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PDBsum entry 3odm

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Lyase PDB id
3odm
Jmol
Contents
Protein chains
(+ 2 more) 525 a.a.
Ligands
AUC ×36
MLI ×5
Waters ×200
HEADER    LYASE                                   11-AUG-10   3ODM
TITLE     ARCHAEAL-TYPE PHOSPHOENOLPYRUVATE CARBOXYLASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYLASE;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;
COMPND   4 SYNONYM: PEPCASE, PEPC;
COMPND   5 EC: 4.1.1.31;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PERFRINGENS;
SOURCE   3 ORGANISM_TAXID: 1502;
SOURCE   4 GENE: CPE1094, PPCA;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)(PRIL);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PJLK15-19B
KEYWDS    BETA-BARREL, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.W.DUNTEN
REVDAT   4   25-MAY-11 3ODM    1       JRNL
REVDAT   3   11-MAY-11 3ODM    1       REMARK
REVDAT   2   27-APR-11 3ODM    1       JRNL
REVDAT   1   02-FEB-11 3ODM    0
JRNL        AUTH   L.DHARMARAJAN,J.L.KRASZEWSKI,B.MUKHOPADHYAY,P.W.DUNTEN
JRNL        TITL   STRUCTURE OF AN ARCHAEAL-TYPE PHOSPHOENOLPYRUVATE
JRNL        TITL 2 CARBOXYLASE SENSITIVE TO INHIBITION BY ASPARTATE.
JRNL        REF    PROTEINS                      V.  79  1820 2011
JRNL        REFN                   ISSN 0887-3585
JRNL        PMID   21491491
JRNL        DOI    10.1002/PROT.23006
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   L.DHARMARAHAN,J.L.KRASZEWSKI,B.MUKHOPADHYAY,P.W.DUNTEN
REMARK   1  TITL   EXPRESSION, PURIFICATION AND CRYSTALLIZATION OF AN
REMARK   1  TITL 2 ARCHAEAL-TYPE PHOSPHOENOLPYRUVATE CARBOXYLASE
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  65  1193 2009
REMARK   1  REFN                   ESSN 1744-3091
REMARK   1  PMID   19923749
REMARK   1  DOI    10.1107/S1744309109042663
REMARK   2
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0110
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) : 2.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.84
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 116208
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : THIN SHELLS
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178
REMARK   3   R VALUE            (WORKING SET) : 0.178
REMARK   3   FREE R VALUE                     : 0.223
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1135
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) : 2.95
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.03
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8334
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970
REMARK   3   BIN FREE R VALUE SET COUNT          : 0
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 33256
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 107
REMARK   3   SOLVENT ATOMS            : 200
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.52
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.45000
REMARK   3    B22 (A**2) : -1.66000
REMARK   3    B33 (A**2) : -0.78000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
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): 0.357
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.294
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.934
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 33866 ; 0.012 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 45628 ; 1.337 ; 1.982
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4200 ; 5.794 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1491 ;39.894 ;25.111
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  6474 ;19.247 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   176 ;19.795 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5186 ; 0.085 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 24912 ; 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): 20953 ; 0.346 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 33988 ; 0.710 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 12913 ; 1.203 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11640 ; 2.162 ; 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 : 2
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B C D E F G H
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1976 ;  0.33 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1976 ;  0.47 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    C    (A):   1976 ;  0.31 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    D    (A):   1976 ;  0.23 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    E    (A):   1976 ;  0.27 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    F    (A):   1976 ;  0.33 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    G    (A):   1976 ;  0.28 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    H    (A):   1976 ;  0.22 ;  0.05
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1909 ;  0.58 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1909 ;  0.66 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1909 ;  0.53 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1909 ;  0.52 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1909 ;  0.52 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    F    (A):   1909 ;  0.58 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    G    (A):   1909 ;  0.54 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    H    (A):   1909 ;  0.50 ;  0.50
REMARK   3   TIGHT THERMAL      1    A (A**2):   1976 ;  1.72 ;  5.00
REMARK   3   TIGHT THERMAL      1    B (A**2):   1976 ;  1.38 ;  5.00
REMARK   3   TIGHT THERMAL      1    C (A**2):   1976 ;  1.24 ;  5.00
REMARK   3   TIGHT THERMAL      1    D (A**2):   1976 ;  1.48 ;  5.00
REMARK   3   TIGHT THERMAL      1    E (A**2):   1976 ;  1.55 ;  5.00
REMARK   3   TIGHT THERMAL      1    F (A**2):   1976 ;  1.23 ;  5.00
REMARK   3   TIGHT THERMAL      1    G (A**2):   1976 ;  1.96 ;  5.00
REMARK   3   TIGHT THERMAL      1    H (A**2):   1976 ;  1.51 ;  5.00
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1909 ;  2.17 ;  5.00
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1909 ;  1.72 ;  5.00
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1909 ;  1.64 ;  5.00
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1909 ;  1.81 ;  5.00
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1909 ;  1.86 ;  5.00
REMARK   3   MEDIUM THERMAL     1    F (A**2):   1909 ;  1.52 ;  5.00
REMARK   3   MEDIUM THERMAL     1    G (A**2):   1909 ;  2.17 ;  5.00
REMARK   3   MEDIUM THERMAL     1    H (A**2):   1909 ;  1.89 ;  5.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : A B C D E F G H
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   LOOSE POSITIONAL   2    A    (A):    185 ;  0.59 ;  5.00
REMARK   3   LOOSE POSITIONAL   2    B    (A):    185 ;  0.67 ;  5.00
REMARK   3   LOOSE POSITIONAL   2    C    (A):    185 ;  0.78 ;  5.00
REMARK   3   LOOSE POSITIONAL   2    D    (A):    185 ;  0.87 ;  5.00
REMARK   3   LOOSE POSITIONAL   2    E    (A):    185 ;  0.85 ;  5.00
REMARK   3   LOOSE POSITIONAL   2    F    (A):    185 ;  0.78 ;  5.00
REMARK   3   LOOSE POSITIONAL   2    G    (A):    185 ;  0.70 ;  5.00
REMARK   3   LOOSE POSITIONAL   2    H    (A):    185 ;  0.68 ;  5.00
REMARK   3   LOOSE THERMAL      2    A (A**2):    185 ;  3.09 ; 14.00
REMARK   3   LOOSE THERMAL      2    B (A**2):    185 ;  2.80 ; 14.00
REMARK   3   LOOSE THERMAL      2    C (A**2):    185 ;  3.69 ; 14.00
REMARK   3   LOOSE THERMAL      2    D (A**2):    185 ;  1.91 ; 14.00
REMARK   3   LOOSE THERMAL      2    E (A**2):    185 ;  1.40 ; 14.00
REMARK   3   LOOSE THERMAL      2    F (A**2):    185 ;  3.70 ; 14.00
REMARK   3   LOOSE THERMAL      2    G (A**2):    185 ;  1.82 ; 14.00
REMARK   3   LOOSE THERMAL      2    H (A**2):    185 ;  7.37 ; 14.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 58
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     1        A   102
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9189  33.5284  73.4101
REMARK   3    T TENSOR
REMARK   3      T11:   0.0367 T22:   0.0244
REMARK   3      T33:   0.0583 T12:   0.0126
REMARK   3      T13:   0.0070 T23:  -0.0195
REMARK   3    L TENSOR
REMARK   3      L11:   4.0641 L22:   2.2870
REMARK   3      L33:   2.2316 L12:   1.1203
REMARK   3      L13:  -1.4385 L23:   0.2275
REMARK   3    S TENSOR
REMARK   3      S11:   0.0119 S12:   0.0115 S13:   0.2723
REMARK   3      S21:  -0.0951 S22:  -0.0485 S23:  -0.0765
REMARK   3      S31:  -0.1532 S32:  -0.2045 S33:   0.0366
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   103        A   202
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9916  19.1143  68.3066
REMARK   3    T TENSOR
REMARK   3      T11:   0.0688 T22:   0.0737
REMARK   3      T33:   0.0468 T12:  -0.0511
REMARK   3      T13:  -0.0178 T23:  -0.0094
REMARK   3    L TENSOR
REMARK   3      L11:   2.5457 L22:   2.6366
REMARK   3      L33:   2.0214 L12:   0.0279
REMARK   3      L13:  -0.5704 L23:   0.5085
REMARK   3    S TENSOR
REMARK   3      S11:   0.0501 S12:  -0.0007 S13:  -0.2084
REMARK   3      S21:  -0.1292 S22:  -0.1190 S23:   0.2749
REMARK   3      S31:   0.0470 S32:  -0.2619 S33:   0.0689
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   203        A   280
REMARK   3    ORIGIN FOR THE GROUP (A):  23.2686  24.1737  61.3523
REMARK   3    T TENSOR
REMARK   3      T11:   0.0737 T22:   0.1263
REMARK   3      T33:   0.0683 T12:   0.0055
REMARK   3      T13:   0.0606 T23:   0.0176
REMARK   3    L TENSOR
REMARK   3      L11:   2.2129 L22:   1.8611
REMARK   3      L33:   1.9113 L12:   0.1325
REMARK   3      L13:   0.3401 L23:  -0.0940
REMARK   3    S TENSOR
REMARK   3      S11:   0.1174 S12:   0.4886 S13:   0.1845
REMARK   3      S21:  -0.2480 S22:   0.0088 S23:  -0.0864
REMARK   3      S31:  -0.0280 S32:   0.0690 S33:  -0.1262
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   281        A   346
REMARK   3    ORIGIN FOR THE GROUP (A):  28.3793  20.5419  66.6219
REMARK   3    T TENSOR
REMARK   3      T11:   0.0833 T22:   0.0373
REMARK   3      T33:   0.0394 T12:  -0.0296
REMARK   3      T13:   0.0469 T23:  -0.0350
REMARK   3    L TENSOR
REMARK   3      L11:   2.7384 L22:   2.4187
REMARK   3      L33:   1.4452 L12:  -0.9740
REMARK   3      L13:   0.1059 L23:   0.8615
REMARK   3    S TENSOR
REMARK   3      S11:   0.0237 S12:   0.1513 S13:  -0.1010
REMARK   3      S21:  -0.0773 S22:   0.0402 S23:  -0.0238
REMARK   3      S31:   0.0644 S32:   0.1339 S33:  -0.0639
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   359        A   388
REMARK   3    ORIGIN FOR THE GROUP (A):  30.8198   1.7179  71.7164
REMARK   3    T TENSOR
REMARK   3      T11:   0.3838 T22:   0.2326
REMARK   3      T33:   0.3299 T12:   0.0047
REMARK   3      T13:   0.0593 T23:   0.0146
REMARK   3    L TENSOR
REMARK   3      L11:   1.8293 L22:   7.4671
REMARK   3      L33:   3.6124 L12:   0.3451
REMARK   3      L13:   0.7838 L23:   4.5938
REMARK   3    S TENSOR
REMARK   3      S11:   0.1216 S12:  -0.4024 S13:  -0.3825
REMARK   3      S21:   0.6837 S22:   0.1412 S23:  -0.2510
REMARK   3      S31:   0.6358 S32:   0.2155 S33:  -0.2628
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   389        A   393
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0209  22.7392  78.6705
REMARK   3    T TENSOR
REMARK   3      T11:   0.1562 T22:   0.0430
REMARK   3      T33:   0.0992 T12:   0.0014
REMARK   3      T13:  -0.0180 T23:  -0.0475
REMARK   3    L TENSOR
REMARK   3      L11:  28.5858 L22:  68.1060
REMARK   3      L33:  11.8389 L12: -43.8966
REMARK   3      L13:  -2.2599 L23:   6.3227
REMARK   3    S TENSOR
REMARK   3      S11:   0.6642 S12:   0.5844 S13:  -1.6135
REMARK   3      S21:  -1.0362 S22:  -1.0319 S23:   2.5357
REMARK   3      S31:  -0.1933 S32:  -0.6222 S33:   0.3676
REMARK   3
REMARK   3   TLS GROUP : 7
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   394        A   490
REMARK   3    ORIGIN FOR THE GROUP (A):  43.6768  19.7195  66.7048
REMARK   3    T TENSOR
REMARK   3      T11:   0.0865 T22:   0.1398
REMARK   3      T33:   0.1509 T12:   0.0284
REMARK   3      T13:   0.0768 T23:  -0.0707
REMARK   3    L TENSOR
REMARK   3      L11:   2.2419 L22:   2.3629
REMARK   3      L33:   2.4678 L12:   0.8380
REMARK   3      L13:   0.5837 L23:   1.8438
REMARK   3    S TENSOR
REMARK   3      S11:   0.1704 S12:   0.2299 S13:  -0.0733
REMARK   3      S21:  -0.0979 S22:   0.1806 S23:  -0.3812
REMARK   3      S31:   0.0343 S32:   0.4101 S33:  -0.3510
REMARK   3
REMARK   3   TLS GROUP : 8
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   491        A   537
REMARK   3    ORIGIN FOR THE GROUP (A):  40.1011  30.8044  87.1368
REMARK   3    T TENSOR
REMARK   3      T11:   0.2326 T22:   0.0870
REMARK   3      T33:   0.2216 T12:  -0.0195
REMARK   3      T13:   0.0366 T23:  -0.0679
REMARK   3    L TENSOR
REMARK   3      L11:   1.5812 L22:   2.0453
REMARK   3      L33:  10.8920 L12:   0.1699
REMARK   3      L13:   1.9845 L23:   0.3048
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0896 S12:  -0.3220 S13:   0.0226
REMARK   3      S21:   0.5440 S22:  -0.0558 S23:  -0.1584
REMARK   3      S31:  -0.6456 S32:  -0.3551 S33:   0.1455
REMARK   3
REMARK   3   TLS GROUP : 9
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     1        B   106
REMARK   3    ORIGIN FOR THE GROUP (A):  86.3372  75.5700 165.7676
REMARK   3    T TENSOR
REMARK   3      T11:   0.1287 T22:   0.0653
REMARK   3      T33:   0.0926 T12:  -0.0164
REMARK   3      T13:  -0.0443 T23:   0.0057
REMARK   3    L TENSOR
REMARK   3      L11:   1.7512 L22:   1.1476
REMARK   3      L33:   3.7914 L12:  -0.2331
REMARK   3      L13:   1.1347 L23:   0.6449
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1298 S12:   0.1913 S13:   0.0836
REMARK   3      S21:   0.0122 S22:   0.1697 S23:  -0.1528
REMARK   3      S31:  -0.1152 S32:   0.1799 S33:  -0.0398
REMARK   3
REMARK   3   TLS GROUP : 10
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   107        B   191
REMARK   3    ORIGIN FOR THE GROUP (A): 102.6684  72.3204 171.3763
REMARK   3    T TENSOR
REMARK   3      T11:   0.2290 T22:   0.1182
REMARK   3      T33:   0.2839 T12:  -0.0226
REMARK   3      T13:  -0.1125 T23:   0.0267
REMARK   3    L TENSOR
REMARK   3      L11:   3.7834 L22:   1.7791
REMARK   3      L33:   2.7641 L12:  -0.0320
REMARK   3      L13:  -0.3145 L23:  -0.0292
REMARK   3    S TENSOR
REMARK   3      S11:   0.0378 S12:   0.0085 S13:   0.0047
REMARK   3      S21:  -0.0864 S22:  -0.0683 S23:  -0.4537
REMARK   3      S31:  -0.2753 S32:   0.5361 S33:   0.0306
REMARK   3
REMARK   3   TLS GROUP : 11
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   192        B   286
REMARK   3    ORIGIN FOR THE GROUP (A):  96.4572  70.6122 150.3909
REMARK   3    T TENSOR
REMARK   3      T11:   0.2244 T22:   0.2242
REMARK   3      T33:   0.1470 T12:  -0.0531
REMARK   3      T13:   0.0061 T23:  -0.0487
REMARK   3    L TENSOR
REMARK   3      L11:   1.4437 L22:   2.0688
REMARK   3      L33:   2.0123 L12:  -0.1702
REMARK   3      L13:  -0.1749 L23:  -1.0025
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0587 S12:   0.2348 S13:  -0.1016
REMARK   3      S21:  -0.1021 S22:  -0.0829 S23:  -0.3489
REMARK   3      S31:   0.1192 S32:   0.4198 S33:   0.1416
REMARK   3
REMARK   3   TLS GROUP : 12
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   287        B   346
REMARK   3    ORIGIN FOR THE GROUP (A): 100.1016  79.1996 145.4727
REMARK   3    T TENSOR
REMARK   3      T11:   0.2741 T22:   0.4296
REMARK   3      T33:   0.1567 T12:  -0.0896
REMARK   3      T13:  -0.0810 T23:  -0.0919
REMARK   3    L TENSOR
REMARK   3      L11:   2.3935 L22:   0.9732
REMARK   3      L33:   1.6793 L12:   0.0286
REMARK   3      L13:  -0.4768 L23:  -1.1507
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1512 S12:   0.0943 S13:   0.0443
REMARK   3      S21:   0.0202 S22:  -0.0703 S23:  -0.2930
REMARK   3      S31:   0.0429 S32:   0.3561 S33:   0.2215
REMARK   3
REMARK   3   TLS GROUP : 13
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   355        B   390
REMARK   3    ORIGIN FOR THE GROUP (A): 112.1263  90.3726 145.7011
REMARK   3    T TENSOR
REMARK   3      T11:   0.4947 T22:   0.6514
REMARK   3      T33:   0.5855 T12:  -0.0641
REMARK   3      T13:  -0.0250 T23:   0.0099
REMARK   3    L TENSOR
REMARK   3      L11:   3.7877 L22:   0.4663
REMARK   3      L33:   2.1435 L12:  -0.9932
REMARK   3      L13:  -1.2739 L23:   0.2431
REMARK   3    S TENSOR
REMARK   3      S11:   0.0053 S12:  -0.0064 S13:   0.4081
REMARK   3      S21:   0.2884 S22:   0.0228 S23:  -0.2257
REMARK   3      S31:   0.0942 S32:   0.0750 S33:  -0.0281
REMARK   3
REMARK   3   TLS GROUP : 14
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   391        B   490
REMARK   3    ORIGIN FOR THE GROUP (A):  97.2289  82.7455 131.6736
REMARK   3    T TENSOR
REMARK   3      T11:   0.2991 T22:   0.3797
REMARK   3      T33:   0.1510 T12:  -0.1333
REMARK   3      T13:   0.0152 T23:   0.0317
REMARK   3    L TENSOR
REMARK   3      L11:   2.5221 L22:   2.0106
REMARK   3      L33:   2.0599 L12:  -0.9729
REMARK   3      L13:   0.6599 L23:   0.1512
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0303 S12:   0.5725 S13:   0.0323
REMARK   3      S21:  -0.4239 S22:  -0.0464 S23:  -0.1674
REMARK   3      S31:   0.0408 S32:   0.3498 S33:   0.0767
REMARK   3
REMARK   3   TLS GROUP : 15
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   491        B   537
REMARK   3    ORIGIN FOR THE GROUP (A):  82.4054  97.9535 141.0876
REMARK   3    T TENSOR
REMARK   3      T11:   0.3769 T22:   0.2838
REMARK   3      T33:   0.3209 T12:  -0.1146
REMARK   3      T13:  -0.1361 T23:  -0.0066
REMARK   3    L TENSOR
REMARK   3      L11:   2.6548 L22:   5.3767
REMARK   3      L33:   1.0511 L12:  -1.8813
REMARK   3      L13:  -0.3278 L23:  -1.0395
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1696 S12:  -0.2689 S13:   0.5469
REMARK   3      S21:   0.3816 S22:   0.2755 S23:   0.3556
REMARK   3      S31:  -0.4358 S32:  -0.0382 S33:  -0.1059
REMARK   3
REMARK   3   TLS GROUP : 16
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C     1        C   102
REMARK   3    ORIGIN FOR THE GROUP (A):  55.1247  66.8861 106.1168
REMARK   3    T TENSOR
REMARK   3      T11:   0.0693 T22:   0.0208
REMARK   3      T33:   0.0977 T12:  -0.0254
REMARK   3      T13:  -0.0511 T23:   0.0224
REMARK   3    L TENSOR
REMARK   3      L11:   2.7376 L22:   4.6775
REMARK   3      L33:   2.0065 L12:   0.2660
REMARK   3      L13:   0.0758 L23:  -0.6995
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1704 S12:   0.1769 S13:  -0.0928
REMARK   3      S21:   0.2838 S22:  -0.0634 S23:  -0.2094
REMARK   3      S31:  -0.0020 S32:   0.1089 S33:   0.2338
REMARK   3
REMARK   3   TLS GROUP : 17
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   103        C   193
REMARK   3    ORIGIN FOR THE GROUP (A):  70.8902  73.9110 109.0188
REMARK   3    T TENSOR
REMARK   3      T11:   0.1236 T22:   0.1480
REMARK   3      T33:   0.1888 T12:  -0.0643
REMARK   3      T13:  -0.1189 T23:   0.0217
REMARK   3    L TENSOR
REMARK   3      L11:   4.2762 L22:   3.4083
REMARK   3      L33:   2.5735 L12:  -0.4715
REMARK   3      L13:  -0.0357 L23:  -0.6130
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0440 S12:   0.1356 S13:   0.1461
REMARK   3      S21:   0.0849 S22:  -0.0200 S23:  -0.5223
REMARK   3      S31:  -0.0769 S32:   0.4282 S33:   0.0640
REMARK   3
REMARK   3   TLS GROUP : 18
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   194        C   280
REMARK   3    ORIGIN FOR THE GROUP (A):  66.5788  52.4369 111.7933
REMARK   3    T TENSOR
REMARK   3      T11:   0.1716 T22:   0.0766
REMARK   3      T33:   0.2174 T12:   0.0341
REMARK   3      T13:  -0.1206 T23:   0.0270
REMARK   3    L TENSOR
REMARK   3      L11:   2.7659 L22:   3.3079
REMARK   3      L33:   2.3399 L12:   0.9591
REMARK   3      L13:   0.4856 L23:   1.4393
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1279 S12:  -0.0416 S13:  -0.4102
REMARK   3      S21:   0.3832 S22:   0.1895 S23:  -0.4368
REMARK   3      S31:   0.1191 S32:   0.3145 S33:  -0.0617
REMARK   3
REMARK   3   TLS GROUP : 19
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   281        C   348
REMARK   3    ORIGIN FOR THE GROUP (A):  67.7790  48.0226 104.8011
REMARK   3    T TENSOR
REMARK   3      T11:   0.0786 T22:   0.0976
REMARK   3      T33:   0.3672 T12:  -0.0390
REMARK   3      T13:  -0.0500 T23:   0.0776
REMARK   3    L TENSOR
REMARK   3      L11:   3.3530 L22:   2.1828
REMARK   3      L33:   2.4555 L12:  -1.2863
REMARK   3      L13:   0.4960 L23:   1.0340
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2108 S12:   0.1530 S13:  -0.1141
REMARK   3      S21:   0.2276 S22:   0.0479 S23:  -0.4719
REMARK   3      S31:   0.0625 S32:   0.3968 S33:   0.1629
REMARK   3
REMARK   3   TLS GROUP : 20
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   356        C   389
REMARK   3    ORIGIN FOR THE GROUP (A):  83.3316  46.0725  94.0544
REMARK   3    T TENSOR
REMARK   3      T11:   0.6840 T22:   0.8602
REMARK   3      T33:   0.8573 T12:  -0.0529
REMARK   3      T13:  -0.0363 T23:   0.0222
REMARK   3    L TENSOR
REMARK   3      L11:   5.8962 L22:   0.5558
REMARK   3      L33:   0.4438 L12:  -1.0441
REMARK   3      L13:  -1.0245 L23:   0.4840
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2069 S12:   0.5263 S13:  -0.0748
REMARK   3      S21:   0.0258 S22:   0.2983 S23:  -0.1417
REMARK   3      S31:  -0.0723 S32:   0.2748 S33:  -0.0914
REMARK   3
REMARK   3   TLS GROUP : 21
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   390        C   490
REMARK   3    ORIGIN FOR THE GROUP (A):  66.9177  33.5574 101.2971
REMARK   3    T TENSOR
REMARK   3      T11:   0.1808 T22:   0.0824
REMARK   3      T33:   0.4342 T12:   0.0814
REMARK   3      T13:  -0.0262 T23:  -0.0387
REMARK   3    L TENSOR
REMARK   3      L11:   2.6448 L22:   2.0877
REMARK   3      L33:   2.9234 L12:   0.0930
REMARK   3      L13:   1.2652 L23:  -0.8938
REMARK   3    S TENSOR
REMARK   3      S11:   0.0132 S12:   0.1388 S13:  -0.5391
REMARK   3      S21:   0.2408 S22:  -0.0005 S23:  -0.4459
REMARK   3      S31:   0.4357 S32:   0.3657 S33:  -0.0127
REMARK   3
REMARK   3   TLS GROUP : 22
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   491        C   537
REMARK   3    ORIGIN FOR THE GROUP (A):  52.3538  42.1594  85.5897
REMARK   3    T TENSOR
REMARK   3      T11:   0.0899 T22:   0.1934
REMARK   3      T33:   0.2581 T12:  -0.0457
REMARK   3      T13:   0.0123 T23:  -0.0836
REMARK   3    L TENSOR
REMARK   3      L11:   2.3655 L22:   1.4063
REMARK   3      L33:   7.1811 L12:   0.1175
REMARK   3      L13:   0.2703 L23:   2.0620
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3244 S12:   0.4909 S13:   0.1517
REMARK   3      S21:  -0.2063 S22:   0.0358 S23:  -0.2155
REMARK   3      S31:  -0.5272 S32:  -0.5230 S33:   0.2886
REMARK   3
REMARK   3   TLS GROUP : 23
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D     1        D   102
REMARK   3    ORIGIN FOR THE GROUP (A):  49.7685  76.9494  82.2803
REMARK   3    T TENSOR
REMARK   3      T11:   0.0671 T22:   0.2077
REMARK   3      T33:   0.0561 T12:  -0.0299
REMARK   3      T13:  -0.0217 T23:   0.0623
REMARK   3    L TENSOR
REMARK   3      L11:   3.5303 L22:   1.8953
REMARK   3      L33:   1.0925 L12:  -0.0136
REMARK   3      L13:   1.3245 L23:   0.0902
REMARK   3    S TENSOR
REMARK   3      S11:   0.0738 S12:   0.4023 S13:   0.0037
REMARK   3      S21:  -0.1698 S22:  -0.1870 S23:   0.0225
REMARK   3      S31:   0.0278 S32:   0.1117 S33:   0.1132
REMARK   3
REMARK   3   TLS GROUP : 24
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D   103        D   177
REMARK   3    ORIGIN FOR THE GROUP (A):  58.3407  89.3780  84.3674
REMARK   3    T TENSOR
REMARK   3      T11:   0.0812 T22:   0.2013
REMARK   3      T33:   0.2101 T12:  -0.0755
REMARK   3      T13:  -0.0200 T23:   0.1461
REMARK   3    L TENSOR
REMARK   3      L11:   5.5820 L22:   3.1407
REMARK   3      L33:   2.9601 L12:  -1.1044
REMARK   3      L13:   0.5251 L23:  -0.2420
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1263 S12:   0.1130 S13:   0.6771
REMARK   3      S21:  -0.0567 S22:  -0.0498 S23:  -0.2740
REMARK   3      S31:  -0.2481 S32:   0.2610 S33:   0.1761
REMARK   3
REMARK   3   TLS GROUP : 25
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D   178        D   280
REMARK   3    ORIGIN FOR THE GROUP (A):  41.5890  92.8686  77.3741
REMARK   3    T TENSOR
REMARK   3      T11:   0.1273 T22:   0.2379
REMARK   3      T33:   0.2140 T12:  -0.0222
REMARK   3      T13:  -0.0275 T23:   0.1742
REMARK   3    L TENSOR
REMARK   3      L11:   2.8469 L22:   0.7946
REMARK   3      L33:   1.2716 L12:  -0.0334
REMARK   3      L13:   0.0283 L23:   0.1648
REMARK   3    S TENSOR
REMARK   3      S11:   0.0709 S12:   0.5842 S13:   0.4469
REMARK   3      S21:  -0.1885 S22:  -0.0193 S23:  -0.1596
REMARK   3      S31:  -0.1824 S32:   0.0739 S33:  -0.0516
REMARK   3
REMARK   3   TLS GROUP : 26
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D   281        D   346
REMARK   3    ORIGIN FOR THE GROUP (A):  32.3072  91.7386  82.8803
REMARK   3    T TENSOR
REMARK   3      T11:   0.0940 T22:   0.1329
REMARK   3      T33:   0.1149 T12:  -0.1057
REMARK   3      T13:  -0.0844 T23:   0.1129
REMARK   3    L TENSOR
REMARK   3      L11:   2.4389 L22:   2.8248
REMARK   3      L33:   1.1964 L12:  -1.4574
REMARK   3      L13:  -0.2403 L23:   0.1024
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0469 S12:   0.2356 S13:   0.2962
REMARK   3      S21:   0.0307 S22:  -0.1419 S23:  -0.2740
REMARK   3      S31:  -0.1512 S32:   0.1341 S33:   0.1888
REMARK   3
REMARK   3   TLS GROUP : 27
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D   358        D   390
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7417 104.8873  95.8538
REMARK   3    T TENSOR
REMARK   3      T11:   0.6454 T22:   0.6398
REMARK   3      T33:   0.5204 T12:  -0.0861
REMARK   3      T13:  -0.1527 T23:  -0.0810
REMARK   3    L TENSOR
REMARK   3      L11:   1.5109 L22:  12.7086
REMARK   3      L33:   0.9787 L12:  -1.2207
REMARK   3      L13:   0.4373 L23:  -3.2972
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3339 S12:  -0.5848 S13:   0.5506
REMARK   3      S21:   0.8675 S22:   0.3040 S23:  -0.1263
REMARK   3      S31:  -0.4234 S32:   0.0249 S33:   0.0299
REMARK   3
REMARK   3   TLS GROUP : 28
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D   391        D   506
REMARK   3    ORIGIN FOR THE GROUP (A):  17.2006  90.0100  86.0619
REMARK   3    T TENSOR
REMARK   3      T11:   0.0639 T22:   0.1211
REMARK   3      T33:   0.0985 T12:   0.0357
REMARK   3      T13:  -0.0326 T23:  -0.0026
REMARK   3    L TENSOR
REMARK   3      L11:   2.0808 L22:   2.8295
REMARK   3      L33:   2.3247 L12:   0.7936
REMARK   3      L13:   0.2692 L23:  -1.6595
REMARK   3    S TENSOR
REMARK   3      S11:   0.1038 S12:   0.2708 S13:   0.1737
REMARK   3      S21:   0.1428 S22:  -0.0787 S23:   0.3247
REMARK   3      S31:  -0.2548 S32:  -0.0865 S33:  -0.0250
REMARK   3
REMARK   3   TLS GROUP : 29
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D   507        D   537
REMARK   3    ORIGIN FOR THE GROUP (A):  24.5029  72.1587  97.6297
REMARK   3    T TENSOR
REMARK   3      T11:   0.1744 T22:   0.0171
REMARK   3      T33:   0.1957 T12:  -0.0065
REMARK   3      T13:  -0.0451 T23:   0.0325
REMARK   3    L TENSOR
REMARK   3      L11:   3.4533 L22:   2.4336
REMARK   3      L33:  17.6806 L12:   0.7481
REMARK   3      L13:  -2.3959 L23:  -3.2825
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1811 S12:  -0.1986 S13:  -0.2526
REMARK   3      S21:   0.3411 S22:  -0.0162 S23:  -0.1758
REMARK   3      S31:   0.7703 S32:  -0.1077 S33:   0.1973
REMARK   3
REMARK   3   TLS GROUP : 30
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E     1        E   106
REMARK   3    ORIGIN FOR THE GROUP (A):   6.7876  31.9120  99.3419
REMARK   3    T TENSOR
REMARK   3      T11:   0.0257 T22:   0.0072
REMARK   3      T33:   0.0407 T12:  -0.0105
REMARK   3      T13:   0.0219 T23:  -0.0147
REMARK   3    L TENSOR
REMARK   3      L11:   2.3129 L22:   4.1879
REMARK   3      L33:   3.4354 L12:   1.3669
REMARK   3      L13:   0.4203 L23:   1.3116
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0978 S12:  -0.0016 S13:   0.0869
REMARK   3      S21:   0.0693 S22:   0.0028 S23:   0.0846
REMARK   3      S31:   0.1161 S32:  -0.0900 S33:   0.0951
REMARK   3
REMARK   3   TLS GROUP : 31
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E   107        E   191
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.4417  25.3043  99.5454
REMARK   3    T TENSOR
REMARK   3      T11:   0.0701 T22:   0.1037
REMARK   3      T33:   0.1710 T12:  -0.0630
REMARK   3      T13:   0.0182 T23:  -0.0153
REMARK   3    L TENSOR
REMARK   3      L11:   3.1805 L22:   3.7771
REMARK   3      L33:   3.1037 L12:   0.0222
REMARK   3      L13:  -0.0476 L23:   1.1131
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0361 S12:   0.0807 S13:  -0.1091
REMARK   3      S21:  -0.0846 S22:  -0.0354 S23:   0.7180
REMARK   3      S31:   0.0824 S32:  -0.4455 S33:   0.0715
REMARK   3
REMARK   3   TLS GROUP : 32
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E   192        E   280
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3385  42.4617 111.3873
REMARK   3    T TENSOR
REMARK   3      T11:   0.1182 T22:   0.1198
REMARK   3      T33:   0.0951 T12:  -0.0051
REMARK   3      T13:   0.0825 T23:  -0.0474
REMARK   3    L TENSOR
REMARK   3      L11:   1.2788 L22:   3.8115
REMARK   3      L33:   1.1235 L12:   0.5613
REMARK   3      L13:  -0.4790 L23:  -0.8208
REMARK   3    S TENSOR
REMARK   3      S11:   0.0260 S12:  -0.0888 S13:   0.1162
REMARK   3      S21:   0.4351 S22:   0.0366 S23:   0.4551
REMARK   3      S31:   0.0196 S32:  -0.1546 S33:  -0.0626
REMARK   3
REMARK   3   TLS GROUP : 33
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E   281        E   346
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8224  49.7951 107.4847
REMARK   3    T TENSOR
REMARK   3      T11:   0.0367 T22:   0.1170
REMARK   3      T33:   0.0820 T12:  -0.0251
REMARK   3      T13:   0.0443 T23:  -0.0332
REMARK   3    L TENSOR
REMARK   3      L11:   2.9714 L22:   2.9246
REMARK   3      L33:   1.3899 L12:  -0.0364
REMARK   3      L13:  -0.5461 L23:  -0.2855
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0684 S12:   0.0128 S13:   0.2023
REMARK   3      S21:   0.2527 S22:   0.0698 S23:   0.3559
REMARK   3      S31:   0.0364 S32:  -0.3409 S33:  -0.0014
REMARK   3
REMARK   3   TLS GROUP : 34
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E   360        E   389
REMARK   3    ORIGIN FOR THE GROUP (A): -22.3571  55.6734  99.5710
REMARK   3    T TENSOR
REMARK   3      T11:   0.4836 T22:   0.7049
REMARK   3      T33:   0.7924 T12:   0.0820
REMARK   3      T13:  -0.0730 T23:   0.0085
REMARK   3    L TENSOR
REMARK   3      L11:  12.5239 L22:   0.5563
REMARK   3      L33:   4.6540 L12:  -0.1826
REMARK   3      L13:  -7.6148 L23:   0.2188
REMARK   3    S TENSOR
REMARK   3      S11:   0.0205 S12:   0.5372 S13:   0.4613
REMARK   3      S21:  -0.2059 S22:   0.1272 S23:   0.5938
REMARK   3      S31:  -0.0179 S32:  -0.2973 S33:  -0.1477
REMARK   3
REMARK   3   TLS GROUP : 35
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E   390        E   393
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6367  49.7420  96.7083
REMARK   3    T TENSOR
REMARK   3      T11:   2.5765 T22:   0.9592
REMARK   3      T33:   0.3736 T12:  -0.6537
REMARK   3      T13:  -0.2449 T23:   0.3982
REMARK   3    L TENSOR
REMARK   3      L11:  65.0958 L22: 105.3162
REMARK   3      L33:   5.4307 L12: -82.7882
REMARK   3      L13:  18.7968 L23: -23.9137
REMARK   3    S TENSOR
REMARK   3      S11:  -2.9171 S12:  -3.2938 S13:  -4.3700
REMARK   3      S21:   3.3940 S22:   4.2491 S23:   5.6038
REMARK   3      S31:  -0.7418 S32:  -0.9725 S33:  -1.3320
REMARK   3
REMARK   3   TLS GROUP : 36
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E   394        E   490
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.1778  64.8243 110.4589
REMARK   3    T TENSOR
REMARK   3      T11:   0.2652 T22:   0.0677
REMARK   3      T33:   0.2340 T12:   0.0709
REMARK   3      T13:   0.0465 T23:  -0.0791
REMARK   3    L TENSOR
REMARK   3      L11:   3.7908 L22:   3.1442
REMARK   3      L33:   3.6745 L12:   1.3026
REMARK   3      L13:  -1.6029 L23:  -1.1225
REMARK   3    S TENSOR
REMARK   3      S11:   0.0611 S12:  -0.2961 S13:   0.7372
REMARK   3      S21:   0.7089 S22:   0.0059 S23:   0.3109
REMARK   3      S31:  -0.5390 S32:  -0.2355 S33:  -0.0670
REMARK   3
REMARK   3   TLS GROUP : 37
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E   491        E   537
REMARK   3    ORIGIN FOR THE GROUP (A):   9.1597  63.5941  91.9954
REMARK   3    T TENSOR
REMARK   3      T11:   0.0443 T22:   0.1934
REMARK   3      T33:   0.1882 T12:  -0.0522
REMARK   3      T13:  -0.0458 T23:   0.1237
REMARK   3    L TENSOR
REMARK   3      L11:   2.7241 L22:   3.8333
REMARK   3      L33:   7.7609 L12:   2.0310
REMARK   3      L13:  -0.0369 L23:  -2.3141
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3407 S12:   0.4910 S13:   0.4534
REMARK   3      S21:  -0.3028 S22:  -0.0956 S23:  -0.0070
REMARK   3      S31:   0.1141 S32:   0.4958 S33:   0.4363
REMARK   3
REMARK   3   TLS GROUP : 38
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   F     1        F    56
REMARK   3    ORIGIN FOR THE GROUP (A):  39.6380  81.2537 136.3248
REMARK   3    T TENSOR
REMARK   3      T11:   0.2580 T22:   0.1398
REMARK   3      T33:   0.0966 T12:   0.0825
REMARK   3      T13:  -0.1464 T23:  -0.0102
REMARK   3    L TENSOR
REMARK   3      L11:   1.8578 L22:   2.8859
REMARK   3      L33:   2.5404 L12:  -0.3035
REMARK   3      L13:   0.0682 L23:  -1.2801
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0407 S12:  -0.0446 S13:  -0.0009
REMARK   3      S21:  -0.1186 S22:  -0.0027 S23:   0.1396
REMARK   3      S31:  -0.0793 S32:  -0.0222 S33:   0.0434
REMARK   3
REMARK   3   TLS GROUP : 39
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   F    57        F   188
REMARK   3    ORIGIN FOR THE GROUP (A):  25.2801  84.9394 126.3531
REMARK   3    T TENSOR
REMARK   3      T11:   0.3043 T22:   0.2089
REMARK   3      T33:   0.1768 T12:   0.0901
REMARK   3      T13:  -0.1560 T23:  -0.0441
REMARK   3    L TENSOR
REMARK   3      L11:   3.4709 L22:   1.7979
REMARK   3      L33:   1.9094 L12:   0.3714
REMARK   3      L13:  -0.0389 L23:  -0.2797
REMARK   3    S TENSOR
REMARK   3      S11:   0.0348 S12:  -0.0919 S13:   0.1662
REMARK   3      S21:   0.0105 S22:  -0.0323 S23:   0.3997
REMARK   3      S31:  -0.0883 S32:  -0.3993 S33:  -0.0025
REMARK   3
REMARK   3   TLS GROUP : 40
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   F   189        F   292
REMARK   3    ORIGIN FOR THE GROUP (A):  26.9622  71.2704 141.9802
REMARK   3    T TENSOR
REMARK   3      T11:   0.2911 T22:   0.2198
REMARK   3      T33:   0.2564 T12:  -0.0253
REMARK   3      T13:  -0.1640 T23:   0.0146
REMARK   3    L TENSOR
REMARK   3      L11:   1.7883 L22:   0.8253
REMARK   3      L33:   2.9805 L12:   0.4505
REMARK   3      L13:   0.4492 L23:   0.2459
REMARK   3    S TENSOR
REMARK   3      S11:   0.0092 S12:  -0.1111 S13:  -0.3061
REMARK   3      S21:  -0.1370 S22:  -0.0481 S23:   0.2563
REMARK   3      S31:   0.2197 S32:  -0.5609 S33:   0.0388
REMARK   3
REMARK   3   TLS GROUP : 41
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   F   293        F   346
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2786  78.8267 152.9023
REMARK   3    T TENSOR
REMARK   3      T11:   0.3048 T22:   0.3939
REMARK   3      T33:   0.4044 T12:   0.1280
REMARK   3      T13:  -0.1735 T23:   0.1267
REMARK   3    L TENSOR
REMARK   3      L11:   1.7795 L22:   0.7919
REMARK   3      L33:   2.7011 L12:   0.4350
REMARK   3      L13:  -0.6055 L23:   0.9244
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0827 S12:   0.0348 S13:   0.1183
REMARK   3      S21:  -0.0566 S22:  -0.0523 S23:   0.3792
REMARK   3      S31:   0.0396 S32:  -0.5958 S33:   0.1349
REMARK   3
REMARK   3   TLS GROUP : 42
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   F   355        F   390
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0522  85.7358 156.4400
REMARK   3    T TENSOR
REMARK   3      T11:   0.6232 T22:   0.7432
REMARK   3      T33:   0.7806 T12:  -0.0036
REMARK   3      T13:  -0.0753 T23:   0.0400
REMARK   3    L TENSOR
REMARK   3      L11:   7.7062 L22:   2.2239
REMARK   3      L33:   0.0623 L12:   3.7104
REMARK   3      L13:  -0.4680 L23:  -0.1584
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0905 S12:   0.0510 S13:   0.4650
REMARK   3      S21:  -0.4463 S22:   0.0247 S23:   0.5859
REMARK   3      S31:   0.0054 S32:  -0.0694 S33:   0.0659
REMARK   3
REMARK   3   TLS GROUP : 43
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   F   391        F   490
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8450  73.3922 165.1436
REMARK   3    T TENSOR
REMARK   3      T11:   0.2554 T22:   0.3769
REMARK   3      T33:   0.2341 T12:   0.0062
REMARK   3      T13:  -0.0315 T23:   0.0272
REMARK   3    L TENSOR
REMARK   3      L11:   3.0678 L22:   1.8749
REMARK   3      L33:   2.3430 L12:   0.6745
REMARK   3      L13:   1.5263 L23:   0.0144
REMARK   3    S TENSOR
REMARK   3      S11:   0.0974 S12:  -0.3736 S13:  -0.3047
REMARK   3      S21:   0.2046 S22:  -0.0679 S23:   0.3425
REMARK   3      S31:   0.2649 S32:  -0.5768 S33:  -0.0294
REMARK   3
REMARK   3   TLS GROUP : 44
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   F   491        F   537
REMARK   3    ORIGIN FOR THE GROUP (A):  40.3109  91.5607 164.0846
REMARK   3    T TENSOR
REMARK   3      T11:   0.3781 T22:   0.2282
REMARK   3      T33:   0.2182 T12:   0.0414
REMARK   3      T13:  -0.1340 T23:   0.0321
REMARK   3    L TENSOR
REMARK   3      L11:   2.0531 L22:   5.8528
REMARK   3      L33:   3.3153 L12:   1.5643
REMARK   3      L13:  -0.7420 L23:   2.8088
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0847 S12:  -0.0016 S13:   0.4025
REMARK   3      S21:  -0.6080 S22:   0.2208 S23:  -0.0389
REMARK   3      S31:  -0.6882 S32:   0.3225 S33:  -0.1361
REMARK   3
REMARK   3   TLS GROUP : 45
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   G     1        G   106
REMARK   3    ORIGIN FOR THE GROUP (A):  40.0225 109.7173 133.0392
REMARK   3    T TENSOR
REMARK   3      T11:   0.4683 T22:   0.1407
REMARK   3      T33:   0.1195 T12:   0.1026
REMARK   3      T13:  -0.0559 T23:   0.0288
REMARK   3    L TENSOR
REMARK   3      L11:   3.3969 L22:   1.7847
REMARK   3      L33:   2.2710 L12:   1.0453
REMARK   3      L13:   1.7274 L23:   0.0921
REMARK   3    S TENSOR
REMARK   3      S11:   0.0865 S12:  -0.1359 S13:   0.1939
REMARK   3      S21:   0.0107 S22:  -0.0123 S23:   0.1859
REMARK   3      S31:  -0.2395 S32:   0.0190 S33:  -0.0742
REMARK   3
REMARK   3   TLS GROUP : 46
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   G   107        G   175
REMARK   3    ORIGIN FOR THE GROUP (A):  32.0519 112.4976 120.4744
REMARK   3    T TENSOR
REMARK   3      T11:   0.4449 T22:   0.1470
REMARK   3      T33:   0.2311 T12:   0.1903
REMARK   3      T13:  -0.1260 T23:   0.0025
REMARK   3    L TENSOR
REMARK   3      L11:   2.5122 L22:   2.0145
REMARK   3      L33:   4.7780 L12:   0.6642
REMARK   3      L13:   0.1663 L23:  -0.0905
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0227 S12:   0.2193 S13:   0.1576
REMARK   3      S21:  -0.0076 S22:   0.0234 S23:   0.3334
REMARK   3      S31:  -0.1309 S32:  -0.4094 S33:  -0.0006
REMARK   3
REMARK   3   TLS GROUP : 47
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   G   176        G   286
REMARK   3    ORIGIN FOR THE GROUP (A):  48.2248 121.1553 121.1770
REMARK   3    T TENSOR
REMARK   3      T11:   0.5771 T22:   0.1324
REMARK   3      T33:   0.2491 T12:   0.0616
REMARK   3      T13:  -0.0837 T23:   0.0204
REMARK   3    L TENSOR
REMARK   3      L11:   1.3112 L22:   1.1127
REMARK   3      L33:   0.9179 L12:   0.4132
REMARK   3      L13:  -0.0301 L23:  -0.6381
REMARK   3    S TENSOR
REMARK   3      S11:   0.0423 S12:   0.1683 S13:   0.3438
REMARK   3      S21:   0.0941 S22:  -0.0745 S23:   0.0575
REMARK   3      S31:  -0.3582 S32:   0.0338 S33:   0.0322
REMARK   3
REMARK   3   TLS GROUP : 48
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   G   287        G   346
REMARK   3    ORIGIN FOR THE GROUP (A):  57.9498 115.6595 117.4706
REMARK   3    T TENSOR
REMARK   3      T11:   0.3982 T22:   0.2541
REMARK   3      T33:   0.2670 T12:  -0.0515
REMARK   3      T13:  -0.1530 T23:   0.0319
REMARK   3    L TENSOR
REMARK   3      L11:   0.8770 L22:   2.3064
REMARK   3      L33:   1.9324 L12:  -0.6423
REMARK   3      L13:  -0.4592 L23:  -0.6601
REMARK   3    S TENSOR
REMARK   3      S11:   0.1060 S12:   0.2184 S13:   0.3144
REMARK   3      S21:  -0.2219 S22:  -0.0425 S23:  -0.2434
REMARK   3      S31:  -0.0494 S32:   0.0123 S33:  -0.0634
REMARK   3
REMARK   3   TLS GROUP : 49
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   G   357        G   393
REMARK   3    ORIGIN FOR THE GROUP (A):  58.8343 109.3758 103.7220
REMARK   3    T TENSOR
REMARK   3      T11:   0.7661 T22:   0.8362
REMARK   3      T33:   0.5196 T12:  -0.0885
REMARK   3      T13:  -0.0639 T23:   0.0030
REMARK   3    L TENSOR
REMARK   3      L11:   0.1710 L22:   1.6981
REMARK   3      L33:   6.5133 L12:  -0.3756
REMARK   3      L13:   0.6890 L23:  -2.9760
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0001 S12:   0.2133 S13:  -0.0336
REMARK   3      S21:  -0.4482 S22:  -0.1651 S23:  -0.1919
REMARK   3      S31:   0.7519 S32:  -0.4018 S33:   0.1653
REMARK   3
REMARK   3   TLS GROUP : 50
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   G   394        G   491
REMARK   3    ORIGIN FOR THE GROUP (A):  72.9647 116.2141 118.2041
REMARK   3    T TENSOR
REMARK   3      T11:   0.5387 T22:   0.3628
REMARK   3      T33:   0.3168 T12:  -0.0647
REMARK   3      T13:  -0.0214 T23:   0.1154
REMARK   3    L TENSOR
REMARK   3      L11:   1.2605 L22:   3.2469
REMARK   3      L33:   0.8807 L12:   0.1645
REMARK   3      L13:   0.2610 L23:  -0.6367
REMARK   3    S TENSOR
REMARK   3      S11:   0.0749 S12:   0.2478 S13:   0.3831
REMARK   3      S21:  -0.1015 S22:  -0.1729 S23:  -0.3611
REMARK   3      S31:  -0.1918 S32:   0.5175 S33:   0.0981
REMARK   3
REMARK   3   TLS GROUP : 51
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   G   492        G   537
REMARK   3    ORIGIN FOR THE GROUP (A):  69.6478  95.8632 129.9209
REMARK   3    T TENSOR
REMARK   3      T11:   0.3921 T22:   0.2425
REMARK   3      T33:   0.1387 T12:  -0.0445
REMARK   3      T13:  -0.1705 T23:   0.0340
REMARK   3    L TENSOR
REMARK   3      L11:   1.7621 L22:   7.3560
REMARK   3      L33:   2.3672 L12:  -1.9580
REMARK   3      L13:  -0.9004 L23:   1.2198
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0144 S12:   0.0006 S13:  -0.2139
REMARK   3      S21:   0.1793 S22:  -0.0810 S23:   0.1283
REMARK   3      S31:   0.1090 S32:  -0.1001 S33:   0.0954
REMARK   3
REMARK   3   TLS GROUP : 52
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   H     1        H   106
REMARK   3    ORIGIN FOR THE GROUP (A):  82.4843  98.5096 177.7386
REMARK   3    T TENSOR
REMARK   3      T11:   0.2912 T22:   0.0383
REMARK   3      T33:   0.0320 T12:  -0.0720
REMARK   3      T13:  -0.0308 T23:   0.0100
REMARK   3    L TENSOR
REMARK   3      L11:   3.2949 L22:   1.9046
REMARK   3      L33:   1.7084 L12:  -1.2719
REMARK   3      L13:   0.0704 L23:   0.1734
REMARK   3    S TENSOR
REMARK   3      S11:   0.1403 S12:   0.1900 S13:   0.0871
REMARK   3      S21:  -0.0842 S22:   0.0165 S23:  -0.1334
REMARK   3      S31:  -0.1803 S32:   0.0542 S33:  -0.1568
REMARK   3
REMARK   3   TLS GROUP : 53
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   H   107        H   195
REMARK   3    ORIGIN FOR THE GROUP (A):  90.1703  95.4430 193.2606
REMARK   3    T TENSOR
REMARK   3      T11:   0.3515 T22:   0.1693
REMARK   3      T33:   0.1096 T12:  -0.0659
REMARK   3      T13:  -0.1204 T23:   0.0023
REMARK   3    L TENSOR
REMARK   3      L11:   2.9236 L22:   2.2202
REMARK   3      L33:   3.1309 L12:  -0.6546
REMARK   3      L13:  -0.0641 L23:  -0.0646
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0310 S12:  -0.4709 S13:  -0.0453
REMARK   3      S21:   0.2195 S22:   0.0774 S23:  -0.3047
REMARK   3      S31:   0.1027 S32:   0.4350 S33:  -0.0464
REMARK   3
REMARK   3   TLS GROUP : 54
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   H   196        H   285
REMARK   3    ORIGIN FOR THE GROUP (A):  69.6346 103.6016 191.4634
REMARK   3    T TENSOR
REMARK   3      T11:   0.3671 T22:   0.0070
REMARK   3      T33:   0.0731 T12:  -0.0100
REMARK   3      T13:  -0.0100 T23:  -0.0135
REMARK   3    L TENSOR
REMARK   3      L11:   2.8717 L22:   0.9913
REMARK   3      L33:   1.0788 L12:   0.8316
REMARK   3      L13:  -1.1008 L23:   0.3811
REMARK   3    S TENSOR
REMARK   3      S11:   0.2207 S12:  -0.1176 S13:   0.1749
REMARK   3      S21:  -0.0795 S22:  -0.0420 S23:  -0.0819
REMARK   3      S31:  -0.2469 S32:   0.0357 S33:  -0.1787
REMARK   3
REMARK   3   TLS GROUP : 55
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   H   286        H   346
REMARK   3    ORIGIN FOR THE GROUP (A):  64.0784  96.0236 193.5728
REMARK   3    T TENSOR
REMARK   3      T11:   0.1654 T22:   0.0260
REMARK   3      T33:   0.0625 T12:   0.0374
REMARK   3      T13:  -0.0901 T23:  -0.0254
REMARK   3    L TENSOR
REMARK   3      L11:   3.0304 L22:   2.5633
REMARK   3      L33:   3.5694 L12:   0.9108
REMARK   3      L13:  -1.5402 L23:   0.3380
REMARK   3    S TENSOR
REMARK   3      S11:   0.0097 S12:  -0.1343 S13:   0.0979
REMARK   3      S21:   0.1334 S22:  -0.0074 S23:   0.1049
REMARK   3      S31:  -0.0091 S32:   0.2369 S33:  -0.0022
REMARK   3
REMARK   3   TLS GROUP : 56
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   H   354        H   393
REMARK   3    ORIGIN FOR THE GROUP (A):  63.7727  83.8783 201.2997
REMARK   3    T TENSOR
REMARK   3      T11:   0.6704 T22:   0.2376
REMARK   3      T33:   0.3657 T12:   0.1113
REMARK   3      T13:   0.0486 T23:  -0.0051
REMARK   3    L TENSOR
REMARK   3      L11:   0.1687 L22:   0.3568
REMARK   3      L33:   7.1405 L12:  -0.0597
REMARK   3      L13:   0.5162 L23:   1.0933
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0393 S12:   0.0074 S13:  -0.0678
REMARK   3      S21:   0.2085 S22:   0.2570 S23:  -0.0919
REMARK   3      S31:   0.9817 S32:   1.1125 S33:  -0.2177
REMARK   3
REMARK   3   TLS GROUP : 57
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   H   394        H   504
REMARK   3    ORIGIN FOR THE GROUP (A):  48.7727  95.2389 190.8243
REMARK   3    T TENSOR
REMARK   3      T11:   0.2557 T22:   0.1013
REMARK   3      T33:   0.1928 T12:   0.0709
REMARK   3      T13:   0.0366 T23:   0.0182
REMARK   3    L TENSOR
REMARK   3      L11:   1.3935 L22:   1.7334
REMARK   3      L33:   3.4332 L12:  -0.3258
REMARK   3      L13:   0.9391 L23:   1.1344
REMARK   3    S TENSOR
REMARK   3      S11:   0.1154 S12:  -0.0443 S13:   0.2293
REMARK   3      S21:  -0.0285 S22:  -0.2047 S23:   0.2877
REMARK   3      S31:  -0.2657 S32:  -0.5545 S33:   0.0893
REMARK   3
REMARK   3   TLS GROUP : 58
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   H   505        H   537
REMARK   3    ORIGIN FOR THE GROUP (A):  55.7289  84.4844 171.7650
REMARK   3    T TENSOR
REMARK   3      T11:   0.2338 T22:   0.2859
REMARK   3      T33:   0.2353 T12:   0.0796
REMARK   3      T13:  -0.0772 T23:  -0.1280
REMARK   3    L TENSOR
REMARK   3      L11:   0.4098 L22:   9.6574
REMARK   3      L33:   4.2422 L12:   1.2843
REMARK   3      L13:  -0.5035 L23:   1.8043
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0855 S12:   0.1940 S13:  -0.1648
REMARK   3      S21:  -1.2057 S22:   0.2192 S23:  -0.4160
REMARK   3      S31:  -0.1751 S32:  -0.0486 S33:  -0.1337
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 RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3ODM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB060982.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL11-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03948
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 116208
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.830
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 14.300
REMARK 200  R MERGE                    (I) : 0.13300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.03
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.60
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M SODIUM MALONATE, PH 7.0, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       60.71000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      139.99000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       80.79000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      139.99000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.71000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       80.79000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 72810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, E
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 73150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F, G, H
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G
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   -22
REMARK 465     GLY A   -21
REMARK 465     HIS A   -20
REMARK 465     HIS A   -19
REMARK 465     HIS A   -18
REMARK 465     HIS A   -17
REMARK 465     HIS A   -16
REMARK 465     HIS A   -15
REMARK 465     HIS A   -14
REMARK 465     HIS A   -13
REMARK 465     HIS A   -12
REMARK 465     HIS A   -11
REMARK 465     SER A   -10
REMARK 465     SER A    -9
REMARK 465     GLY A    -8
REMARK 465     HIS A    -7
REMARK 465     ILE A    -6
REMARK 465     ASP A    -5
REMARK 465     ASP A    -4
REMARK 465     ASP A    -3
REMARK 465     ASP A    -2
REMARK 465     LYS A    -1
REMARK 465     HIS A     0
REMARK 465     LYS A   347
REMARK 465     ALA A   348
REMARK 465     LYS A   349
REMARK 465     THR A   350
REMARK 465     GLY A   351
REMARK 465     LEU A   352
REMARK 465     GLU A   353
REMARK 465     TYR A   354
REMARK 465     ASN A   355
REMARK 465     ARG A   356
REMARK 465     GLU A   357
REMARK 465     VAL A   358
REMARK 465     MET B   -22
REMARK 465     GLY B   -21
REMARK 465     HIS B   -20
REMARK 465     HIS B   -19
REMARK 465     HIS B   -18
REMARK 465     HIS B   -17
REMARK 465     HIS B   -16
REMARK 465     HIS B   -15
REMARK 465     HIS B   -14
REMARK 465     HIS B   -13
REMARK 465     HIS B   -12
REMARK 465     HIS B   -11
REMARK 465     SER B   -10
REMARK 465     SER B    -9
REMARK 465     GLY B    -8
REMARK 465     HIS B    -7
REMARK 465     ILE B    -6
REMARK 465     ASP B    -5
REMARK 465     ASP B    -4
REMARK 465     ASP B    -3
REMARK 465     ASP B    -2
REMARK 465     LYS B    -1
REMARK 465     HIS B     0
REMARK 465     LYS B   347
REMARK 465     ALA B   348
REMARK 465     LYS B   349
REMARK 465     THR B   350
REMARK 465     GLY B   351
REMARK 465     LEU B   352
REMARK 465     GLU B   353
REMARK 465     TYR B   354
REMARK 465     MET C   -22
REMARK 465     GLY C   -21
REMARK 465     HIS C   -20
REMARK 465     HIS C   -19
REMARK 465     HIS C   -18
REMARK 465     HIS C   -17
REMARK 465     HIS C   -16
REMARK 465     HIS C   -15
REMARK 465     HIS C   -14
REMARK 465     HIS C   -13
REMARK 465     HIS C   -12
REMARK 465     HIS C   -11
REMARK 465     SER C   -10
REMARK 465     SER C    -9
REMARK 465     GLY C    -8
REMARK 465     HIS C    -7
REMARK 465     ILE C    -6
REMARK 465     ASP C    -5
REMARK 465     ASP C    -4
REMARK 465     ASP C    -3
REMARK 465     ASP C    -2
REMARK 465     LYS C    -1
REMARK 465     HIS C     0
REMARK 465     LYS C   349
REMARK 465     THR C   350
REMARK 465     GLY C   351
REMARK 465     LEU C   352
REMARK 465     GLU C   353
REMARK 465     TYR C   354
REMARK 465     ASN C   355
REMARK 465     MET D   -22
REMARK 465     GLY D   -21
REMARK 465     HIS D   -20
REMARK 465     HIS D   -19
REMARK 465     HIS D   -18
REMARK 465     HIS D   -17
REMARK 465     HIS D   -16
REMARK 465     HIS D   -15
REMARK 465     HIS D   -14
REMARK 465     HIS D   -13
REMARK 465     HIS D   -12
REMARK 465     HIS D   -11
REMARK 465     SER D   -10
REMARK 465     SER D    -9
REMARK 465     GLY D    -8
REMARK 465     HIS D    -7
REMARK 465     ILE D    -6
REMARK 465     ASP D    -5
REMARK 465     ASP D    -4
REMARK 465     ASP D    -3
REMARK 465     ASP D    -2
REMARK 465     LYS D    -1
REMARK 465     HIS D     0
REMARK 465     LYS D   347
REMARK 465     ALA D   348
REMARK 465     LYS D   349
REMARK 465     THR D   350
REMARK 465     GLY D   351
REMARK 465     LEU D   352
REMARK 465     GLU D   353
REMARK 465     TYR D   354
REMARK 465     ASN D   355
REMARK 465     ARG D   356
REMARK 465     GLU D   357
REMARK 465     MET E   -22
REMARK 465     GLY E   -21
REMARK 465     HIS E   -20
REMARK 465     HIS E   -19
REMARK 465     HIS E   -18
REMARK 465     HIS E   -17
REMARK 465     HIS E   -16
REMARK 465     HIS E   -15
REMARK 465     HIS E   -14
REMARK 465     HIS E   -13
REMARK 465     HIS E   -12
REMARK 465     HIS E   -11
REMARK 465     SER E   -10
REMARK 465     SER E    -9
REMARK 465     GLY E    -8
REMARK 465     HIS E    -7
REMARK 465     ILE E    -6
REMARK 465     ASP E    -5
REMARK 465     ASP E    -4
REMARK 465     ASP E    -3
REMARK 465     ASP E    -2
REMARK 465     LYS E    -1
REMARK 465     HIS E     0
REMARK 465     LYS E   347
REMARK 465     ALA E   348
REMARK 465     LYS E   349
REMARK 465     THR E   350
REMARK 465     GLY E   351
REMARK 465     LEU E   352
REMARK 465     GLU E   353
REMARK 465     TYR E   354
REMARK 465     ASN E   355
REMARK 465     ARG E   356
REMARK 465     GLU E   357
REMARK 465     VAL E   358
REMARK 465     ALA E   359
REMARK 465     MET F   -22
REMARK 465     GLY F   -21
REMARK 465     HIS F   -20
REMARK 465     HIS F   -19
REMARK 465     HIS F   -18
REMARK 465     HIS F   -17
REMARK 465     HIS F   -16
REMARK 465     HIS F   -15
REMARK 465     HIS F   -14
REMARK 465     HIS F   -13
REMARK 465     HIS F   -12
REMARK 465     HIS F   -11
REMARK 465     SER F   -10
REMARK 465     SER F    -9
REMARK 465     GLY F    -8
REMARK 465     HIS F    -7
REMARK 465     ILE F    -6
REMARK 465     ASP F    -5
REMARK 465     ASP F    -4
REMARK 465     ASP F    -3
REMARK 465     ASP F    -2
REMARK 465     LYS F    -1
REMARK 465     HIS F     0
REMARK 465     LYS F   347
REMARK 465     ALA F   348
REMARK 465     LYS F   349
REMARK 465     THR F   350
REMARK 465     GLY F   351
REMARK 465     LEU F   352
REMARK 465     GLU F   353
REMARK 465     TYR F   354
REMARK 465     MET G   -22
REMARK 465     GLY G   -21
REMARK 465     HIS G   -20
REMARK 465     HIS G   -19
REMARK 465     HIS G   -18
REMARK 465     HIS G   -17
REMARK 465     HIS G   -16
REMARK 465     HIS G   -15
REMARK 465     HIS G   -14
REMARK 465     HIS G   -13
REMARK 465     HIS G   -12
REMARK 465     HIS G   -11
REMARK 465     SER G   -10
REMARK 465     SER G    -9
REMARK 465     GLY G    -8
REMARK 465     HIS G    -7
REMARK 465     ILE G    -6
REMARK 465     ASP G    -5
REMARK 465     ASP G    -4
REMARK 465     ASP G    -3
REMARK 465     ASP G    -2
REMARK 465     LYS G    -1
REMARK 465     HIS G     0
REMARK 465     LYS G   347
REMARK 465     ALA G   348
REMARK 465     LYS G   349
REMARK 465     THR G   350
REMARK 465     GLY G   351
REMARK 465     LEU G   352
REMARK 465     GLU G   353
REMARK 465     TYR G   354
REMARK 465     ASN G   355
REMARK 465     ARG G   356
REMARK 465     MET H   -22
REMARK 465     GLY H   -21
REMARK 465     HIS H   -20
REMARK 465     HIS H   -19
REMARK 465     HIS H   -18
REMARK 465     HIS H   -17
REMARK 465     HIS H   -16
REMARK 465     HIS H   -15
REMARK 465     HIS H   -14
REMARK 465     HIS H   -13
REMARK 465     HIS H   -12
REMARK 465     HIS H   -11
REMARK 465     SER H   -10
REMARK 465     SER H    -9
REMARK 465     GLY H    -8
REMARK 465     HIS H    -7
REMARK 465     ILE H    -6
REMARK 465     ASP H    -5
REMARK 465     ASP H    -4
REMARK 465     ASP H    -3
REMARK 465     ASP H    -2
REMARK 465     LYS H    -1
REMARK 465     HIS H     0
REMARK 465     LYS H   347
REMARK 465     ALA H   348
REMARK 465     LYS H   349
REMARK 465     THR H   350
REMARK 465     GLY H   351
REMARK 465     LEU H   352
REMARK 465     GLU H   353
REMARK 465     ASP H   381
REMARK 465     ASN H   382
REMARK 465     SER H   383
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     LYS B 340    CG   CD   CE   NZ
REMARK 470     ASN B 355    CG   OD1
REMARK 470     VAL B 358    CG1  CG2
REMARK 470     LYS B 369    CD   CE   NZ
REMARK 470     ALA C 348    C    O    CB
REMARK 470     ARG C 356    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL C 358    CG1  CG2
REMARK 470     ARG C 390    CD   NE   CZ   NH1  NH2
REMARK 470     LYS E 192    CG   CD   CE   NZ
REMARK 470     ARG F 175    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASN F 355    CG   OD1
REMARK 470     ARG F 356    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL F 358    CG1  CG2
REMARK 470     LYS F 384    CG   CD   CE   NZ
REMARK 470     GLU G 357    CG   CD   OE1  OE2
REMARK 470     VAL G 358    CG1  CG2
REMARK 470     ASN H 355    CG   OD1
REMARK 470     LYS H 384    CG   CD   CE   NZ
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 E     5    AU    AUC E   605              1.32
REMARK 500   SG   CYS A     5    AU    AUC A   608              1.54
REMARK 500   SG   CYS B     5    AU    AUC B   609              1.56
REMARK 500   SG   CYS D     5    AU    AUC D   604              1.64
REMARK 500   SG   CYS C     5    AU    AUC C   601              1.65
REMARK 500   OE1  GLU H   279    AU    AUC H   617              1.71
REMARK 500   OH   TYR C    18     OD2  ASP C   343              2.05
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   5   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES
REMARK 500    CYS G   5   CA  -  CB  -  SG  ANGL. DEV. =   8.6 DEGREES
REMARK 500    CYS H   5   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    PRO A  12       47.04    -83.69
REMARK 500    LEU A  53       31.49    -86.99
REMARK 500    GLU A  89     -144.99   -107.34
REMARK 500    ASN A 300       73.35     47.60
REMARK 500    ASN A 341       31.05    -90.78
REMARK 500    ASP A 366       -8.19    -53.58
REMARK 500    SER A 379       61.43   -104.86
REMARK 500    ASP A 381      107.70    -57.82
REMARK 500    SER A 383       38.25    -67.63
REMARK 500    LYS A 454       -6.36     78.98
REMARK 500    ILE A 455      -63.36   -100.97
REMARK 500    ASN A 476       59.66     32.96
REMARK 500    PRO B  12       45.52    -89.50
REMARK 500    LEU B  53       30.52    -74.78
REMARK 500    LYS B  75      -63.56   -124.89
REMARK 500    GLU B  89     -104.09    -81.16
REMARK 500    GLU B 126      -39.86   -133.45
REMARK 500    ALA B 171      -75.64    -83.47
REMARK 500    ASN B 172       55.88    -69.91
REMARK 500    ASN B 300       73.03     31.94
REMARK 500    ASP B 366      -15.58    -49.99
REMARK 500    ASN B 448      113.05   -163.17
REMARK 500    LYS B 454        6.33     90.08
REMARK 500    ASN B 476       70.57     36.69
REMARK 500    LYS C   2      163.18    -44.91
REMARK 500    PRO C  12       40.73    -81.02
REMARK 500    LEU C  53       36.19    -77.65
REMARK 500    GLU C  89     -112.63    -79.83
REMARK 500    GLU C 126      -61.16   -130.67
REMARK 500    GLU C 130      -54.79    -24.65
REMARK 500    ASN C 172       28.49   -140.84
REMARK 500    ALA C 294        0.34    -53.44
REMARK 500    ASN C 300       76.42     65.72
REMARK 500    ASN C 341       42.74   -101.41
REMARK 500    THR C 346       80.86    -15.96
REMARK 500    LYS C 347       49.82    173.59
REMARK 500    GLU C 357      126.16    155.87
REMARK 500    VAL C 372       -1.49    -59.88
REMARK 500    ILE C 377      -74.46    -72.07
REMARK 500    ASN C 382       35.06   -147.52
REMARK 500    GLU C 385       55.33    -60.18
REMARK 500    GLU C 424      -57.61    -20.87
REMARK 500    ASN C 476       52.07     27.78
REMARK 500    GLU C 509      -55.60    -25.65
REMARK 500    PRO D  12       47.03    -88.49
REMARK 500    PRO D  34      154.48    -49.38
REMARK 500    LEU D  53       34.98    -81.94
REMARK 500    GLU D  89     -116.46   -105.72
REMARK 500    ASN D 156       18.88     51.50
REMARK 500    ASN D 172       59.31   -110.68
REMARK 500
REMARK 500 THIS ENTRY HAS     119 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     AUC A  608
REMARK 610     AUC A  624
REMARK 610     AUC B  630
REMARK 610     AUC B  609
REMARK 610     AUC B  622
REMARK 610     AUC B  638
REMARK 610     AUC B  640
REMARK 610     AUC C  635
REMARK 610     AUC C  601
REMARK 610     AUC C  621
REMARK 610     AUC C  634
REMARK 610     AUC D  604
REMARK 610     AUC D  618
REMARK 610     AUC D  640
REMARK 610     AUC E  605
REMARK 610     AUC E  619
REMARK 610     AUC E  628
REMARK 610     AUC F  637
REMARK 610     AUC F  613
REMARK 610     AUC F  620
REMARK 610     AUC F  627
REMARK 610     AUC F  641
REMARK 610     AUC G  616
REMARK 610     AUC G  626
REMARK 610     AUC H  612
REMARK 610     AUC H  617
REMARK 610     AUC H  629
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                             AUC G 615  AU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G  48   OD2
REMARK 620 2 AUC G 615   C1  101.5
REMARK 620 3 AUC G 615   C2   77.6 177.4
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             AUC F 637  AU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET F 144   SD
REMARK 620 2 MET G 144   SD  152.0
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC A 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC B 630
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC A 631
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC C 635
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC F 637
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC B 638
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC B 640
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC C 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC C 634
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC D 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC D 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC D 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC D 640
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI D 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI E 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC F 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC F 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC F 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC F 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC F 641
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC G 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC G 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC G 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC H 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC H 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC H 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC H 629
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI H 901
DBREF  3ODM A    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537
DBREF  3ODM B    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537
DBREF  3ODM C    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537
DBREF  3ODM D    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537
DBREF  3ODM E    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537
DBREF  3ODM F    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537
DBREF  3ODM G    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537
DBREF  3ODM H    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537
SEQADV 3ODM MET A  -22  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY A  -21  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS A  -20  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS A  -19  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS A  -18  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS A  -17  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS A  -16  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS A  -15  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS A  -14  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS A  -13  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS A  -12  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS A  -11  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER A  -10  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER A   -9  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY A   -8  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS A   -7  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ILE A   -6  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP A   -5  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP A   -4  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP A   -3  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP A   -2  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM LYS A   -1  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS A    0  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM MET B  -22  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY B  -21  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS B  -20  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS B  -19  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS B  -18  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS B  -17  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS B  -16  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS B  -15  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS B  -14  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS B  -13  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS B  -12  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS B  -11  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER B  -10  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER B   -9  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY B   -8  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS B   -7  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ILE B   -6  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP B   -5  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP B   -4  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP B   -3  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP B   -2  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM LYS B   -1  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS B    0  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM MET C  -22  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY C  -21  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS C  -20  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS C  -19  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS C  -18  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS C  -17  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS C  -16  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS C  -15  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS C  -14  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS C  -13  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS C  -12  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS C  -11  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER C  -10  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER C   -9  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY C   -8  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS C   -7  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ILE C   -6  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP C   -5  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP C   -4  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP C   -3  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP C   -2  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM LYS C   -1  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS C    0  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM MET D  -22  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY D  -21  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS D  -20  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS D  -19  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS D  -18  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS D  -17  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS D  -16  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS D  -15  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS D  -14  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS D  -13  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS D  -12  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS D  -11  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER D  -10  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER D   -9  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY D   -8  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS D   -7  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ILE D   -6  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP D   -5  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP D   -4  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP D   -3  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP D   -2  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM LYS D   -1  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS D    0  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM MET E  -22  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY E  -21  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS E  -20  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS E  -19  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS E  -18  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS E  -17  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS E  -16  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS E  -15  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS E  -14  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS E  -13  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS E  -12  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS E  -11  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER E  -10  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER E   -9  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY E   -8  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS E   -7  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ILE E   -6  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP E   -5  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP E   -4  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP E   -3  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP E   -2  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM LYS E   -1  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS E    0  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM MET F  -22  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY F  -21  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS F  -20  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS F  -19  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS F  -18  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS F  -17  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS F  -16  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS F  -15  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS F  -14  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS F  -13  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS F  -12  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS F  -11  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER F  -10  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER F   -9  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY F   -8  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS F   -7  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ILE F   -6  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP F   -5  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP F   -4  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP F   -3  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP F   -2  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM LYS F   -1  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS F    0  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM MET G  -22  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY G  -21  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS G  -20  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS G  -19  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS G  -18  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS G  -17  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS G  -16  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS G  -15  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS G  -14  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS G  -13  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS G  -12  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS G  -11  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER G  -10  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER G   -9  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY G   -8  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS G   -7  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ILE G   -6  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP G   -5  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP G   -4  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP G   -3  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP G   -2  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM LYS G   -1  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS G    0  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM MET H  -22  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY H  -21  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS H  -20  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS H  -19  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS H  -18  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS H  -17  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS H  -16  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS H  -15  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS H  -14  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS H  -13  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS H  -12  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS H  -11  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER H  -10  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM SER H   -9  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM GLY H   -8  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS H   -7  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ILE H   -6  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP H   -5  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP H   -4  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP H   -3  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM ASP H   -2  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM LYS H   -1  UNP  Q8XLE8              EXPRESSION TAG
SEQADV 3ODM HIS H    0  UNP  Q8XLE8              EXPRESSION TAG
SEQRES   1 A  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES   2 A  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE
SEQRES   3 A  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU
SEQRES   4 A  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE
SEQRES   5 A  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE
SEQRES   6 A  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO
SEQRES   7 A  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER
SEQRES   8 A  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO
SEQRES   9 A  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN
SEQRES  10 A  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN
SEQRES  11 A  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL
SEQRES  12 A  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU
SEQRES  13 A  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN
SEQRES  14 A  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG
SEQRES  15 A  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN
SEQRES  16 A  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS
SEQRES  17 A  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE
SEQRES  18 A  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER
SEQRES  19 A  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR
SEQRES  20 A  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE
SEQRES  21 A  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER
SEQRES  22 A  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY
SEQRES  23 A  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP
SEQRES  24 A  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU
SEQRES  25 A  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER
SEQRES  26 A  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE
SEQRES  27 A  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE
SEQRES  28 A  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN
SEQRES  29 A  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR
SEQRES  30 A  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU
SEQRES  31 A  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE
SEQRES  32 A  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER
SEQRES  33 A  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU
SEQRES  34 A  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR
SEQRES  35 A  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE
SEQRES  36 A  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG
SEQRES  37 A  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU
SEQRES  38 A  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL
SEQRES  39 A  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU
SEQRES  40 A  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR
SEQRES  41 A  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN
SEQRES  42 A  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN
SEQRES  43 A  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE
SEQRES  44 A  560  GLY
SEQRES   1 B  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES   2 B  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE
SEQRES   3 B  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU
SEQRES   4 B  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE
SEQRES   5 B  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE
SEQRES   6 B  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO
SEQRES   7 B  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER
SEQRES   8 B  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO
SEQRES   9 B  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN
SEQRES  10 B  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN
SEQRES  11 B  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL
SEQRES  12 B  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU
SEQRES  13 B  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN
SEQRES  14 B  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG
SEQRES  15 B  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN
SEQRES  16 B  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS
SEQRES  17 B  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE
SEQRES  18 B  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER
SEQRES  19 B  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR
SEQRES  20 B  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE
SEQRES  21 B  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER
SEQRES  22 B  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY
SEQRES  23 B  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP
SEQRES  24 B  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU
SEQRES  25 B  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER
SEQRES  26 B  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE
SEQRES  27 B  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE
SEQRES  28 B  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN
SEQRES  29 B  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR
SEQRES  30 B  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU
SEQRES  31 B  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE
SEQRES  32 B  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER
SEQRES  33 B  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU
SEQRES  34 B  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR
SEQRES  35 B  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE
SEQRES  36 B  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG
SEQRES  37 B  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU
SEQRES  38 B  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL
SEQRES  39 B  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU
SEQRES  40 B  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR
SEQRES  41 B  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN
SEQRES  42 B  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN
SEQRES  43 B  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE
SEQRES  44 B  560  GLY
SEQRES   1 C  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES   2 C  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE
SEQRES   3 C  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU
SEQRES   4 C  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE
SEQRES   5 C  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE
SEQRES   6 C  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO
SEQRES   7 C  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER
SEQRES   8 C  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO
SEQRES   9 C  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN
SEQRES  10 C  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN
SEQRES  11 C  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL
SEQRES  12 C  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU
SEQRES  13 C  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN
SEQRES  14 C  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG
SEQRES  15 C  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN
SEQRES  16 C  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS
SEQRES  17 C  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE
SEQRES  18 C  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER
SEQRES  19 C  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR
SEQRES  20 C  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE
SEQRES  21 C  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER
SEQRES  22 C  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY
SEQRES  23 C  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP
SEQRES  24 C  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU
SEQRES  25 C  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER
SEQRES  26 C  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE
SEQRES  27 C  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE
SEQRES  28 C  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN
SEQRES  29 C  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR
SEQRES  30 C  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU
SEQRES  31 C  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE
SEQRES  32 C  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER
SEQRES  33 C  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU
SEQRES  34 C  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR
SEQRES  35 C  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE
SEQRES  36 C  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG
SEQRES  37 C  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU
SEQRES  38 C  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL
SEQRES  39 C  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU
SEQRES  40 C  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR
SEQRES  41 C  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN
SEQRES  42 C  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN
SEQRES  43 C  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE
SEQRES  44 C  560  GLY
SEQRES   1 D  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES   2 D  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE
SEQRES   3 D  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU
SEQRES   4 D  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE
SEQRES   5 D  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE
SEQRES   6 D  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO
SEQRES   7 D  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER
SEQRES   8 D  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO
SEQRES   9 D  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN
SEQRES  10 D  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN
SEQRES  11 D  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL
SEQRES  12 D  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU
SEQRES  13 D  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN
SEQRES  14 D  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG
SEQRES  15 D  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN
SEQRES  16 D  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS
SEQRES  17 D  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE
SEQRES  18 D  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER
SEQRES  19 D  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR
SEQRES  20 D  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE
SEQRES  21 D  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER
SEQRES  22 D  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY
SEQRES  23 D  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP
SEQRES  24 D  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU
SEQRES  25 D  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER
SEQRES  26 D  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE
SEQRES  27 D  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE
SEQRES  28 D  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN
SEQRES  29 D  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR
SEQRES  30 D  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU
SEQRES  31 D  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE
SEQRES  32 D  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER
SEQRES  33 D  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU
SEQRES  34 D  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR
SEQRES  35 D  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE
SEQRES  36 D  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG
SEQRES  37 D  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU
SEQRES  38 D  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL
SEQRES  39 D  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU
SEQRES  40 D  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR
SEQRES  41 D  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN
SEQRES  42 D  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN
SEQRES  43 D  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE
SEQRES  44 D  560  GLY
SEQRES   1 E  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES   2 E  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE
SEQRES   3 E  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU
SEQRES   4 E  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE
SEQRES   5 E  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE
SEQRES   6 E  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO
SEQRES   7 E  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER
SEQRES   8 E  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO
SEQRES   9 E  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN
SEQRES  10 E  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN
SEQRES  11 E  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL
SEQRES  12 E  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU
SEQRES  13 E  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN
SEQRES  14 E  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG
SEQRES  15 E  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN
SEQRES  16 E  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS
SEQRES  17 E  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE
SEQRES  18 E  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER
SEQRES  19 E  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR
SEQRES  20 E  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE
SEQRES  21 E  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER
SEQRES  22 E  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY
SEQRES  23 E  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP
SEQRES  24 E  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU
SEQRES  25 E  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER
SEQRES  26 E  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE
SEQRES  27 E  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE
SEQRES  28 E  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN
SEQRES  29 E  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR
SEQRES  30 E  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU
SEQRES  31 E  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE
SEQRES  32 E  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER
SEQRES  33 E  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU
SEQRES  34 E  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR
SEQRES  35 E  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE
SEQRES  36 E  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG
SEQRES  37 E  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU
SEQRES  38 E  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL
SEQRES  39 E  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU
SEQRES  40 E  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR
SEQRES  41 E  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN
SEQRES  42 E  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN
SEQRES  43 E  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE
SEQRES  44 E  560  GLY
SEQRES   1 F  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES   2 F  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE
SEQRES   3 F  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU
SEQRES   4 F  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE
SEQRES   5 F  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE
SEQRES   6 F  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO
SEQRES   7 F  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER
SEQRES   8 F  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO
SEQRES   9 F  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN
SEQRES  10 F  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN
SEQRES  11 F  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL
SEQRES  12 F  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU
SEQRES  13 F  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN
SEQRES  14 F  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG
SEQRES  15 F  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN
SEQRES  16 F  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS
SEQRES  17 F  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE
SEQRES  18 F  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER
SEQRES  19 F  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR
SEQRES  20 F  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE
SEQRES  21 F  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER
SEQRES  22 F  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY
SEQRES  23 F  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP
SEQRES  24 F  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU
SEQRES  25 F  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER
SEQRES  26 F  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE
SEQRES  27 F  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE
SEQRES  28 F  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN
SEQRES  29 F  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR
SEQRES  30 F  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU
SEQRES  31 F  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE
SEQRES  32 F  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER
SEQRES  33 F  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU
SEQRES  34 F  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR
SEQRES  35 F  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE
SEQRES  36 F  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG
SEQRES  37 F  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU
SEQRES  38 F  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL
SEQRES  39 F  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU
SEQRES  40 F  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR
SEQRES  41 F  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN
SEQRES  42 F  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN
SEQRES  43 F  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE
SEQRES  44 F  560  GLY
SEQRES   1 G  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES   2 G  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE
SEQRES   3 G  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU
SEQRES   4 G  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE
SEQRES   5 G  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE
SEQRES   6 G  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO
SEQRES   7 G  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER
SEQRES   8 G  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO
SEQRES   9 G  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN
SEQRES  10 G  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN
SEQRES  11 G  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL
SEQRES  12 G  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU
SEQRES  13 G  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN
SEQRES  14 G  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG
SEQRES  15 G  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN
SEQRES  16 G  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS
SEQRES  17 G  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE
SEQRES  18 G  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER
SEQRES  19 G  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR
SEQRES  20 G  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE
SEQRES  21 G  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER
SEQRES  22 G  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY
SEQRES  23 G  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP
SEQRES  24 G  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU
SEQRES  25 G  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER
SEQRES  26 G  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE
SEQRES  27 G  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE
SEQRES  28 G  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN
SEQRES  29 G  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR
SEQRES  30 G  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU
SEQRES  31 G  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE
SEQRES  32 G  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER
SEQRES  33 G  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU
SEQRES  34 G  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR
SEQRES  35 G  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE
SEQRES  36 G  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG
SEQRES  37 G  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU
SEQRES  38 G  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL
SEQRES  39 G  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU
SEQRES  40 G  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR
SEQRES  41 G  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN
SEQRES  42 G  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN
SEQRES  43 G  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE
SEQRES  44 G  560  GLY
SEQRES   1 H  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES   2 H  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE
SEQRES   3 H  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU
SEQRES   4 H  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE
SEQRES   5 H  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE
SEQRES   6 H  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO
SEQRES   7 H  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER
SEQRES   8 H  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO
SEQRES   9 H  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN
SEQRES  10 H  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN
SEQRES  11 H  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL
SEQRES  12 H  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU
SEQRES  13 H  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN
SEQRES  14 H  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG
SEQRES  15 H  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN
SEQRES  16 H  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS
SEQRES  17 H  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE
SEQRES  18 H  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER
SEQRES  19 H  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR
SEQRES  20 H  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE
SEQRES  21 H  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER
SEQRES  22 H  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY
SEQRES  23 H  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP
SEQRES  24 H  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU
SEQRES  25 H  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER
SEQRES  26 H  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE
SEQRES  27 H  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE
SEQRES  28 H  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN
SEQRES  29 H  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR
SEQRES  30 H  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU
SEQRES  31 H  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE
SEQRES  32 H  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER
SEQRES  33 H  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU
SEQRES  34 H  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR
SEQRES  35 H  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE
SEQRES  36 H  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG
SEQRES  37 H  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU
SEQRES  38 H  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL
SEQRES  39 H  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU
SEQRES  40 H  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR
SEQRES  41 H  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN
SEQRES  42 H  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN
SEQRES  43 H  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE
SEQRES  44 H  560  GLY
HET    AUC  A 607       5
HET    AUC  A 608       1
HET    AUC  A 624       1
HET    AUC  A 631       5
HET    MLI  A 901       7
HET    AUC  B 630       1
HET    AUC  B 609       1
HET    AUC  B 610       5
HET    AUC  B 622       1
HET    AUC  B 638       1
HET    AUC  B 640       1
HET    AUC  C 635       1
HET    AUC  C 601       1
HET    AUC  C 602       5
HET    AUC  C 621       1
HET    AUC  C 634       1
HET    MLI  C 901       7
HET    AUC  D 603       5
HET    AUC  D 604       1
HET    AUC  D 618       1
HET    AUC  D 640       1
HET    MLI  D 901       7
HET    AUC  E 605       1
HET    AUC  E 606       5
HET    AUC  E 619       1
HET    AUC  E 628       1
HET    MLI  E 901       7
HET    AUC  F 637       1
HET    AUC  F 613       1
HET    AUC  F 614       5
HET    AUC  F 620       1
HET    AUC  F 627       1
HET    AUC  F 641       1
HET    AUC  G 615       5
HET    AUC  G 616       1
HET    AUC  G 626       1
HET    AUC  H 611       5
HET    AUC  H 612       1
HET    AUC  H 617       1
HET    AUC  H 629       1
HET    MLI  H 901       7
HETNAM     AUC GOLD (I) CYANIDE ION
HETNAM     MLI MALONATE ION
FORMUL   9  AUC    36(C2 AU N2)
FORMUL  13  MLI    5(C3 H2 O4 2-)
FORMUL  50  HOH   *200(H2 O)
HELIX    1   1 GLN A   23  LEU A   32  1                                  10
HELIX    2   2 PRO A   34  GLY A   38  5                                   5
HELIX    3   3 HIS A   57  SER A   68  1                                  12
HELIX    4   4 SER A   90  GLY A  113  1                                  24
HELIX    5   5 THR A  127  TYR A  149  1                                  23
HELIX    6   6 ASP A  166  ASN A  172  1                                   7
HELIX    7   7 ILE A  173  LYS A  187  1                                  15
HELIX    8   8 ARG A  200  GLY A  208  1                                   9
HELIX    9   9 GLY A  208  GLY A  231  1                                  24
HELIX   10  10 LEU A  243  GLY A  247  5                                   5
HELIX   11  11 ASN A  253  TYR A  261  1                                   9
HELIX   12  12 GLN A  270  ASP A  276  1                                   7
HELIX   13  13 GLY A  278  ILE A  293  1                                  16
HELIX   14  14 ALA A  294  SER A  296  5                                   3
HELIX   15  15 SER A  302  ASP A  336  1                                  35
HELIX   16  16 ASN A  360  ASP A  366  1                                   7
HELIX   17  17 ASP A  370  SER A  379  1                                  10
HELIX   18  18 ARG A  390  LEU A  401  1                                  12
HELIX   19  19 PRO A  404  MET A  408  5                                   5
HELIX   20  20 GLY A  409  GLY A  422  1                                  14
HELIX   21  21 GLY A  422  TYR A  433  1                                  12
HELIX   22  22 ILE A  435  ARG A  445  1                                  11
HELIX   23  23 ASP A  457  LEU A  475  1                                  19
HELIX   24  24 ASP A  480  GLU A  488  1                                   9
HELIX   25  25 GLU A  488  LEU A  507  1                                  20
HELIX   26  26 GLU A  508  SER A  515  1                                   8
HELIX   27  27 SER A  515  GLY A  534  1                                  20
HELIX   28  28 GLN B   23  THR B   33  1                                  11
HELIX   29  29 PRO B   34  GLY B   38  5                                   5
HELIX   30  30 HIS B   57  SER B   68  1                                  12
HELIX   31  31 SER B   90  GLY B  113  1                                  24
HELIX   32  32 THR B  127  TYR B  149  1                                  23
HELIX   33  33 ASP B  166  ASN B  172  1                                   7
HELIX   34  34 ASN B  172  LYS B  187  1                                  16
HELIX   35  35 ARG B  200  GLY B  208  1                                   9
HELIX   36  36 GLY B  208  GLY B  231  1                                  24
HELIX   37  37 LEU B  243  GLY B  247  5                                   5
HELIX   38  38 SER B  250  GLU B  252  5                                   3
HELIX   39  39 ASN B  253  TYR B  261  1                                   9
HELIX   40  40 GLN B  270  ASP B  276  1                                   7
HELIX   41  41 HIS B  277  ILE B  293  1                                  17
HELIX   42  42 ALA B  294  SER B  296  5                                   3
HELIX   43  43 SER B  302  ASP B  336  1                                  35
HELIX   44  44 LEU B  361  ASP B  366  1                                   6
HELIX   45  45 ASP B  370  SER B  379  1                                  10
HELIX   46  46 ARG B  390  LEU B  401  1                                  12
HELIX   47  47 GLY B  409  TYR B  433  1                                  25
HELIX   48  48 ILE B  435  ARG B  445  1                                  11
HELIX   49  49 ASP B  457  LEU B  475  1                                  19
HELIX   50  50 ASP B  480  GLU B  488  1                                   9
HELIX   51  51 GLU B  488  GLY B  506  1                                  19
HELIX   52  52 GLU B  508  SER B  515  1                                   8
HELIX   53  53 SER B  515  GLY B  534  1                                  20
HELIX   54  54 GLN C   23  THR C   33  1                                  11
HELIX   55  55 PRO C   34  GLY C   38  5                                   5
HELIX   56  56 HIS C   57  ASN C   69  1                                  13
HELIX   57  57 SER C   90  GLY C  113  1                                  24
HELIX   58  58 THR C  127  TYR C  149  1                                  23
HELIX   59  59 ASN C  172  LYS C  187  1                                  16
HELIX   60  60 ARG C  200  GLY C  208  1                                   9
HELIX   61  61 GLY C  208  GLY C  231  1                                  24
HELIX   62  62 LEU C  243  GLY C  247  5                                   5
HELIX   63  63 ASN C  253  TYR C  261  1                                   9
HELIX   64  64 GLN C  270  ASP C  276  1                                   7
HELIX   65  65 GLY C  278  ALA C  294  1                                  17
HELIX   66  66 SER C  302  ASP C  336  1                                  35
HELIX   67  67 LEU C  361  ASP C  366  1                                   6
HELIX   68  68 ASP C  370  ILE C  380  1                                  11
HELIX   69  69 ARG C  390  LEU C  401  1                                  12
HELIX   70  70 GLY C  409  TYR C  433  1                                  25
HELIX   71  71 ILE C  435  ARG C  445  1                                  11
HELIX   72  72 ASP C  457  LEU C  475  1                                  19
HELIX   73  73 ASP C  482  GLU C  488  1                                   7
HELIX   74  74 GLU C  488  GLY C  506  1                                  19
HELIX   75  75 GLU C  508  SER C  515  1                                   8
HELIX   76  76 SER C  515  GLY C  534  1                                  20
HELIX   77  77 SER D   20  GLN D   22  5                                   3
HELIX   78  78 GLN D   23  THR D   33  1                                  11
HELIX   79  79 PRO D   34  GLY D   38  5                                   5
HELIX   80  80 HIS D   57  ASN D   69  1                                  13
HELIX   81  81 SER D   90  GLY D  113  1                                  24
HELIX   82  82 THR D  127  TYR D  149  1                                  23
HELIX   83  83 ASP D  166  ASN D  172  1                                   7
HELIX   84  84 ASN D  172  SER D  186  1                                  15
HELIX   85  85 ARG D  200  GLY D  208  1                                   9
HELIX   86  86 GLY D  208  HIS D  230  1                                  23
HELIX   87  87 LEU D  243  GLY D  247  5                                   5
HELIX   88  88 ASN D  253  TYR D  261  1                                   9
HELIX   89  89 GLN D  270  ASP D  276  1                                   7
HELIX   90  90 GLY D  278  ILE D  293  1                                  16
HELIX   91  91 ALA D  294  SER D  296  5                                   3
HELIX   92  92 SER D  302  ASP D  336  1                                  35
HELIX   93  93 ASN D  360  ASP D  366  1                                   7
HELIX   94  94 ASP D  370  SER D  379  1                                  10
HELIX   95  95 ARG D  390  LEU D  401  1                                  12
HELIX   96  96 PRO D  404  MET D  408  5                                   5
HELIX   97  97 GLY D  409  TYR D  433  1                                  25
HELIX   98  98 ILE D  435  ARG D  445  1                                  11
HELIX   99  99 ASP D  457  LEU D  475  1                                  19
HELIX  100 100 ASP D  480  GLU D  488  1                                   9
HELIX  101 101 GLU D  488  GLY D  506  1                                  19
HELIX  102 102 GLU D  508  SER D  515  1                                   8
HELIX  103 103 SER D  515  GLY D  534  1                                  20
HELIX  104 104 SER E   20  GLN E   22  5                                   3
HELIX  105 105 GLN E   23  THR E   33  1                                  11
HELIX  106 106 PRO E   34  GLY E   38  5                                   5
HELIX  107 107 HIS E   57  SER E   68  1                                  12
HELIX  108 108 SER E   90  GLY E  113  1                                  24
HELIX  109 109 THR E  127  TYR E  149  1                                  23
HELIX  110 110 ASP E  166  ASN E  172  1                                   7
HELIX  111 111 ASN E  172  LYS E  187  1                                  16
HELIX  112 112 ARG E  200  GLY E  208  1                                   9
HELIX  113 113 GLY E  208  GLY E  231  1                                  24
HELIX  114 114 LEU E  243  GLY E  247  5                                   5
HELIX  115 115 SER E  250  GLU E  252  5                                   3
HELIX  116 116 ASN E  253  TYR E  261  1                                   9
HELIX  117 117 GLN E  270  ASP E  276  1                                   7
HELIX  118 118 GLY E  278  ILE E  293  1                                  16
HELIX  119 119 ALA E  294  SER E  296  5                                   3
HELIX  120 120 SER E  302  ASP E  336  1                                  35
HELIX  121 121 ASN E  360  ASP E  366  1                                   7
HELIX  122 122 ASP E  370  SER E  379  1                                  10
HELIX  123 123 ARG E  390  LEU E  401  1                                  12
HELIX  124 124 PRO E  404  MET E  408  5                                   5
HELIX  125 125 GLY E  409  TYR E  433  1                                  25
HELIX  126 126 ILE E  435  ARG E  445  1                                  11
HELIX  127 127 ASP E  457  LEU E  475  1                                  19
HELIX  128 128 ASP E  480  GLU E  488  1                                   9
HELIX  129 129 GLU E  488  GLY E  506  1                                  19
HELIX  130 130 GLU E  508  ASN E  514  1                                   7
HELIX  131 131 SER E  515  GLY E  534  1                                  20
HELIX  132 132 GLN F   23  LEU F   32  1                                  10
HELIX  133 133 PRO F   34  GLY F   38  5                                   5
HELIX  134 134 HIS F   57  ASN F   69  1                                  13
HELIX  135 135 SER F   90  GLY F  113  1                                  24
HELIX  136 136 THR F  127  LYS F  147  1                                  21
HELIX  137 137 ASP F  166  ASN F  172  1                                   7
HELIX  138 138 ILE F  173  LYS F  187  1                                  15
HELIX  139 139 ARG F  200  GLY F  208  1                                   9
HELIX  140 140 GLY F  208  HIS F  230  1                                  23
HELIX  141 141 LEU F  243  GLY F  247  5                                   5
HELIX  142 142 ASN F  253  TYR F  261  1                                   9
HELIX  143 143 GLN F  270  ASP F  276  1                                   7
HELIX  144 144 GLY F  278  ILE F  293  1                                  16
HELIX  145 145 ALA F  294  SER F  296  5                                   3
HELIX  146 146 SER F  302  ASP F  336  1                                  35
HELIX  147 147 LEU F  361  ASP F  366  1                                   6
HELIX  148 148 ASP F  370  SER F  379  1                                  10
HELIX  149 149 ARG F  390  LEU F  401  1                                  12
HELIX  150 150 PRO F  404  MET F  408  5                                   5
HELIX  151 151 GLY F  409  TYR F  421  1                                  13
HELIX  152 152 TYR F  421  TYR F  433  1                                  13
HELIX  153 153 ILE F  435  ARG F  445  1                                  11
HELIX  154 154 GLY F  449  LYS F  453  5                                   5
HELIX  155 155 ASP F  457  LEU F  475  1                                  19
HELIX  156 156 ASP F  480  GLU F  488  1                                   9
HELIX  157 157 GLU F  488  GLY F  506  1                                  19
HELIX  158 158 GLU F  508  SER F  515  1                                   8
HELIX  159 159 SER F  515  GLY F  534  1                                  20
HELIX  160 160 GLN G   23  THR G   33  1                                  11
HELIX  161 161 PRO G   34  GLY G   38  5                                   5
HELIX  162 162 HIS G   57  ASN G   69  1                                  13
HELIX  163 163 SER G   90  GLY G  113  1                                  24
HELIX  164 164 THR G  127  TYR G  149  1                                  23
HELIX  165 165 ASP G  166  ASN G  172  1                                   7
HELIX  166 166 ILE G  173  SER G  186  1                                  14
HELIX  167 167 ARG G  200  GLY G  208  1                                   9
HELIX  168 168 GLY G  208  HIS G  230  1                                  23
HELIX  169 169 LEU G  243  GLY G  247  5                                   5
HELIX  170 170 ASN G  253  TYR G  261  1                                   9
HELIX  171 171 GLN G  270  ASP G  276  1                                   7
HELIX  172 172 GLY G  278  ILE G  293  1                                  16
HELIX  173 173 ALA G  294  SER G  296  5                                   3
HELIX  174 174 SER G  302  ASP G  336  1                                  35
HELIX  175 175 LEU G  361  ASP G  366  1                                   6
HELIX  176 176 ASP G  370  LEU G  378  1                                   9
HELIX  177 177 ARG G  390  LEU G  401  1                                  12
HELIX  178 178 GLY G  409  TYR G  433  1                                  25
HELIX  179 179 ILE G  435  ARG G  445  1                                  11
HELIX  180 180 ASP G  457  LEU G  475  1                                  19
HELIX  181 181 ASP G  480  GLU G  488  1                                   9
HELIX  182 182 GLU G  488  GLY G  506  1                                  19
HELIX  183 183 GLU G  508  SER G  515  1                                   8
HELIX  184 184 SER G  515  GLY G  534  1                                  20
HELIX  185 185 GLN H   23  THR H   33  1                                  11
HELIX  186 186 PRO H   34  GLY H   38  5                                   5
HELIX  187 187 HIS H   57  SER H   68  1                                  12
HELIX  188 188 SER H   90  GLY H  113  1                                  24
HELIX  189 189 THR H  127  TYR H  149  1                                  23
HELIX  190 190 ASP H  166  ASN H  172  1                                   7
HELIX  191 191 ILE H  173  SER H  186  1                                  14
HELIX  192 192 ARG H  200  GLY H  208  1                                   9
HELIX  193 193 GLY H  208  GLY H  231  1                                  24
HELIX  194 194 LEU H  243  GLY H  247  5                                   5
HELIX  195 195 ASN H  253  TYR H  261  1                                   9
HELIX  196 196 GLN H  270  ASP H  276  1                                   7
HELIX  197 197 GLY H  278  ILE H  293  1                                  16
HELIX  198 198 ALA H  294  SER H  296  5                                   3
HELIX  199 199 SER H  302  SER H  335  1                                  34
HELIX  200 200 ASP H  336  ILE H  338  5                                   3
HELIX  201 201 ASN H  360  ASP H  366  1                                   7
HELIX  202 202 ASP H  370  LEU H  378  1                                   9
HELIX  203 203 ARG H  390  LEU H  401  1                                  12
HELIX  204 204 PRO H  404  MET H  408  5                                   5
HELIX  205 205 GLY H  409  TYR H  433  1                                  25
HELIX  206 206 ILE H  435  ARG H  445  1                                  11
HELIX  207 207 ASP H  457  LEU H  475  1                                  19
HELIX  208 208 ASP H  480  GLU H  488  1                                   9
HELIX  209 209 GLU H  488  GLY H  506  1                                  19
HELIX  210 210 GLU H  508  SER H  515  1                                   8
HELIX  211 211 SER H  515  GLY H  534  1                                  20
SHEET    1   A 9 SER A   6  MET A   8  0
SHEET    2   A 9 GLU A  44  ASP A  48  1  O  GLU A  44   N  MET A   8
SHEET    3   A 9 ARG A  78  ARG A  82  1  O  THR A  80   N  VAL A  45
SHEET    4   A 9 GLU A 119  VAL A 122  1  O  VAL A 121   N  PRO A  81
SHEET    5   A 9 ARG A 159  VAL A 164  1  O  ILE A 161   N  VAL A 120
SHEET    6   A 9 ASP A 193  ALA A 199  1  O  MET A 197   N  PRO A 162
SHEET    7   A 9 THR A 233  GLY A 239  1  O  ILE A 237   N  ILE A 196
SHEET    8   A 9 THR A 266  PHE A 269  1  O  THR A 266   N  LEU A 238
SHEET    9   A 9 SER A   6  MET A   8  1  N  MET A   7   O  PHE A 269
SHEET    1   B 8 ARG B  78  VAL B  79  0
SHEET    2   B 8 GLU B  44  VAL B  45  1  N  VAL B  45   O  ARG B  78
SHEET    3   B 8 SER B   6  MET B   8  1  N  MET B   8   O  GLU B  44
SHEET    4   B 8 THR B 266  PHE B 269  1  O  PHE B 269   N  MET B   7
SHEET    5   B 8 THR B 233  GLY B 239  1  N  LEU B 238   O  THR B 266
SHEET    6   B 8 ASP B 193  ALA B 199  1  N  ILE B 198   O  ILE B 237
SHEET    7   B 8 ARG B 159  VAL B 164  1  N  VAL B 164   O  MET B 197
SHEET    8   B 8 GLU B 119  VAL B 122  1  N  VAL B 120   O  ILE B 161
SHEET    1   C 2 ARG B 356  VAL B 358  0
SHEET    2   C 2 GLU B 385  ALA B 387 -1  O  TYR B 386   N  GLU B 357
SHEET    1   D 9 SER C   6  MET C   8  0
SHEET    2   D 9 GLU C  44  ASP C  48  1  O  GLU C  44   N  MET C   8
SHEET    3   D 9 ARG C  78  ARG C  82  1  O  THR C  80   N  VAL C  45
SHEET    4   D 9 GLU C 119  VAL C 122  1  O  VAL C 121   N  PRO C  81
SHEET    5   D 9 ARG C 159  VAL C 164  1  O  ILE C 161   N  VAL C 120
SHEET    6   D 9 ASP C 193  ALA C 199  1  O  MET C 197   N  PRO C 162
SHEET    7   D 9 THR C 233  GLY C 239  1  O  THR C 233   N  LEU C 194
SHEET    8   D 9 THR C 266  PHE C 269  1  O  THR C 266   N  LEU C 238
SHEET    9   D 9 SER C   6  MET C   8  1  N  MET C   7   O  PHE C 269
SHEET    1   E 8 ARG D  78  VAL D  79  0
SHEET    2   E 8 GLU D  44  VAL D  45  1  N  VAL D  45   O  ARG D  78
SHEET    3   E 8 SER D   6  MET D   8  1  N  MET D   8   O  GLU D  44
SHEET    4   E 8 THR D 266  PHE D 269  1  O  PHE D 269   N  MET D   7
SHEET    5   E 8 THR D 233  GLY D 239  1  N  LEU D 238   O  THR D 266
SHEET    6   E 8 ASP D 193  ALA D 199  1  N  ILE D 198   O  ILE D 237
SHEET    7   E 8 ARG D 159  VAL D 164  1  N  PRO D 162   O  MET D 197
SHEET    8   E 8 GLU D 119  VAL D 122  1  N  VAL D 120   O  ILE D 161
SHEET    1   F 9 SER E   6  MET E   8  0
SHEET    2   F 9 GLU E  44  ASP E  48  1  O  MET E  46   N  MET E   8
SHEET    3   F 9 ARG E  78  ARG E  82  1  O  THR E  80   N  VAL E  45
SHEET    4   F 9 GLU E 119  VAL E 122  1  O  VAL E 121   N  PRO E  81
SHEET    5   F 9 ARG E 159  VAL E 164  1  O  ILE E 161   N  VAL E 120
SHEET    6   F 9 ASP E 193  ALA E 199  1  O  MET E 197   N  PRO E 162
SHEET    7   F 9 THR E 233  GLY E 239  1  O  ILE E 237   N  ILE E 196
SHEET    8   F 9 THR E 266  PHE E 269  1  O  THR E 266   N  LEU E 238
SHEET    9   F 9 SER E   6  MET E   8  1  N  MET E   7   O  PHE E 269
SHEET    1   G 6 SER F   6  MET F   8  0
SHEET    2   G 6 THR F 266  PHE F 269  1  O  PHE F 269   N  MET F   7
SHEET    3   G 6 THR F 233  GLY F 239  1  N  LEU F 238   O  THR F 266
SHEET    4   G 6 ASP F 193  ALA F 199  1  N  ILE F 196   O  ILE F 237
SHEET    5   G 6 ARG F 159  VAL F 164  1  N  VAL F 164   O  MET F 197
SHEET    6   G 6 GLU F 119  VAL F 122  1  N  VAL F 120   O  ILE F 161
SHEET    1   H 2 GLU F  44  VAL F  45  0
SHEET    2   H 2 ARG F  78  VAL F  79  1  O  ARG F  78   N  VAL F  45
SHEET    1   I 2 ARG F 356  GLU F 357  0
SHEET    2   I 2 TYR F 386  ALA F 387 -1  O  TYR F 386   N  GLU F 357
SHEET    1   J 8 ARG G  78  VAL G  79  0
SHEET    2   J 8 GLU G  44  MET G  46  1  N  VAL G  45   O  ARG G  78
SHEET    3   J 8 SER G   6  THR G   9  1  N  MET G   8   O  GLU G  44
SHEET    4   J 8 THR G 266  PHE G 269  1  O  PHE G 269   N  MET G   7
SHEET    5   J 8 THR G 233  GLY G 239  1  N  LEU G 238   O  THR G 266
SHEET    6   J 8 ASP G 193  ALA G 199  1  N  LEU G 194   O  THR G 233
SHEET    7   J 8 ARG G 159  VAL G 164  1  N  PRO G 162   O  MET G 197
SHEET    8   J 8 GLU G 119  VAL G 122  1  N  VAL G 120   O  ILE G 161
SHEET    1   K 9 SER H   6  MET H   8  0
SHEET    2   K 9 GLU H  44  ASP H  48  1  O  GLU H  44   N  MET H   8
SHEET    3   K 9 ARG H  78  ARG H  82  1  O  ARG H  82   N  ILE H  47
SHEET    4   K 9 GLU H 119  VAL H 122  1  O  VAL H 121   N  PRO H  81
SHEET    5   K 9 ARG H 159  VAL H 164  1  O  ILE H 161   N  VAL H 120
SHEET    6   K 9 ASP H 193  ALA H 199  1  O  MET H 197   N  PRO H 162
SHEET    7   K 9 THR H 233  GLY H 239  1  O  THR H 233   N  LEU H 194
SHEET    8   K 9 THR H 266  PHE H 269  1  O  THR H 266   N  LEU H 238
SHEET    9   K 9 SER H   6  MET H   8  1  N  MET H   7   O  PHE H 269
LINK         SG  CYS H   5                AU   AUC H 612     1555   1555  2.03
LINK         OE2 GLU C 279                AU   AUC C 621     1555   1555  2.12
LINK         SG  CYS G   5                AU   AUC G 616     1555   1555  2.13
LINK         OE1 GLU E 279                AU   AUC E 619     1555   1555  2.35
LINK         OE1 GLU G 279                AU   AUC G 626     1555   1555  2.50
LINK         OE1 GLU B 279                AU   AUC B 622     1555   1555  2.53
LINK         SG  CYS F   5                AU   AUC F 613     1555   1555  2.63
LINK         NH1 ARG B  82                AU   AUC B 640     1555   1555  2.72
LINK         O   GLY H  38                AU   AUC H 617     1555   1555  2.74
LINK         OD2 ASP G  48                AU   AUC G 615     1555   1555  2.79
LINK         SD  MET F 144                AU   AUC F 637     1555   1555  2.96
LINK         SD  MET G 144                AU   AUC F 637     1555   1555  2.99
SITE     1 AC1  5 GLN A  10  HIS A  11  MET A  46  ASP A  48
SITE     2 AC1  5 ARG A 344
SITE     1 AC2  1 CYS A   5
SITE     1 AC3  3 GLY A  38  LEU A  40  GLU A 279
SITE     1 AC4  2 MET B 144  MET H 144
SITE     1 AC5  7 ASP A  36  LYS A  37  GLN H 423  LEU H 430
SITE     2 AC5  7 ARG H 437  ILE H 474  ASN H 476
SITE     1 AC6  2 MET C 144  MET D 144
SITE     1 AC7  2 MET F 144  MET G 144
SITE     1 AC8  7 HIS A  11  ARG A  82  ALA A 199  ARG A 200
SITE     2 AC8  7 SER A 201  GLY A 239  GLN A 270
SITE     1 AC9  3 CYS B   5  GLU B  43  LYS B 290
SITE     1 BC1  5 GLN B  10  HIS B  11  ASP B  48  ARG B  82
SITE     2 BC1  5 ARG B 344
SITE     1 BC2  4 LYS B  30  GLY B  38  LEU B  40  GLU B 279
SITE     1 BC3  1 HIS B 284
SITE     1 BC4  3 HIS B  11  ARG B  82  MET B 197
SITE     1 BC5  3 LYS C   2  CYS C   5  LYS C 290
SITE     1 BC6  6 THR C   9  GLN C  10  HIS C  11  MET C  46
SITE     2 BC6  6 ASP C  48  ARG C 344
SITE     1 BC7  4 LYS C  30  GLY C  38  LEU C  40  GLU C 279
SITE     1 BC8  1 HIS C 284
SITE     1 BC9  5 HIS C  11  ARG C  82  ALA C 199  SER C 201
SITE     2 BC9  5 GLY C 239
SITE     1 CC1  5 THR D   9  GLN D  10  HIS D  11  ASP D  48
SITE     2 CC1  5 ARG D 344
SITE     1 CC2  2 CYS D   5  LYS D 290
SITE     1 CC3  4 LYS D  30  GLY D  38  LEU D  40  GLU D 279
SITE     1 CC4  1 HIS D 284
SITE     1 CC5  7 HIS D  11  ARG D  82  ALA D 199  ARG D 200
SITE     2 CC5  7 SER D 201  ASP D 202  GLY D 239
SITE     1 CC6  2 CYS E   5  LYS E 290
SITE     1 CC7  6 GLN E  10  HIS E  11  MET E  46  ASP E  48
SITE     2 CC7  6 ARG E 344  ARG E 390
SITE     1 CC8  3 GLY E  38  LEU E  40  GLU E 279
SITE     1 CC9  8 HIS E  11  ARG E  82  ALA E 199  ARG E 200
SITE     2 CC9  8 SER E 201  ASP E 202  GLY E 239  GLN E 270
SITE     1 DC1  2 CYS F   5  LYS F 290
SITE     1 DC2  5 GLN F  10  HIS F  11  ASP F  48  ARG F 344
SITE     2 DC2  5 ARG F 390
SITE     1 DC3  4 LYS F  30  GLY F  38  LEU F  40  GLU F 279
SITE     1 DC4  1 HIS F 284
SITE     1 DC5  3 HIS F  11  ARG F  82  MET F 197
SITE     1 DC6  5 GLN G  10  HIS G  11  MET G  46  ASP G  48
SITE     2 DC6  5 ARG G 344
SITE     1 DC7  2 CYS G   5  LYS G 290
SITE     1 DC8  3 GLY G  38  LEU G  40  GLU G 279
SITE     1 DC9  4 HIS H  11  MET H  46  ASP H  48  ARG H 344
SITE     1 EC1  3 CYS H   5  GLU H  43  LYS H 290
SITE     1 EC2  4 LYS H  30  GLY H  38  LEU H  40  GLU H 279
SITE     1 EC3  1 HIS H 284
SITE     1 EC4  6 HIS H  11  ARG H  82  ALA H 199  ARG H 200
SITE     2 EC4  6 SER H 201  ASP H 202
CRYST1  121.420  161.580  279.980  90.00  90.00  90.00 P 21 21 21   32
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      0.008236  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006189  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003572        0.00000
      
PROCHECK
Go to PROCHECK summary
 References