASP LYS PRO TYR LEU
SEQRES   2 M  395  GLU GLU LYS VAL LYS GLN ALA SER ASN ILE LEU PRO GLN
SEQRES   3 M  395  LYS ILE VAL ASP ASP LEU LYS ASN LEU ILE LEU ASN LYS
SEQRES   4 M  395  GLU ILE ILE VAL THR ARG ASP GLU ILE ASP LYS ILE PHE
SEQRES   5 M  395  ASP LEU ALA ILE LYS GLU TYR SER GLU GLY LEU ILE ALA
SEQRES   6 M  395  PRO GLY GLU ALA ILE GLY ILE VAL ALA ALA GLN SER VAL
SEQRES   7 M  395  GLY GLU PRO GLY THR GLN MET THR LEU ARG THR PHE HIS
SEQRES   8 M  395  PHE ALA GLY ILE ARG GLU LEU ASN VAL THR LEU GLY LEU
SEQRES   9 M  395  PRO ARG LEU ILE GLU ILE VAL ASP ALA LYS LYS VAL PRO
SEQRES  10 M  395  SER THR PRO MET MET THR ILE TYR LEU THR ASP GLU TYR
SEQRES  11 M  395  LYS ARG ASP ARG ASP LYS ALA LEU GLU VAL ALA ARG LYS
SEQRES  12 M  395  LEU GLU TYR THR LYS ILE GLU ASN VAL VAL SER SER THR
SEQRES  13 M  395  SER ILE ASP ILE ALA SER MET SER ILE ILE LEU GLN LEU
SEQRES  14 M  395  ASP ASN GLU MET LEU LYS ASP LYS GLY VAL THR VAL ASP
SEQRES  15 M  395  ASP VAL LYS LYS ALA ILE GLY ARG LEU LYS LEU GLY ASP
SEQRES  16 M  395  PHE MET ILE GLU GLU SER GLU ASP SER THR LEU ASN ILE
SEQRES  17 M  395  ASN PHE ALA ASN ILE ASP SER ILE ALA ALA LEU PHE LYS
SEQRES  18 M  395  LEU ARG ASP LYS ILE LEU ASN THR LYS ILE LYS GLY ILE
SEQRES  19 M  395  LYS GLY ILE LYS ARG ALA ILE VAL GLN LYS LYS GLY ASP
SEQRES  20 M  395  GLU TYR ILE ILE LEU THR ASP GLY SER ASN LEU SER GLY
SEQRES  21 M  395  VAL LEU SER VAL LYS GLY VAL ASP VAL ALA LYS VAL GLU
SEQRES  22 M  395  THR ASN ASN ILE ARG GLU ILE GLU GLU VAL PHE GLY ILE
SEQRES  23 M  395  GLU ALA ALA ARG GLU ILE ILE ILE ARG GLU ILE SER LYS
SEQRES  24 M  395  VAL LEU ALA GLU GLN GLY LEU ASP VAL ASP ILE ARG HIS
SEQRES  25 M  395  ILE LEU LEU ILE ALA ASP VAL MET THR ARG THR GLY ILE
SEQRES  26 M  395  VAL ARG GLN ILE GLY ARG HIS GLY VAL THR GLY GLU LYS
SEQRES  27 M  395  ASN SER VAL LEU ALA ARG ALA ALA PHE GLU VAL THR VAL
SEQRES  28 M  395  LYS HIS LEU LEU ASP ALA ALA ALA ARG GLY ASP VAL GLU
SEQRES  29 M  395  GLU PHE LYS GLY VAL VAL GLU ASN ILE ILE ILE GLY HIS
SEQRES  30 M  395  PRO ILE LYS LEU GLY THR GLY MET VAL GLU LEU THR MET
SEQRES  31 M  395  ARG PRO ILE LEU ARG
SEQRES   1 J 1124  MET ALA SER ASN LEU THR ILE ASP GLU ARG TRP ARG VAL
SEQRES   2 J 1124  ILE GLU ALA TYR PHE LYS SER LYS GLY LEU VAL ARG GLN
SEQRES   3 J 1124  HIS LEU ASP SER TYR ASN ASP PHE VAL ARG ASN LYS LEU
SEQRES   4 J 1124  GLN GLU ILE ILE ASP GLU GLN GLY GLU ILE PRO THR GLU
SEQRES   5 J 1124  ILE PRO GLY LEU LYS VAL ARG LEU GLY LYS ILE ARG ILE
SEQRES   6 J 1124  GLY LYS PRO ARG VAL ARG GLU SER ASP ARG GLY GLU ARG
SEQRES   7 J 1124  GLU ILE SER PRO MET GLU ALA ARG LEU ARG ASN LEU THR
SEQRES   8 J 1124  TYR ALA ALA PRO LEU TRP LEU THR MET ILE PRO VAL GLU
SEQRES   9 J 1124  ASN ASN ILE GLU ALA GLU PRO GLU GLU VAL TYR ILE GLY
SEQRES  10 J 1124  ASP LEU PRO ILE MET LEU LYS SER ALA ILE ASP PRO ILE
SEQRES  11 J 1124  SER GLN TYR THR LEU ASP LYS LEU ILE GLU ILE GLY GLU
SEQRES  12 J 1124  ASP PRO LYS ASP PRO GLY GLY TYR PHE ILE VAL ASN GLY
SEQRES  13 J 1124  SER GLU ARG VAL ILE VAL THR GLN GLU ASP LEU ALA PRO
SEQRES  14 J 1124  ASN ARG VAL LEU VAL ASP THR GLY LYS THR GLY SER ASN
SEQRES  15 J 1124  ILE THR HIS THR ALA LYS ILE ILE SER SER THR ALA GLY
SEQRES  16 J 1124  TYR ARG VAL PRO VAL THR ILE GLU ARG LEU LYS ASP GLY
SEQRES  17 J 1124  THR PHE HIS VAL SER PHE PRO ALA VAL PRO GLY LYS ILE
SEQRES  18 J 1124  PRO PHE VAL ILE LEU MET ARG ALA LEU GLY ILE LEU THR
SEQRES  19 J 1124  ASP ARG ASP ILE VAL TYR ALA VAL SER LEU ASP PRO GLU
SEQRES  20 J 1124  VAL GLN ASN GLU LEU PHE PRO SER LEU GLU GLN ALA SER
SEQRES  21 J 1124  SER ILE ALA ASN VAL ASP ASP ALA LEU ASP PHE ILE GLY
SEQRES  22 J 1124  SER ARG VAL ALA ILE GLY GLN LYS ARG GLU ASN ARG ILE
SEQRES  23 J 1124  GLU LYS ALA GLN GLN ILE ILE ASP LYS TYR PHE LEU PRO
SEQRES  24 J 1124  HIS LEU GLY THR SER ALA GLU ASP ARG LYS LYS LYS ALA
SEQRES  25 J 1124  TYR TYR LEU ALA TYR ALA ILE SER LYS VAL ILE GLU LEU
SEQRES  26 J 1124  TYR LEU GLY ARG ARG GLU PRO ASP ASP LYS ASP HIS TYR
SEQRES  27 J 1124  ALA ASN LYS ARG LEU ARG LEU ALA GLY ASP LEU PHE ALA
SEQRES  28 J 1124  SER LEU PHE ARG VAL ALA PHE LYS ALA PHE VAL LYS ASP
SEQRES  29 J 1124  LEU THR TYR GLN LEU GLU LYS SER LYS VAL ARG GLY ARG
SEQRES  30 J 1124  LYS LEU ALA LEU LYS ALA LEU VAL ARG PRO ASP ILE VAL
SEQRES  31 J 1124  THR GLU ARG ILE ARG HIS ALA LEU ALA THR GLY ASN TRP
SEQRES  32 J 1124  VAL GLY GLY ARG THR GLY VAL SER GLN LEU LEU ASP ARG
SEQRES  33 J 1124  THR ASN TRP LEU SER MET LEU SER HIS LEU ARG ARG VAL
SEQRES  34 J 1124  ILE SER SER LEU ALA ARG GLY GLN PRO ASN PHE GLU ALA
SEQRES  35 J 1124  ARG ASP LEU HIS GLY THR GLN TRP GLY ARG MET CYS PRO
SEQRES  36 J 1124  PHE GLU THR PRO GLU GLY PRO ASN SER GLY LEU VAL LYS
SEQRES  37 J 1124  ASN LEU ALA LEU MET ALA GLN ILE ALA VAL GLY ILE ASN
SEQRES  38 J 1124  GLU ARG ILE VAL GLU LYS THR LEU TYR GLU MET GLY VAL
SEQRES  39 J 1124  VAL PRO VAL GLU GLU VAL ILE ARG ARG VAL THR GLU GLY
SEQRES  40 J 1124  GLY GLU ASP GLN ASN GLU TYR LEU LYS TRP SER LYS VAL
SEQRES  41 J 1124  ILE LEU ASN GLY ARG LEU ILE GLY TYR TYR GLN ASP GLY
SEQRES  42 J 1124  GLY GLU LEU ALA ASN LYS ILE ARG GLU ARG ARG ARG LYS
SEQRES  43 J 1124  GLY GLU ILE SER ASP GLU VAL ASN VAL GLY HIS ILE VAL
SEQRES  44 J 1124  THR ASP PHE ILE ASN GLU VAL HIS VAL ASN CYS ASP SER
SEQRES  45 J 1124  GLY ARG VAL ARG ARG PRO LEU ILE ILE VAL SER ASN GLY
SEQRES  46 J 1124  ASN PRO LEU VAL THR ILE GLU ASP ILE GLU LYS LEU GLU
SEQRES  47 J 1124  SER GLY ALA ILE THR PHE ASP ASP LEU VAL ARG GLN GLY
SEQRES  48 J 1124  LYS ILE GLU TYR LEU ASP ALA GLU GLU GLU GLU ASN ALA
SEQRES  49 J 1124  TYR VAL ALA LEU GLU PRO ASN ASP LEU THR PRO ASP HIS
SEQRES  50 J 1124  THR HIS LEU GLU ILE TRP SER PRO ALA ILE LEU GLY ILE
SEQRES  51 J 1124  THR ALA SER ILE ILE PRO TYR PRO GLU HIS ASN GLN SER
SEQRES  52 J 1124  PRO ARG ASN THR TYR GLN SER ALA MET ALA LYS GLN ALA
SEQRES  53 J 1124  LEU GLY LEU TYR ALA ALA ASN TYR GLN LEU ARG THR ASP
SEQRES  54 J 1124  THR ARG ALA HIS LEU LEU HIS TYR PRO GLN ARG PRO LEU
SEQRES  55 J 1124  VAL GLN THR ARG ALA LEU ASP ILE ILE GLY TYR THR ASN
SEQRES  56 J 1124  ARG PRO ALA GLY ASN ASN ALA ILE LEU ALA VAL MET SER
SEQRES  57 J 1124  PHE THR GLY TYR ASN MET GLU ASP SER ILE ILE MET ASN
SEQRES  58 J 1124  ARG SER SER VAL GLU ARG GLY MET TYR ARG SER THR PHE
SEQRES  59 J 1124  PHE ARG LEU TYR SER THR GLU GLU VAL LYS TYR PRO GLY
SEQRES  60 J 1124  GLY GLN GLU ASP LYS ILE VAL MET PRO GLU ALA GLY VAL
SEQRES  61 J 1124  ARG GLY TYR LYS GLY LYS GLU TYR TYR ARG LEU LEU GLU
SEQRES  62 J 1124  ASP ASN GLY VAL VAL SER PRO GLU VAL GLU VAL LYS GLY
SEQRES  63 J 1124  GLY ASP VAL LEU ILE GLY LYS VAL SER PRO PRO ARG PHE
SEQRES  64 J 1124  LEU GLN GLU PHE LYS GLU LEU SER PRO GLU GLN ALA LYS
SEQRES  65 J 1124  ARG ASP THR SER ILE VAL THR ARG HIS GLY GLU MET GLY
SEQRES  66 J 1124  ILE VAL ASP LEU VAL LEU ILE THR GLU THR ALA GLU GLY
SEQRES  67 J 1124  ASN LYS LEU VAL LYS VAL ARG VAL ARG ASP LEU ARG ILE
SEQRES  68 J 1124  PRO THR ILE GLY ASP LYS PHE ALA SER ARG HIS GLY GLN
SEQRES  69 J 1124  LYS GLY VAL ILE GLY MET LEU ILE PRO GLN VAL ASP MET
SEQRES  70 J 1124  PRO TYR THR VAL LYS GLY VAL VAL PRO ASP ILE ILE LEU
SEQRES  71 J 1124  ASN PRO HIS ALA LEU PRO SER ARG MET THR LEU GLY GLN
SEQRES  72 J 1124  ILE MET GLU GLY ILE ALA GLY LYS TYR ALA ALA LEU SER
SEQRES  73 J 1124  GLY ASN ILE VAL ASP ALA THR PRO PHE TYR LYS THR PRO
SEQRES  74 J 1124  ILE GLU GLN LEU GLN ASN GLU ILE LEU ARG TYR GLY TYR
SEQRES  75 J 1124  LEU PRO ASP ALA THR GLU VAL VAL TYR ASP GLY ARG THR
SEQRES  76 J 1124  GLY GLN LYS ILE LYS SER ARG ILE TYR PHE GLY VAL VAL
SEQRES  77 J 1124  TYR TYR GLN LYS LEU HIS HIS MET VAL ALA ASP LYS LEU
SEQRES  78 J 1124  HIS ALA ARG ALA ARG GLY PRO VAL GLN ILE LEU THR ARG
SEQRES  79 J 1124  GLN PRO THR GLU GLY ARG ALA ARG GLU GLY GLY LEU ARG
SEQRES  80 J 1124  PHE GLY GLU MET GLU ARG ASP CYS LEU ILE GLY PHE GLY
SEQRES  81 J 1124  THR ALA MET LEU LEU LYS ASP ARG LEU LEU ASP ASN SER
SEQRES  82 J 1124  ASP ARG THR MET ILE TYR VAL CYS ASP GLN CYS GLY TYR
SEQRES  83 J 1124  ILE GLY TRP TYR ASP LYS ASN LYS ASN LYS TYR VAL CYS
SEQRES  84 J 1124  PRO ILE HIS GLY ASP LYS SER ASN LEU PHE PRO VAL THR
SEQRES  85 J 1124  VAL SER TYR ALA PHE LYS LEU LEU ILE GLN GLU LEU MET
SEQRES  86 J 1124  SER MET ILE ILE SER PRO ARG LEU VAL LEU GLU ASP LYS
SEQRES  87 J 1124  VAL GLY LEU SER GLY GLY
SEQRES   1 O  265  MET SER ILE ASN LEU LEU HIS LYS ASP ASP THR ARG ILE
SEQRES   2 O  265  ASP LEU VAL PHE GLU GLY TYR PRO LEU GLU PHE VAL ASN
SEQRES   3 O  265  ALA ILE ARG ARG ALA SER MET LEU TYR VAL PRO ILE MET
SEQRES   4 O  265  ALA VAL ASP ASP VAL TYR PHE ILE GLU ASN ASN SER PRO
SEQRES   5 O  265  LEU TYR ASP GLU ILE LEU ALA HIS ARG LEU ALA LEU ILE
SEQRES   6 O  265  PRO PHE MET SER GLU GLU ALA LEU ASP THR TYR ARG TRP
SEQRES   7 O  265  PRO GLU GLU CYS ILE GLU CYS THR GLU ASN CYS GLU LYS
SEQRES   8 O  265  CYS TYR THR LYS ILE TYR ILE GLU ALA GLU ALA PRO ASN
SEQRES   9 O  265  GLU PRO ARG MET ILE TYR SER LYS ASP ILE LYS SER GLU
SEQRES  10 O  265  ASP PRO SER VAL VAL PRO ILE SER GLY ASP ILE PRO ILE
SEQRES  11 O  265  VAL LEU LEU GLY THR ASN GLN LYS ILE SER LEU GLU ALA
SEQRES  12 O  265  ARG LEU ARG LEU GLY TYR GLY LYS GLU HIS ALA LYS PHE
SEQRES  13 O  265  ILE PRO VAL SER LEU SER VAL VAL ARG TYR TYR PRO LYS
SEQRES  14 O  265  VAL GLU ILE LEU ALA ASN CYS GLU LYS ALA VAL ASN VAL
SEQRES  15 O  265  CYS PRO GLU GLY VAL PHE GLU LEU LYS ASP GLY LYS LEU
SEQRES  16 O  265  SER VAL LYS ASN GLU LEU SER CYS THR LEU CYS GLU GLU
SEQRES  17 O  265  CYS LEU ARG TYR CYS ASN GLY SER ILE ARG ILE SER PHE
SEQRES  18 O  265  VAL GLU ASP LYS TYR ILE LEU GLU ILE GLU SER VAL GLY
SEQRES  19 O  265  SER LEU LYS PRO GLU ARG ILE LEU LEU GLU ALA GLY LYS
SEQRES  20 O  265  SER ILE ILE ARG LYS ILE GLU GLU LEU GLU LYS LYS LEU
SEQRES  21 O  265  VAL GLU VAL VAL LYS
SEQRES   1 Q  180  MET TYR LYS LEU ILE LYS ALA ARG SER ILE VAL ARG ILE
SEQRES   2 Q  180  PRO PRO ASN GLU PHE GLY LYS PRO LEU ASN GLU ILE ALA
SEQRES   3 Q  180  LEU ASN GLU LEU ARG GLN GLN TYR GLN GLU LYS ILE LEU
SEQRES   4 Q  180  LYS ASP LEU GLY LEU VAL LEU ALA ILE LEU ASN VAL LYS
SEQRES   5 Q  180  THR SER GLU GLU GLY ILE LEU VAL PHE GLY ASP GLY ALA
SEQRES   6 Q  180  THR TYR HIS GLU VAL GLU PHE ASP MET ILE THR TYR VAL
SEQRES   7 Q  180  PRO VAL VAL GLN GLU VAL VAL GLU GLY GLU VAL LEU GLN
SEQRES   8 Q  180  VAL ASP ASN TYR GLY ILE PHE VAL ASN LEU GLY PRO MET
SEQRES   9 Q  180  ASP GLY LEU VAL HIS ILE SER GLN ILE THR ASP ASP THR
SEQRES  10 Q  180  LEU LYS TYR ASP ASN VAL ARG GLY ILE ILE PHE GLY GLU
SEQRES  11 Q  180  LYS SER LYS LYS VAL ILE GLN LYS GLY ASP LYS VAL ARG
SEQRES  12 Q  180  ALA ARG VAL ILE SER VAL ALA SER THR VAL THR GLY ARG
SEQRES  13 Q  180  LEU PRO ARG ILE ALA LEU THR MET ARG GLN PRO TYR LEU
SEQRES  14 Q  180  GLY LYS LEU GLU TRP ILE THR GLN THR LYS LYS
SEQRES   1 R  113  MET SER SER VAL TYR ILE VAL GLU GLU HIS TYR ILE PRO
SEQRES   2 R  113  TYR SER VAL ALA LYS LYS LEU LEU THR ASP VAL ILE ARG
SEQRES   3 R  113  SER GLY GLY SER SER ASN LEU LEU GLN ARG THR TYR ASP
SEQRES   4 R  113  TYR LEU ASN SER VAL GLU LYS CYS ASP ALA GLU SER ALA
SEQRES   5 R  113  GLN LYS VAL ILE GLU GLU LEU SER ASN ILE VAL SER ARG
SEQRES   6 R  113  GLU ASP VAL ARG ALA ILE LEU ALA SER ILE CYS PRO THR
SEQRES   7 R  113  THR SER ASP GLU VAL ARG SER ILE LEU VAL MET ASP THR
SEQRES   8 R  113  ASN LYS THR TYR THR SER GLU ASP ILE GLN LYS ILE ILE
SEQRES   9 R  113  ASP ILE ILE ARG LYS TYR ILE LYS SER
SEQRES   1 S  132  MET MET GLU SER VAL ALA GLN GLU ILE ILE LEU SER CYS
SEQRES   2 S  132  GLU ILE ASN SER ILE GLU ARG GLY SER LEU LYS ASN LEU
SEQRES   3 S  132  SER MET VAL ASN MET SER CYS ASN GLY PHE ASN VAL SER
SEQRES   4 S  132  PHE ASP ILE ILE ASP SER ILE ASN ILE PHE SER GLN LYS
SEQRES   5 S  132  GLU LYS VAL LYS VAL ILE ILE SER LYS ASN ARG PRO SER
SEQRES   6 S  132  TYR SER HIS ASP ASP PHE CYS GLY HIS GLY TYR ILE VAL
SEQRES   7 S  132  THR GLU LEU LYS ASP SER SER LEU ASN ASN GLY ASN LYS
SEQRES   8 S  132  TYR THR THR ILE ILE SER LEU TYR GLY LEU LEU VAL LYS
SEQRES   9 S  132  ILE ILE SER ASN LYS GLU SER PHE LEU ARG THR SER GLN
SEQRES  10 S  132  LEU ASN ILE MET ASP HIS VAL TYR PHE CYS VAL LYS LYS
SEQRES  11 S  132  ASN ASN
SEQRES   1 T   84  MET ARG GLY SER SER ASN LYS LYS ILE ASP PRO ARG ILE
SEQRES   2 T   84  HIS TYR LEU VAL PRO LYS HIS GLU VAL LEU ASN ILE ASP
SEQRES   3 T   84  GLU ALA TYR LYS ILE LEU LYS GLU LEU GLY ILE ARG PRO
SEQRES   4 T   84  GLU GLN LEU PRO TRP ILE ARG ALA SER ASP PRO VAL ALA
SEQRES   5 T   84  ARG SER ILE ASN ALA LYS PRO GLY ASP ILE ILE ARG ILE
SEQRES   6 T   84  ILE ARG LYS SER GLN LEU TYR GLY GLU VAL VAL SER TYR
SEQRES   7 T   84  ARG TYR VAL ILE SER GLY
SEQRES   1 U   95  MET GLY LEU GLU ARG ASP GLU ILE LEU SER GLN ASP LEU
SEQRES   2 U   95  HIS PHE ASN GLU VAL PHE ILE SER LEU TRP GLN ASN ARG
SEQRES   3 U   95  LEU THR ARG TYR GLU ILE ALA ARG VAL ILE SER ALA ARG
SEQRES   4 U   95  ALA LEU GLN LEU ALA MET GLY ALA PRO ALA LEU ILE ASP
SEQRES   5 U   95  ILE ASN ASN LEU SER SER THR ASP VAL ILE SER ILE ALA
SEQRES   6 U   95  GLU GLU GLU PHE ARG ARG GLY VAL LEU PRO ILE THR ILE
SEQRES   7 U   95  ARG ARG ARG LEU PRO ASN GLY LYS ILE ILE LEU LEU SER
SEQRES   8 U   95  LEU ARG LYS SER
SEQRES   1 V   92  MET GLU ILE ARG ILE LEU LYS SER GLU SER ASN TYR LEU
SEQRES   2 V   92  GLU LEU GLU ILE GLU GLY GLU ASP HIS THR LEU GLY ASN
SEQRES   3 V   92  LEU ILE ALA GLY THR LEU ARG ARG ILE SER GLY VAL SER
SEQRES   4 V   92  PHE ALA SER TYR TYR GLN PRO HIS PRO LEU SER ASP LYS
SEQRES   5 V   92  ILE ILE VAL LYS ILE LEU THR ASP GLY SER ILE THR PRO
SEQRES   6 V   92  LYS ASP ALA LEU LEU LYS ALA ILE GLU ASN ILE ARG GLY
SEQRES   7 V   92  MET THR SER HIS TYR ILE ASP GLU ILE LYS GLY LEU THR
SEQRES   8 V   92  LYS
SEQRES   1 W   66  MET LEU ILE PRO ILE ARG CYS PHE THR CYS GLY SER LEU
SEQRES   2 W   66  ILE ALA ASP LYS TRP GLN SER PHE ILE THR ARG VAL ASN
SEQRES   3 W   66  ALA GLY GLU ASN PRO GLY LYS VAL LEU ASP ASP LEU GLY
SEQRES   4 W   66  VAL LYS ARG TYR CYS CYS ARG ARG MET LEU LEU SER HIS
SEQRES   5 W   66  VAL ASP ILE ILE ASN GLU VAL ILE HIS TYR THR ARG PRO
SEQRES   6 W   66  ILE
SEQRES   1 X   48  MET ALA VAL TYR ARG CYS GLY LYS CYS TRP LYS THR PHE
SEQRES   2 X   48  THR ASP GLU GLN LEU LYS VAL LEU PRO GLY VAL ARG CYS
SEQRES   3 X   48  PRO TYR CYS GLY TYR LYS ILE ILE PHE MET VAL ARG LYS
SEQRES   4 X   48  PRO THR ILE LYS ILE VAL LYS ALA ILE
SEQRES   1 Z  104  MET VAL SER GLY MET SER THR ASP GLU GLU LYS GLU GLY
SEQRES   2 Z  104  THR SER ASP GLU GLU VAL ASN GLU GLU LYS GLU VAL GLU
SEQRES   3 Z  104  GLU THR SER GLU ASP GLU PHE PRO LYS LEU SER ILE GLN
SEQRES   4 Z  104  ASP ILE GLU LEU LEU MET ARG ASN THR GLU ILE TRP ASP
SEQRES   5 Z  104  ASN LEU LEU ASN GLY LYS ILE THR LEU GLU GLU ALA LYS
SEQRES   6 Z  104  LYS LEU PHE GLU ASP ASN TYR LYS GLU TYR GLU LYS ARG
SEQRES   7 Z  104  ASP SER ARG ARG LYS ALA LYS LYS ALA VAL SER LYS LYS
SEQRES   8 Z  104  VAL LYS LYS THR LYS LYS LYS GLU LYS SER VAL GLU GLY
HET     ZN  A1001       1
HET     ZN  A1002       1
HET     MG  A1003       1
HET     ZN  B2001       1
HET    F3S  D1001       7
HET     ZN  N1001       1
HET     ZN  P1001       1
HET     ZN  I1001       1
HET     ZN  I1002       1
HET     MG  I1003       1
HET     ZN  J2001       1
HET    F3S  O1001       7
HET     ZN  W1001       1
HET     ZN  X1001       1
HETNAM      ZN ZINC ION
HETNAM      MG MAGNESIUM ION
HETNAM     F3S FE3-S4 CLUSTER
FORMUL  27   ZN    10(ZN 2+)
FORMUL  29   MG    2(MG 2+)
FORMUL  31  F3S    2(FE3 S4)
HELIX    1   1 SER A   15  SER A   23  1                                   9
HELIX    2   2 LEU A   86  LEU A   94  1                                   9
HELIX    3   3 LYS A  113  TYR A  118  1                                   6
HELIX    4   4 LYS A  123  THR A  139  1                                  17
HELIX    5   5 THR A  176  LYS A  186  1                                  11
HELIX    6   6 PRO A  188  TYR A  197  1                                  10
HELIX    7   7 PRO A  216  ARG A  220  5                                   5
HELIX    8   8 ASP A  233  ARG A  248  1                                  16
HELIX    9   9 ILE A  261  LEU A  265  5                                   5
HELIX   10  10 TRP A  266  GLN A  270  5                                   5
HELIX   11  11 HIS A  272  ASP A  278  1                                   7
HELIX   12  12 GLU A  341  LEU A  347  1                                   7
HELIX   13  13 ASN A  357  GLY A  368  1                                  12
HELIX   14  14 HIS A  426  ILE A  428  5                                   3
HELIX   15  15 ASN A  446  LEU A  448  5                                   3
HELIX   16  16 VAL A  449  ASN A  454  1                                   6
HELIX   17  17 SER A  469  LEU A  481  1                                  13
HELIX   18  18 VAL A  482  ILE A  486  5                                   5
HELIX   19  19 GLN A  500  THR A  510  1                                  11
HELIX   20  20 THR A  517  ILE A  524  1                                   8
HELIX   21  21 THR A  547  ALA A  554  1                                   8
HELIX   22  22 SER A  570  LEU A  574  5                                   5
HELIX   23  23 ASP A  599  GLY A  604  1                                   6
HELIX   24  24 SER A  610  GLU A  618  1                                   9
HELIX   25  25 GLU A  622  LEU A  631  1                                  10
HELIX   26  26 LEU A  631  GLU A  640  1                                  10
HELIX   27  27 GLY A  654  ASN A  681  1                                  28
HELIX   28  28 THR A  691  LEU A  707  1                                  17
HELIX   29  29 ARG A  708  LEU A  719  1                                  12
HELIX   30  30 ASN A  723  ALA A  729  1                                   7
HELIX   31  31 SER A  736  ALA A  745  1                                  10
HELIX   32  32 THR A  793  GLY A  802  1                                  10
HELIX   33  33 GLU A  804  THR A  809  1                                   6
HELIX   34  34 ARG A  812  LEU A  827  1                                  16
HELIX   35  35 ALA A  849  ASP A  853  5                                   5
HELIX   36  36 PHE A  856  SER A  860  5                                   5
HELIX   37  37 VAL A  866  VAL A  875  1                                  10
HELIX   38  38 GLU C   15  ALA C   20  1                                   6
HELIX   39  39 ILE C   23  LYS C   27  5                                   5
HELIX   40  40 ASP C   31  ILE C   41  1                                  11
HELIX   41  41 ASP C   49  TYR C   59  1                                  11
HELIX   42  42 ALA C   69  VAL C   78  1                                  10
HELIX   43  43 GLY C   79  THR C   83  5                                   5
HELIX   44  44 LEU C  104  ASP C  112  1                                   9
HELIX   45  45 ARG C  134  GLU C  139  1                                   6
HELIX   46  46 GLU C  139  LEU C  144  1                                   6
HELIX   47  47 LYS C  148  VAL C  152  5                                   5
HELIX   48  48 ASN C  171  LYS C  177  1                                   7
HELIX   49  49 ALA C  218  LEU C  222  5                                   5
HELIX   50  50 ARG C  223  ASN C  228  1                                   6
HELIX   51  51 GLU C  279  GLY C  285  1                                   7
HELIX   52  52 GLY C  285  GLU C  296  1                                  12
HELIX   53  53 ASP C  309  ASP C  318  1                                  10
HELIX   54  54 SER C  340  ALA C  346  1                                   7
HELIX   55  55 THR C  350  ARG C  360  1                                  11
HELIX   56  56 GLY C  368  ILE C  375  1                                   8
HELIX   57  57 ILE B    7  LYS B   21  1                                  15
HELIX   58  58 HIS B   27  ARG B   36  1                                  10
HELIX   59  59 SER B   81  ARG B   86  1                                   6
HELIX   60  60 ASP B  128  TYR B  133  5                                   6
HELIX   61  61 THR B  134  GLY B  142  1                                   9
HELIX   62  62 PHE B  223  LEU B  230  1                                   8
HELIX   63  63 THR B  234  SER B  243  1                                  10
HELIX   64  64 GLN B  249  PHE B  253  5                                   5
HELIX   65  65 PRO B  254  ALA B  259  5                                   6
HELIX   66  66 ASP B  266  ALA B  268  5                                   3
HELIX   67  67 LEU B  269  SER B  274  1                                   6
HELIX   68  68 GLU B  283  LYS B  295  1                                  13
HELIX   69  69 ARG B  308  ILE B  323  1                                  16
HELIX   70  70 LEU B  345  LYS B  373  1                                  29
HELIX   71  71 ALA B  380  LEU B  384  5                                   5
HELIX   72  72 THR B  391  HIS B  396  1                                   6
HELIX   73  73 ASN B  418  ARG B  428  1                                  11
HELIX   74  74 GLU B  482  LYS B  487  1                                   6
HELIX   75  75 LEU B  489  GLY B  493  5                                   5
HELIX   76  76 ASP B  532  LYS B  546  1                                  15
HELIX   77  77 VAL B  589  LYS B  596  1                                   8
HELIX   78  78 THR B  603  GLN B  610  1                                   8
HELIX   79  79 GLU B  629  LEU B  633  5                                   5
HELIX   80  80 TRP B  643  LEU B  648  5                                   6
HELIX   81  81 GLY B  649  ILE B  654  1                                   6
HELIX   82  82 GLN B  662  ALA B  673  1                                  12
HELIX   83  83 LYS B  674  ALA B  676  5                                   3
HELIX   84  84 GLY B  712  ARG B  716  5                                   5
HELIX   85  85 ARG B  742  ARG B  747  1                                   6
HELIX   86  86 TYR B  788  LEU B  792  5                                   5
HELIX   87  87 HIS B  913  MET B  919  1                                   7
HELIX   88  88 GLY B  922  LEU B  935  1                                  14
HELIX   89  89 ILE B  950  TYR B  960  1                                  11
HELIX   90  90 GLY B 1019  GLU B 1023  5                                   5
HELIX   91  91 GLY B 1029  GLU B 1032  5                                   4
HELIX   92  92 ARG B 1033  PHE B 1039  1                                   7
HELIX   93  93 LEU B 1045  LEU B 1050  1                                   6
HELIX   94  94 LYS B 1072  LYS B 1076  5                                   5
HELIX   95  95 SER B 1094  MET B 1107  1                                  14
HELIX   96  96 PRO D   21  LEU D   34  1                                  14
HELIX   97  97 TYR D   54  LEU D   64  1                                  11
HELIX   98  98 MET D   68  TYR D   76  1                                   9
HELIX   99  99 LYS D  112  ILE D  114  5                                   3
HELIX  100 100 TYR D  149  ALA D  154  1                                   6
HELIX  101 101 LYS D  178  CYS D  183  1                                   6
HELIX  102 102 CYS D  209  ASN D  214  1                                   6
HELIX  103 103 LYS D  237  GLU D  262  1                                  26
HELIX  104 104 PRO E   15  GLY E   19  5                                   5
HELIX  105 105 PRO E   21  GLN E   35  1                                  15
HELIX  106 106 LYS E  171  ILE E  175  5                                   5
HELIX  107 107 PRO F   13  THR F   22  1                                  10
HELIX  108 108 ASP F   23  SER F   27  5                                   5
HELIX  109 109 GLN F   35  LEU F   41  1                                   7
HELIX  110 110 ASP F   48  GLU F   58  1                                  11
HELIX  111 111 GLU F   66  ILE F   71  1                                   6
HELIX  112 112 ILE F   71  CYS F   76  1                                   6
HELIX  113 113 VAL F   83  LEU F   87  5                                   5
HELIX  114 114 GLU H   27  GLU H   34  1                                   8
HELIX  115 115 LEU K   13  TRP K   23  1                                  11
HELIX  116 116 THR K   28  GLY K   46  1                                  19
HELIX  117 117 SER K   63  ARG K   71  1                                   9
HELIX  118 118 ASP L   21  ARG L   33  1                                  13
HELIX  119 119 THR L   64  LYS L   88  1                                  25
HELIX  120 120 ILE N   14  GLN N   19  5                                   6
HELIX  121 121 SER N   20  ALA N   27  1                                   8
HELIX  122 122 ASN N   30  LEU N   38  1                                   9
HELIX  123 123 TYR N   43  SER N   51  1                                   9
HELIX  124 124 ILE N   55  ILE N   60  1                                   6
HELIX  125 125 GLU Y   42  LEU Y   54  1                                  13
HELIX  126 126 ILE Y   59  LYS Y   73  1                                  15
HELIX  127 127 SER I   15  SER I   23  1                                   9
HELIX  128 128 LEU I   86  LEU I   94  1                                   9
HELIX  129 129 LYS I  113  TYR I  118  1                                   6
HELIX  130 130 LYS I  123  THR I  139  1                                  17
HELIX  131 131 THR I  176  LYS I  186  1                                  11
HELIX  132 132 PRO I  188  TYR I  197  1                                  10
HELIX  133 133 PRO I  216  ARG I  220  5                                   5
HELIX  134 134 ASP I  233  ARG I  248  1                                  16
HELIX  135 135 ILE I  261  LEU I  265  5                                   5
HELIX  136 136 TRP I  266  GLN I  270  5                                   5
HELIX  137 137 HIS I  272  ASP I  278  1                                   7
HELIX  138 138 GLU I  341  LEU I  347  1                                   7
HELIX  139 139 ASN I  357  GLY I  368  1                                  12
HELIX  140 140 HIS I  426  ILE I  428  5                                   3
HELIX  141 141 ASN I  446  LEU I  448  5                                   3
HELIX  142 142 VAL I  449  ASN I  454  1                                   6
HELIX  143 143 SER I  469  LEU I  481  1                                  13
HELIX  144 144 VAL I  482  ILE I  486  5                                   5
HELIX  145 145 GLN I  500  THR I  510  1                                  11
HELIX  146 146 THR I  517  ILE I  524  1                                   8
HELIX  147 147 THR I  547  ALA I  554  1                                   8
HELIX  148 148 SER I  570  LEU I  574  5                                   5
HELIX  149 149 ASP I  599  GLY I  604  1                                   6
HELIX  150 150 SER I  610  GLU I  618  1                                   9
HELIX  151 151 GLU I  622  LEU I  631  1                                  10
HELIX  152 152 LEU I  631  GLU I  640  1                                  10
HELIX  153 153 GLY I  654  ASN I  681  1                                  28
HELIX  154 154 THR I  691  LEU I  707  1                                  17
HELIX  155 155 ARG I  708  LEU I  719  1                                  12
HELIX  156 156 ASN I  723  ALA I  729  1                                   7
HELIX  157 157 SER I  736  ALA I  745  1                                  10
HELIX  158 158 THR I  793  GLY I  802  1                                  10
HELIX  159 159 GLU I  804  THR I  809  1                                   6
HELIX  160 160 ARG I  812  LEU I  827  1                                  16
HELIX  161 161 PHE I  856  SER I  860  5                                   5
HELIX  162 162 VAL I  866  VAL I  875  1                                  10
HELIX  163 163 LEU M   13  ALA M   20  1                                   8
HELIX  164 164 ILE M   23  LYS M   27  5                                   5
HELIX  165 165 ASP M   31  ILE M   41  1                                  11
HELIX  166 166 ASP M   49  GLU M   61  1                                  13
HELIX  167 167 ALA M   69  THR M   83  1                                  15
HELIX  168 168 LEU M  104  ASP M  112  1                                   9
HELIX  169 169 ARG M  134  ARG M  142  1                                   9
HELIX  170 170 LYS M  148  ASN M  151  5                                   4
HELIX  171 171 ARG M  223  ASN M  228  1                                   6
HELIX  172 172 ASN M  257  SER M  263  1                                   7
HELIX  173 173 GLU M  279  GLY M  285  1                                   7
HELIX  174 174 GLY M  285  GLU M  303  1                                  19
HELIX  175 175 ASP M  309  THR M  321  1                                  13
HELIX  176 176 VAL M  341  PHE M  347  1                                   7
HELIX  177 177 THR M  350  ARG M  360  1                                  11
HELIX  178 178 GLY M  368  GLY M  376  1                                   9
HELIX  179 179 LEU M  381  MET M  385  5                                   5
HELIX  180 180 ILE J    7  LYS J   21  1                                  15
HELIX  181 181 HIS J   27  ARG J   36  1                                  10
HELIX  182 182 SER J   81  ARG J   86  1                                   6
HELIX  183 183 ASP J  128  TYR J  133  5                                   6
HELIX  184 184 THR J  134  GLY J  142  1                                   9
HELIX  185 185 PHE J  223  LEU J  230  1                                   8
HELIX  186 186 THR J  234  SER J  243  1                                  10
HELIX  187 187 GLN J  249  PHE J  253  5                                   5
HELIX  188 188 PRO J  254  ALA J  259  5                                   6
HELIX  189 189 ASP J  266  ALA J  268  5                                   3
HELIX  190 190 LEU J  269  SER J  274  1                                   6
HELIX  191 191 GLU J  283  LYS J  295  1                                  13
HELIX  192 192 ARG J  308  ILE J  323  1                                  16
HELIX  193 193 LEU J  345  LYS J  373  1                                  29
HELIX  194 194 ALA J  380  LEU J  384  5                                   5
HELIX  195 195 THR J  391  HIS J  396  1                                   6
HELIX  196 196 ASN J  418  ARG J  427  1                                  10
HELIX  197 197 GLU J  482  LYS J  487  1                                   6
HELIX  198 198 LEU J  489  GLY J  493  5                                   5
HELIX  199 199 ASP J  532  LYS J  546  1                                  15
HELIX  200 200 VAL J  589  LYS J  596  1                                   8
HELIX  201 201 THR J  603  GLN J  610  1                                   8
HELIX  202 202 GLU J  629  LEU J  633  5                                   5
HELIX  203 203 TRP J  643  LEU J  648  5                                   6
HELIX  204 204 GLY J  649  ILE J  654  1                                   6
HELIX  205 205 GLN J  662  ALA J  673  1                                  12
HELIX  206 206 LYS J  674  ALA J  676  5                                   3
HELIX  207 207 GLY J  712  ARG J  716  5                                   5
HELIX  208 208 ASN J  741  ARG J  747  1                                   7
HELIX  209 209 TYR J  788  LEU J  792  5                                   5
HELIX  210 210 ALA J  914  MET J  919  1                                   6
HELIX  211 211 GLY J  922  LEU J  935  1                                  14
HELIX  212 212 ILE J  950  GLY J  961  1                                  12
HELIX  213 213 GLY J 1019  GLU J 1023  5                                   5
HELIX  214 214 ARG J 1033  PHE J 1039  1                                   7
HELIX  215 215 LEU J 1045  LEU J 1050  1                                   6
HELIX  216 216 LYS J 1072  LYS J 1076  5                                   5
HELIX  217 217 SER J 1094  MET J 1107  1                                  14
HELIX  218 218 PRO O   21  LEU O   34  1                                  14
HELIX  219 219 TYR O   54  LEU O   64  1                                  11
HELIX  220 220 MET O   68  TYR O   76  1                                   9
HELIX  221 221 LYS O  112  ILE O  114  5                                   3
HELIX  222 222 TYR O  149  ALA O  154  1                                   6
HELIX  223 223 LYS O  178  CYS O  183  1                                   6
HELIX  224 224 CYS O  209  ASN O  214  1                                   6
HELIX  225 225 LYS O  237  GLU O  262  1                                  26
HELIX  226 226 PRO Q   14  PHE Q   18  5                                   5
HELIX  227 227 PRO Q   21  GLN Q   35  1                                  15
HELIX  228 228 GLU Q  173  ILE Q  175  5                                   3
HELIX  229 229 ASP R   23  GLY R   28  1                                   6
HELIX  230 230 SER R   31  LEU R   41  1                                  11
HELIX  231 231 SER R   51  GLU R   58  1                                   8
HELIX  232 232 ARG R   65  ILE R   71  1                                   7
HELIX  233 233 ILE R   71  CYS R   76  1                                   6
HELIX  234 234 SER R   80  SER R   85  1                                   6
HELIX  235 235 ASN T   24  TYR T   29  1                                   6
HELIX  236 236 LYS T   30  LEU T   35  1                                   6
HELIX  237 237 ASP T   49  ILE T   55  1                                   7
HELIX  238 238 LEU U   13  TRP U   23  1                                  11
HELIX  239 239 THR U   28  MET U   45  1                                  18
HELIX  240 240 ALA U   65  ARG U   71  1                                   7
HELIX  241 241 ASP V   21  ILE V   35  1                                  15
HELIX  242 242 THR V   64  GLU V   86  1                                  23
HELIX  243 243 ILE W   14  GLN W   19  5                                   6
HELIX  244 244 SER W   20  ALA W   27  1                                   8
HELIX  245 245 ASN W   30  LEU W   38  1                                   9
HELIX  246 246 TYR W   43  SER W   51  1                                   9
HELIX  247 247 ILE W   55  ILE W   60  1                                   6
HELIX  248 248 GLU Z   42  LEU Z   54  1                                  13
HELIX  249 249 GLU Z   63  TYR Z   72  1                                  10
SHEET    1   A 2 ILE A   9  LYS A  10  0
SHEET    2   A 2 ARG B1112  LEU B1113 -1  O  ARG B1112   N  LYS A  10
SHEET    1   B 2 VAL A  81  ILE A  82  0
SHEET    2   B 2 ILE A 208  LEU A 209 -1  O  LEU A 209   N  VAL A  81
SHEET    1   C 2 LYS A 316  ARG A 317  0
SHEET    2   C 2 ARG B1027  PHE B1028 -1  O  PHE B1028   N  LYS A 316
SHEET    1   D 7 SER A 321  PRO A 328  0
SHEET    2   D 7 PHE A 443  LEU A 445  1  O  PHE A 443   N  VAL A 325
SHEET    3   D 7 VAL A 337  PRO A 340 -1  N  GLY A 338   O  ARG A 444
SHEET    4   D 7 MET A 430  LEU A 438  1  O  ARG A 436   N  VAL A 337
SHEET    5   D 7 ILE A 416  ASN A 420 -1  N  VAL A 417   O  HIS A 433
SHEET    6   D 7 GLU A 461  HIS A 465 -1  O  ASN A 463   N  ASN A 420
SHEET    7   D 7 SER A 321  PRO A 328 -1  N  SER A 322   O  LEU A 464
SHEET    1   E 2 VAL A 349  ARG A 352  0
SHEET    2   E 2 ILE A 406  ARG A 409 -1  O  ARG A 409   N  VAL A 349
SHEET    1   F 2 PHE A 562  GLY A 564  0
SHEET    2   F 2 VAL A 586  ILE A 588 -1  O  VAL A 586   N  GLY A 564
SHEET    1   G 2 ARG A 831  ALA A 832  0
SHEET    2   G 2 VAL A 838  ARG A 839 -1  O  ARG A 839   N  ARG A 831
SHEET    1   H 2 SER C 155  ILE C 158  0
SHEET    2   H 2 ILE C 165  GLN C 168 -1  O  ILE C 166   N  SER C 157
SHEET    1   I 2 GLU C 199  GLU C 200  0
SHEET    2   I 2 THR C 205  LEU C 206 -1  O  LEU C 206   N  GLU C 199
SHEET    1   J 2 ILE C 241  GLN C 243  0
SHEET    2   J 2 ILE C 250  LEU C 252 -1  O  ILE C 250   N  GLN C 243
SHEET    1   K 3 GLU C 387  THR C 389  0
SHEET    2   K 3 THR K  77  ARG K  81 -1  O  THR K  77   N  THR C 389
SHEET    3   K 3 ILE K  87  ILE K  88 -1  O  ILE K  88   N  ARG K  80
SHEET    1   L 2 LEU B  56  LEU B  60  0
SHEET    2   L 2 MET B 100  GLU B 104 -1  O  ILE B 101   N  ARG B  59
SHEET    1   M 2 ARG B  69  VAL B  70  0
SHEET    2   M 2 ARG B  78  GLU B  79 -1  O  ARG B  78   N  VAL B  70
SHEET    1   N 2 ALA B  93  PRO B  95  0
SHEET    2   N 2 ASP B 118  PRO B 120 -1  O  LEU B 119   N  ALA B  94
SHEET    1   O 2 ARG B 159  ILE B 161  0
SHEET    2   O 2 SER B 411  LEU B 413 -1  O  GLN B 412   N  VAL B 160
SHEET    1   P 2 GLN B 164  GLU B 165  0
SHEET    2   P 2 LEU B 343  ARG B 344 -1  O  ARG B 344   N  GLN B 164
SHEET    1   Q 5 ASN B 170  ASP B 175  0
SHEET    2   Q 5 THR B 186  SER B 191 -1  O  ILE B 190   N  ASN B 170
SHEET    3   Q 5 THR B 201  LYS B 206 -1  O  LEU B 205   N  ALA B 187
SHEET    4   Q 5 HIS B 211  SER B 213 -1  O  SER B 213   N  ARG B 204
SHEET    5   Q 5 LYS B 220  PRO B 222 -1  O  ILE B 221   N  VAL B 212
SHEET    1   R 5 VAL B 495  PRO B 496  0
SHEET    2   R 5 LEU B 526  TYR B 529 -1  O  TYR B 529   N  VAL B 495
SHEET    3   R 5 VAL B 520  LEU B 522 -1  N  VAL B 520   O  GLY B 528
SHEET    4   R 5 VAL B 566  ASN B 569  1  O  VAL B 566   N  ILE B 521
SHEET    5   R 5 ASN B 554  HIS B 557 -1  N  ASN B 554   O  ASN B 569
SHEET    1   S 2 ARG B 577  ILE B 580  0
SHEET    2   S 2 ILE B 613  LEU B 616 -1  O  LEU B 616   N  ARG B 577
SHEET    1   T 5 ALA B 692  LEU B 695  0
SHEET    2   T 5 SER B 752  THR B 760 -1  O  PHE B 755   N  ALA B 692
SHEET    3   T 5 LYS B 860  ARG B 867 -1  O  VAL B 864   N  TYR B 758
SHEET    4   T 5 MET B 844  GLU B 854 -1  N  LEU B 849   O  ARG B 865
SHEET    5   T 5 GLU B 803  LYS B 805 -1  N  VAL B 804   O  GLY B 845
SHEET    1   U 3 ALA B 692  LEU B 695  0
SHEET    2   U 3 SER B 752  THR B 760 -1  O  PHE B 755   N  ALA B 692
SHEET    3   U 3 LEU B 869  ARG B 870 -1  O  ARG B 870   N  SER B 752
SHEET    1   V 3 GLY B 719  ILE B 723  0
SHEET    2   V 3 VAL B 987  LYS B 992 -1  O  TYR B 990   N  ASN B 720
SHEET    3   V 3 PHE B 878  SER B 880 -1  N  ALA B 879   O  GLN B 991
SHEET    1   W 3 ILE B 888  ILE B 892  0
SHEET    2   W 3 ILE B 738  ASN B 741  1  N  ILE B 738   O  GLY B 889
SHEET    3   W 3 ILE B 908  LEU B 910 -1  O  ILE B 909   N  ILE B 739
SHEET    1   X 2 VAL B 809  ILE B 811  0
SHEET    2   X 2 ILE B 837  VAL B 838 -1  O  ILE B 837   N  ILE B 811
SHEET    1   Y 2 PRO B 898  THR B 900  0
SHEET    2   Y 2 VAL B 970  ASP B 972 -1  O  TYR B 971   N  TYR B 899
SHEET    1   Z 2 THR B 967  GLU B 968  0
SHEET    2   Z 2 ILE B 983  TYR B 984 -1  O  ILE B 983   N  GLU B 968
SHEET    1  AA 2 MET B1057  CYS B1061  0
SHEET    2  AA 2 LEU B1088  THR B1092 -1  O  VAL B1091   N  ILE B1058
SHEET    1  AB 4 ASN D   4  LYS D   8  0
SHEET    2  AB 4 ILE D  13  GLU D  18 -1  O  ASP D  14   N  LEU D   6
SHEET    3  AB 4 ILE D 219  SER D 232 -1  O  ILE D 230   N  ILE D  13
SHEET    4  AB 4 VAL D 159  VAL D 170 -1  N  LYS D 169   O  SER D 220
SHEET    1  AC 2 ILE D  38  VAL D  41  0
SHEET    2  AC 2 LEU D 145  GLY D 148 -1  O  ARG D 146   N  ALA D  40
SHEET    1  AD 4 TYR D  97  ILE D  98  0
SHEET    2  AD 4 ILE D 139  GLU D 142 -1  O  LEU D 141   N  ILE D  98
SHEET    3  AD 4 ASP D  43  ASN D  49 -1  N  TYR D  45   O  GLU D 142
SHEET    4  AD 4 LYS P  43  LYS P  46 -1  O  VAL P  45   N  VAL D  44
SHEET    1  AE 2 PRO D 106  TYR D 110  0
SHEET    2  AE 2 PRO D 129  GLY D 134 -1  O  LEU D 133   N  ARG D 107
SHEET    1  AF 3 LEU E  44  ILE E  48  0
SHEET    2  AF 3 THR E  66  TYR E  77 -1  O  TYR E  77   N  LEU E  44
SHEET    3  AF 3 GLU E  55  ILE E  58 -1  N  ILE E  58   O  TYR E  67
SHEET    1  AG 4 LEU E  44  ILE E  48  0
SHEET    2  AG 4 THR E  66  TYR E  77 -1  O  TYR E  77   N  LEU E  44
SHEET    3  AG 4 TYR E   2  ILE E  13 -1  N  ILE E  13   O  THR E  66
SHEET    4  AG 4 TYR F   5  ILE F  12 -1  O  GLU F   8   N  LYS E   6
SHEET    1  AH 6 VAL E  84  VAL E  85  0
SHEET    2  AH 6 ALA E 144  VAL E 146 -1  O  ALA E 144   N  VAL E  85
SHEET    3  AH 6 ILE E 160  THR E 163 -1  O  THR E 163   N  ARG E 145
SHEET    4  AH 6 ASP E 105  HIS E 109  1  N  LEU E 107   O  LEU E 162
SHEET    5  AH 6 GLY E  96  ASN E 100 -1  N  ILE E  97   O  VAL E 108
SHEET    6  AH 6 VAL E  89  ASP E  93 -1  N  ASP E  93   O  GLY E  96
SHEET    1  AI 7 ILE G  10  GLU G  14  0
SHEET    2  AI 7 LYS G  54  SER G  60 -1  O  VAL G  57   N  LEU G  11
SHEET    3  AI 7 SER G 111  SER G 116 -1  O  PHE G 112   N  SER G  60
SHEET    4  AI 7 PHE G  71  THR G  79 -1  N  GLY G  75   O  SER G 111
SHEET    5  AI 7 ASP G  83  LEU G  86 -1  O  LEU G  86   N  TYR G  76
SHEET    6  AI 7 LYS G  91  ILE G  95 -1  O  THR G  94   N  ASP G  83
SHEET    7  AI 7 ASN G  37  SER G  39 -1  N  SER G  39   O  THR G  93
SHEET    1  AJ 2 ARG H  64  ARG H  67  0
SHEET    2  AJ 2 VAL H  75  TYR H  78 -1  O  VAL H  75   N  ARG H  67
SHEET    1  AK 4 ARG L   4  GLU L   9  0
SHEET    2  AK 4 TYR L  12  GLU L  18 -1  O  GLU L  14   N  LEU L   6
SHEET    3  AK 4 LYS L  52  LEU L  58 -1  O  ILE L  57   N  LEU L  13
SHEET    4  AK 4 PHE L  40  TYR L  44 -1  N  PHE L  40   O  LEU L  58
SHEET    1  AL 2 GLY P   7  LYS P   8  0
SHEET    2  AL 2 PHE P  35  MET P  36 -1  O  PHE P  35   N  LYS P   8
SHEET    1  AM 2 ILE I   9  LYS I  10  0
SHEET    2  AM 2 ARG J1112  LEU J1113 -1  O  ARG J1112   N  LYS I  10
SHEET    1  AN 2 VAL I  81  ILE I  82  0
SHEET    2  AN 2 ILE I 208  LEU I 209 -1  O  LEU I 209   N  VAL I  81
SHEET    1  AO 2 LYS I 316  ARG I 317  0
SHEET    2  AO 2 ARG J1027  PHE J1028 -1  O  PHE J1028   N  LYS I 316
SHEET    1  AP 7 SER I 321  PRO I 328  0
SHEET    2  AP 7 PHE I 443  LEU I 445  1  O  PHE I 443   N  SER I 327
SHEET    3  AP 7 VAL I 337  PRO I 340 -1  N  GLY I 338   O  ARG I 444
SHEET    4  AP 7 MET I 430  LEU I 438  1  O  LEU I 438   N  VAL I 339
SHEET    5  AP 7 ILE I 416  ASN I 420 -1  N  VAL I 417   O  HIS I 433
SHEET    6  AP 7 GLU I 461  HIS I 465 -1  O  ASN I 463   N  ASN I 420
SHEET    7  AP 7 SER I 321  PRO I 328 -1  N  SER I 322   O  LEU I 464
SHEET    1  AQ 2 VAL I 349  ARG I 352  0
SHEET    2  AQ 2 ILE I 406  ARG I 409 -1  N  ARG I 409   O  VAL I 349
SHEET    1  AR 2 PHE I 562  GLY I 564  0
SHEET    2  AR 2 VAL I 586  ILE I 588 -1  O  VAL I 586   N  GLY I 564
SHEET    1  AS 2 ARG I 831  ALA I 832  0
SHEET    2  AS 2 VAL I 838  ARG I 839 -1  O  ARG I 839   N  ARG I 831
SHEET    1  AT 4 ALA M 240  GLN M 243  0
SHEET    2  AT 4 ILE M 250  THR M 253 -1  O  ILE M 250   N  GLN M 243
SHEET    3  AT 4 THR M 123  LEU M 126 -1  N  ILE M 124   O  ILE M 251
SHEET    4  AT 4 VAL M 267  GLU M 273 -1  O  GLU M 273   N  THR M 123
SHEET    1  AU 2 VAL M 153  ASP M 159  0
SHEET    2  AU 2 SER M 164  LEU M 169 -1  O  SER M 164   N  ASP M 159
SHEET    1  AV 2 MET M 197  ILE M 198  0
SHEET    2  AV 2 ASN M 207  ILE M 208 -1  O  ILE M 208   N  MET M 197
SHEET    1  AW 3 GLU M 387  THR M 389  0
SHEET    2  AW 3 THR U  77  ARG U  81 -1  O  THR U  77   N  THR M 389
SHEET    3  AW 3 ILE U  87  LEU U  90 -1  O  ILE U  88   N  ARG U  80
SHEET    1  AX 2 LEU J  56  LEU J  60  0
SHEET    2  AX 2 MET J 100  GLU J 104 -1  O  ILE J 101   N  ARG J  59
SHEET    1  AY 2 ARG J  69  VAL J  70  0
SHEET    2  AY 2 ARG J  78  GLU J  79 -1  O  ARG J  78   N  VAL J  70
SHEET    1  AZ 2 ALA J  93  PRO J  95  0
SHEET    2  AZ 2 ASP J 118  PRO J 120 -1  O  LEU J 119   N  ALA J  94
SHEET    1  BA 2 ARG J 159  ILE J 161  0
SHEET    2  BA 2 SER J 411  LEU J 413 -1  O  GLN J 412   N  VAL J 160
SHEET    1  BB 2 GLN J 164  GLU J 165  0
SHEET    2  BB 2 LEU J 343  ARG J 344 -1  O  ARG J 344   N  GLN J 164
SHEET    1  BC 5 ASN J 170  ASP J 175  0
SHEET    2  BC 5 THR J 186  SER J 191 -1  O  ILE J 190   N  ASN J 170
SHEET    3  BC 5 THR J 201  LYS J 206 -1  O  LEU J 205   N  ALA J 187
SHEET    4  BC 5 HIS J 211  SER J 213 -1  O  SER J 213   N  ARG J 204
SHEET    5  BC 5 LYS J 220  PRO J 222 -1  O  ILE J 221   N  VAL J 212
SHEET    1  BD 2 ARG J 428  VAL J 429  0
SHEET    2  BD 2 LYS J 468  ASN J 469 -1  O  LYS J 468   N  VAL J 429
SHEET    1  BE 2 VAL J 495  PRO J 496  0
SHEET    2  BE 2 GLY J 528  TYR J 529 -1  O  TYR J 529   N  VAL J 495
SHEET    1  BF 3 VAL J 520  LEU J 522  0
SHEET    2  BF 3 VAL J 566  ASN J 569  1  O  VAL J 566   N  ILE J 521
SHEET    3  BF 3 ASN J 554  HIS J 557 -1  N  ASN J 554   O  ASN J 569
SHEET    1  BG 2 ARG J 577  ILE J 580  0
SHEET    2  BG 2 ILE J 613  LEU J 616 -1  O  LEU J 616   N  ARG J 577
SHEET    1  BH 5 ALA J 692  HIS J 693  0
SHEET    2  BH 5 SER J 752  THR J 760 -1  O  PHE J 755   N  ALA J 692
SHEET    3  BH 5 LYS J 860  ARG J 870 -1  O  VAL J 864   N  TYR J 758
SHEET    4  BH 5 MET J 844  GLU J 854 -1  N  LEU J 849   O  ARG J 865
SHEET    5  BH 5 GLU J 803  LYS J 805 -1  N  VAL J 804   O  GLY J 845
SHEET    1  BI 3 GLY J 719  ILE J 723  0
SHEET    2  BI 3 VAL J 987  LYS J 992 -1  O  TYR J 990   N  ASN J 720
SHEET    3  BI 3 PHE J 878  SER J 880 -1  N  ALA J 879   O  GLN J 991
SHEET    1  BJ 2 ILE J 738  MET J 740  0
SHEET    2  BJ 2 ILE J 908  LEU J 910 -1  O  ILE J 909   N  ILE J 739
SHEET    1  BK 2 PRO J 898  THR J 900  0
SHEET    2  BK 2 VAL J 970  ASP J 972 -1  O  TYR J 971   N  TYR J 899
SHEET    1  BL 2 THR J 967  GLU J 968  0
SHEET    2  BL 2 ILE J 983  TYR J 984 -1  O  ILE J 983   N  GLU J 968
SHEET    1  BM 2 MET J1057  CYS J1061  0
SHEET    2  BM 2 LEU J1088  THR J1092 -1  O  VAL J1091   N  ILE J1058
SHEET    1  BN 4 ASN O   4  LYS O   8  0
SHEET    2  BN 4 ILE O  13  GLU O  18 -1  O  ASP O  14   N  LEU O   6
SHEET    3  BN 4 ILE O 219  SER O 232 -1  O  ILE O 230   N  ILE O  13
SHEET    4  BN 4 VAL O 159  VAL O 170 -1  N  LYS O 169   O  SER O 220
SHEET    1  BO 2 ILE O  38  VAL O  41  0
SHEET    2  BO 2 LEU O 145  GLY O 148 -1  O  ARG O 146   N  ALA O  40
SHEET    1  BP 4 TYR O  97  ILE O  98  0
SHEET    2  BP 4 ILE O 139  GLU O 142 -1  O  LEU O 141   N  ILE O  98
SHEET    3  BP 4 ASP O  43  ASN O  49 -1  N  TYR O  45   O  GLU O 142
SHEET    4  BP 4 LYS X  43  LYS X  46 -1  O  LYS X  43   N  PHE O  46
SHEET    1  BQ 2 PRO O 106  TYR O 110  0
SHEET    2  BQ 2 PRO O 129  GLY O 134 -1  O  LEU O 133   N  ARG O 107
SHEET    1  BR 4 LEU Q  44  ILE Q  48  0
SHEET    2  BR 4 TYR Q  67  TYR Q  77 -1  O  TYR Q  77   N  LEU Q  44
SHEET    3  BR 4 TYR Q   2  ARG Q  12 -1  N  ILE Q   5   O  MET Q  74
SHEET    4  BR 4 TYR R   5  ILE R  12 -1  O  ILE R  12   N  TYR Q   2
SHEET    1  BS 6 VAL Q  84  GLU Q  86  0
SHEET    2  BS 6 VAL Q 142  VAL Q 146 -1  O  ALA Q 144   N  VAL Q  85
SHEET    3  BS 6 ILE Q 160  THR Q 163 -1  O  THR Q 163   N  ARG Q 145
SHEET    4  BS 6 ASP Q 105  HIS Q 109  1  N  LEU Q 107   O  LEU Q 162
SHEET    5  BS 6 GLY Q  96  ASN Q 100 -1  N  VAL Q  99   O  GLY Q 106
SHEET    6  BS 6 GLU Q  88  VAL Q  92 -1  N  GLN Q  91   O  PHE Q  98
SHEET    1  BT 3 VAL Q  84  GLU Q  86  0
SHEET    2  BT 3 VAL Q 142  VAL Q 146 -1  O  ALA Q 144   N  VAL Q  85
SHEET    3  BT 3 GLY Q 170  LYS Q 171 -1  O  GLY Q 170   N  ARG Q 143
SHEET    1  BU 2 LYS Q 119  ASP Q 121  0
SHEET    2  BU 2 ILE Q 126  PHE Q 128 -1  O  ILE Q 126   N  ASP Q 121
SHEET    1  BV10 GLU S  19  ARG S  20  0
SHEET    2  BV10 SER S  27  SER S  32 -1  O  MET S  28   N  GLU S  19
SHEET    3  BV10 ASN S  37  PHE S  40 -1  O  VAL S  38   N  MET S  31
SHEET    4  BV10 LYS S  91  ILE S  95 -1  O  THR S  93   N  SER S  39
SHEET    5  BV10 ASP S  83  LEU S  86 -1  N  SER S  85   O  TYR S  92
SHEET    6  BV10 PHE S  71  THR S  79 -1  N  VAL S  78   O  SER S  84
SHEET    7  BV10 SER S 111  THR S 115 -1  O  SER S 111   N  GLY S  75
SHEET    8  BV10 LYS S  54  SER S  60 -1  N  SER S  60   O  PHE S 112
SHEET    9  BV10 ILE S  10  ILE S  15 -1  N  LEU S  11   O  VAL S  57
SHEET   10  BV10 SER S  27  SER S  32 -1  O  SER S  32   N  GLU S  14
SHEET    1  BW 2 ARG T  67  LYS T  68  0
SHEET    2  BW 2 GLU T  74  VAL T  75 -1  O  VAL T  75   N  ARG T  67
SHEET    1  BX 4 ILE V   5  SER V   8  0
SHEET    2  BX 4 LEU V  13  GLU V  18 -1  O  GLU V  14   N  LEU V   6
SHEET    3  BX 4 LYS V  52  LEU V  58 -1  O  VAL V  55   N  LEU V  15
SHEET    4  BX 4 PHE V  40  TYR V  44 -1  N  PHE V  40   O  LEU V  58
SSBOND   1 CYS A   58    CYS A   68                          1555   1555  2.03
SSBOND   2 CYS A   98    CYS A  101                          1555   1555  2.05
SSBOND   3 CYS A  575    CYS A  580                          1555   1555  2.74
SSBOND   4 CYS D   82    CYS D   92                          1555   1555  2.04
SSBOND   5 CYS D   85    CYS D   89                          1555   1555  2.03
SSBOND   6 CYS D  176    CYS D  213                          1555   1555  2.04
SSBOND   7 CYS G   13    CYS G   33                          1555   1555  2.03
SSBOND   8 CYS N    7    CYS N   45                          1555   1555  2.99
SSBOND   9 CYS N   10    CYS N   45                          1555   1555  2.04
SSBOND  10 CYS I   58    CYS I   68                          1555   1555  2.03
SSBOND  11 CYS I   98    CYS I  101                          1555   1555  2.05
SSBOND  12 CYS I  575    CYS I  580                          1555   1555  2.53
SSBOND  13 CYS O   82    CYS O   92                          1555   1555  2.04
SSBOND  14 CYS O   85    CYS O   89                          1555   1555  2.04
SSBOND  15 CYS O  176    CYS O  213                          1555   1555  2.02
SSBOND  16 CYS S   13    CYS S   33                          1555   1555  2.03
SSBOND  17 CYS W    7    CYS W   45                          1555   1555  2.91
SSBOND  18 CYS W   10    CYS W   45                          1555   1555  2.02
LINK         SG  CYS A  58                ZN    ZN A1001     1555   1555  2.53
LINK         SG  CYS A  68                ZN    ZN A1001     1555   1555  2.04
LINK         NE2 HIS A  71                ZN    ZN A1001     1555   1555  2.28
LINK         SG  CYS A  98                ZN    ZN A1002     1555   1555  2.14
LINK         SG  CYS A 146                ZN    ZN A1002     1555   1555  2.35
LINK         OD2 ASP A 458                MG    MG A1003     1555   1555  2.11
LINK         OD1 ASP A 460                MG    MG A1003     1555   1555  2.50
LINK         SG  CYS B1061                ZN    ZN B2001     1555   1555  2.53
LINK         SG  CYS B1079                ZN    ZN B2001     1555   1555  2.37
LINK         SG  CYS D 203                FE4  F3S D1001     1555   1555  1.92
LINK         SG  CYS D 209                FE1  F3S D1001     1555   1555  2.26
LINK         SG  CYS N   7                ZN    ZN N1001     1555   1555  2.94
LINK         SG  CYS N  10                ZN    ZN N1001     1555   1555  2.53
LINK         SG  CYS N  44                ZN    ZN N1001     1555   1555  2.47
LINK         SG  CYS P   9                ZN    ZN P1001     1555   1555  2.29
LINK         OG1 THR P  12                ZN    ZN P1001     1555   1555  2.39
LINK         SG  CYS P  26                ZN    ZN P1001     1555   1555  2.60
LINK         SG  CYS P  29                ZN    ZN P1001     1555   1555  2.52
LINK         SG  CYS I  68                ZN    ZN I1001     1555   1555  2.80
LINK         SG  CYS I  98                ZN    ZN I1002     1555   1555  2.46
LINK         SG  CYS I 146                ZN    ZN I1002     1555   1555  2.57
LINK         OD1 ASP I 456                MG    MG I1003     1555   1555  2.34
LINK         OD2 ASP I 456                MG    MG I1003     1555   1555  2.44
LINK         OD2 ASP I 458                MG    MG I1003     1555   1555  2.47
LINK         SG  CYS J1061                ZN    ZN J2001     1555   1555  2.48
LINK         SG  CYS J1079                ZN    ZN J2001     1555   1555  2.39
LINK         SG  CYS W   7                ZN    ZN W1001     1555   1555  2.81
LINK         SG  CYS W  44                ZN    ZN W1001     1555   1555  2.48
LINK         SG  CYS W  45                ZN    ZN W1001     1555   1555  2.06
LINK         SG  CYS X   9                ZN    ZN X1001     1555   1555  2.31
LINK         OG1 THR X  12                ZN    ZN X1001     1555   1555  2.12
LINK         SG  CYS X  26                ZN    ZN X1001     1555   1555  2.78
LINK         SG  CYS X  29                ZN    ZN X1001     1555   1555  2.13
CISPEP   1 LYS A  155    ILE A  156          0         1.48
CISPEP   2 GLN A  422    PRO A  423          0         6.59
CISPEP   3 MET C  163    SER C  164          0         9.78
CISPEP   4 GLU B  110    PRO B  111          0       -14.54
CISPEP   5 LEU P   21    PRO P   22          0         4.72
CISPEP   6 LYS I  155    ILE I  156          0         1.97
CISPEP   7 GLN I  422    PRO I  423          0        -0.74
CISPEP   8 MET M  163    SER M  164          0        -5.36
CISPEP   9 GLU J  110    PRO J  111          0       -15.20
CISPEP  10 LEU X   21    PRO X   22          0         3.08
SITE     1 AC1  5 CYS A  58  PRO A  59  ASN A  63  CYS A  68
SITE     2 AC1  5 HIS A  71
SITE     1 AC2  5 CYS A  98  CYS A 101  GLN A 144  VAL A 145
SITE     2 AC2  5 CYS A 146
SITE     1 AC3  3 ASP A 456  ASP A 458  ASP A 460
SITE     1 AC4  4 CYS B1061  CYS B1064  CYS B1079  ILE B1081
SITE     1 AC5  9 CYS D 183  GLU D 185  CYS D 203  THR D 204
SITE     2 AC5  9 LEU D 205  CYS D 206  GLU D 207  GLU D 208
SITE     3 AC5  9 CYS D 209
SITE     1 AC6  4 CYS N   7  CYS N  10  CYS N  44  CYS N  45
SITE     1 AC7  4 CYS P   9  THR P  12  CYS P  26  CYS P  29
SITE     1 AC8  6 CYS I  58  CYS I  61  ASN I  63  CYS I  68
SITE     2 AC8  6 HIS I  71  TYR J1070
SITE     1 AC9  5 CYS I  98  CYS I 101  GLN I 144  VAL I 145
SITE     2 AC9  5 CYS I 146
SITE     1 BC1  3 ASP I 456  ASP I 458  ASP I 460
SITE     1 BC2  3 CYS J1061  CYS J1064  CYS J1079
SITE     1 BC3 10 CYS O 183  GLU O 185  CYS O 203  THR O 204
SITE     2 BC3 10 LEU O 205  CYS O 206  GLU O 207  GLU O 208
SITE     3 BC3 10 CYS O 209  ILE O 219
SITE     1 BC4  5 CYS W   7  THR W   9  CYS W  10  CYS W  44
SITE     2 BC4  5 CYS W  45
SITE     1 BC5  4 CYS X   9  THR X  12  CYS X  26  CYS X  29
CRYST1  125.820  201.235  196.050  90.00 100.92  90.00 P 1 21 1      4
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      0.007948  0.000000  0.001533        0.00000
SCALE2      0.000000  0.004969  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005195        0.00000
      
 References