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PDBsum entry 2v6a

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Oxidoreductase PDB id
2v6a
Jmol
Contents
Protein chains
(+ 2 more) 467 a.a.
(+ 2 more) 140 a.a.
Ligands
CAP ×8
EDO ×59
Metals
_MG ×8
Waters ×3492
HEADER    OXIDOREDUCTASE                          14-JUL-07   2V6A
TITLE     CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH
TITLE    2 LARGE-SUBUNIT MUTATIONS V331A, G344S
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;
COMPND   4 SYNONYM: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   5 EC: 4.1.1.39;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1;
COMPND  10 CHAIN: I, J, K, L, M, N, O, P;
COMPND  11 SYNONYM: RUBISCO SMALL SUBUNIT 1,RIBULOSE-1,5-BISPHOSPHATE
COMPND  12  CARBOXYLASE SMALL CHAIN;
COMPND  13 EC: 4.1.1.39;
COMPND  14 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE   3 ORGANISM_TAXID: 3055;
SOURCE   4 STRAIN: 2137;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 MOL_ID: 2;
SOURCE   8 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE   9 ORGANISM_TAXID: 3055;
SOURCE  10 STRAIN: 2137;
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    LARGE SUBUNIT LOOP 6 MUTATION, CO2/O2 SPECIFICITY, CARBON
KEYWDS   2 DIOXIDE FIXATION, PHOTOSYNTHESIS, TRANSIT PEPTIDE,
KEYWDS   3 PHOTORESPIRATION, METAL-BINDING, HYDROXYLATION,
KEYWDS   4 OXIDOREDUCTASE, METHYLATION, CHLOROPLAST, CALVIN CYCLE,
KEYWDS   5 MONOOXYGENASE, LYASE, RUBISCO, PLASTID, MAGNESIUM,
KEYWDS   6 ACETYLATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.KARKEHABADI,S.SATAGOPAN,T.C.TAYLOR,R.J.SPREITZER,
AUTHOR   2 I.ANDERSSON
REVDAT   6   24-FEB-09 2V6A    1       VERSN
REVDAT   5   23-OCT-07 2V6A    1       REMARK
REVDAT   4   02-OCT-07 2V6A    1       JRNL   REMARK
REVDAT   3   28-AUG-07 2V6A    1       AUTHOR
REVDAT   2   07-AUG-07 2V6A    1       SOURCE REMARK
REVDAT   1   31-JUL-07 2V6A    0
JRNL        AUTH   S.KARKEHABADI,S.SATAGOPAN,T.C.TAYLOR,R.J.SPREITZER,
JRNL        AUTH 2 I.ANDERSSON
JRNL        TITL   STRUCTURAL ANALYSIS OF ALTERED LARGE-SUBUNIT LOOP-
JRNL        TITL 2 6-CARBOXY-TERMINUS INTERACTIONS THAT INFLUENCE
JRNL        TITL 3 CATALYTIC EFFICIENCY AND CO2-O2 SPECIFICITY OF
JRNL        TITL 4 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE
JRNL        REF    BIOCHEMISTRY                  V.  46 11080 2007
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   17824672
JRNL        DOI    10.1021/BI701063F
REMARK   2
REMARK   2 RESOLUTION.    1.5  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7
REMARK   3   NUMBER OF REFLECTIONS             : 740735
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177
REMARK   3   R VALUE            (WORKING SET) : 0.176
REMARK   3   FREE R VALUE                     : 0.192
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 39244
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) : 1.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 50643
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550
REMARK   3   BIN FREE R VALUE SET COUNT          : 2655
REMARK   3   BIN FREE R VALUE                    : 0.2690
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 38101
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 820
REMARK   3   SOLVENT ATOMS            : 3492
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.23
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.34000
REMARK   3    B22 (A**2) : 0.49000
REMARK   3    B33 (A**2) : -0.84000
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): 0.074
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.071
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.045
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.204
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 39827 ; 0.010 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 53897 ; 1.286 ; 1.960
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4833 ; 5.963 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1878 ;31.136 ;23.248
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  6460 ;13.021 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   312 ;15.450 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5701 ; 0.088 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 30552 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 20657 ; 0.199 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 27474 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  3474 ; 0.108 ; 0.200
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):    63 ; 0.214 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.171 ; 0.200
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): 24714 ; 0.719 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 38792 ; 1.122 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 17315 ; 1.832 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 15105 ; 2.801 ; 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 : 16
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     13       A      89      2
REMARK   3           2     A     97       A    1477      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1825 ;  0.00 ;  0.05
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1783 ;  0.00 ;  0.50
REMARK   3   TIGHT THERMAL      1    A (A**2):   1825 ;  0.00 ;  0.50
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1783 ;  0.00 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : B A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     B     13       B      89      2
REMARK   3           1     A     13       A      89      2
REMARK   3           2     B     97       B    1477      2
REMARK   3           2     A     97       A    1477      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   2    B    (A):   1825 ;  0.03 ;  0.05
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   1782 ;  0.15 ;  0.50
REMARK   3   TIGHT THERMAL      2    B (A**2):   1825 ;  0.14 ;  0.50
REMARK   3   MEDIUM THERMAL     2    B (A**2):   1782 ;  0.43 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 3
REMARK   3     CHAIN NAMES                    : C A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     C     13       C      89      2
REMARK   3           1     A     13       A      89      2
REMARK   3           2     C     97       C    1477      2
REMARK   3           2     A     97       A    1477      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   3    C    (A):   1825 ;  0.02 ;  0.05
REMARK   3   MEDIUM POSITIONAL  3    C    (A):   1774 ;  0.18 ;  0.50
REMARK   3   TIGHT THERMAL      3    C (A**2):   1825 ;  0.18 ;  0.50
REMARK   3   MEDIUM THERMAL     3    C (A**2):   1774 ;  0.48 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 4
REMARK   3     CHAIN NAMES                    : D A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     D     13       D      89      2
REMARK   3           1     A     13       A      89      2
REMARK   3           2     D     97       D    1477      2
REMARK   3           2     A     97       A    1477      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   4    D    (A):   1825 ;  0.03 ;  0.05
REMARK   3   MEDIUM POSITIONAL  4    D    (A):   1777 ;  0.20 ;  0.50
REMARK   3   TIGHT THERMAL      4    D (A**2):   1825 ;  0.16 ;  0.50
REMARK   3   MEDIUM THERMAL     4    D (A**2):   1777 ;  0.47 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 5
REMARK   3     CHAIN NAMES                    : E A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     E     13       E      89      2
REMARK   3           1     A     13       A      89      2
REMARK   3           2     E     97       E    1477      2
REMARK   3           2     A     97       A    1477      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   5    E    (A):   1825 ;  0.02 ;  0.05
REMARK   3   MEDIUM POSITIONAL  5    E    (A):   1780 ;  0.18 ;  0.50
REMARK   3   TIGHT THERMAL      5    E (A**2):   1825 ;  0.14 ;  0.50
REMARK   3   MEDIUM THERMAL     5    E (A**2):   1780 ;  0.42 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 6
REMARK   3     CHAIN NAMES                    : F A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     F     13       F      89      2
REMARK   3           1     A     13       A      89      2
REMARK   3           2     F     97       F    1477      2
REMARK   3           2     A     97       A    1477      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   6    F    (A):   1825 ;  0.02 ;  0.05
REMARK   3   MEDIUM POSITIONAL  6    F    (A):   1780 ;  0.18 ;  0.50
REMARK   3   TIGHT THERMAL      6    F (A**2):   1825 ;  0.13 ;  0.50
REMARK   3   MEDIUM THERMAL     6    F (A**2):   1780 ;  0.40 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 7
REMARK   3     CHAIN NAMES                    : G A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     G     13       G      89      2
REMARK   3           1     A     13       A      89      2
REMARK   3           2     G     97       G    1477      2
REMARK   3           2     A     97       A    1477      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   7    G    (A):   1825 ;  0.05 ;  0.05
REMARK   3   MEDIUM POSITIONAL  7    G    (A):   1780 ;  0.20 ;  0.50
REMARK   3   TIGHT THERMAL      7    G (A**2):   1825 ;  0.20 ;  0.50
REMARK   3   MEDIUM THERMAL     7    G (A**2):   1780 ;  0.46 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 8
REMARK   3     CHAIN NAMES                    : H A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     H     13       H      89      2
REMARK   3           1     A     13       A      89      2
REMARK   3           2     H     97       H    1477      2
REMARK   3           2     A     97       A    1477      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   8    H    (A):   1825 ;  0.03 ;  0.05
REMARK   3   MEDIUM POSITIONAL  8    H    (A):   1773 ;  0.18 ;  0.50
REMARK   3   TIGHT THERMAL      8    H (A**2):   1825 ;  0.15 ;  0.50
REMARK   3   MEDIUM THERMAL     8    H (A**2):   1773 ;  0.43 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 9
REMARK   3     CHAIN NAMES                    : I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     I      1       I     140      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   9    I    (A):    560 ;  0.00 ;  0.05
REMARK   3   MEDIUM POSITIONAL  9    I    (A):    587 ;  0.00 ;  0.50
REMARK   3   TIGHT THERMAL      9    I (A**2):    560 ;  0.00 ;  0.50
REMARK   3   MEDIUM THERMAL     9    I (A**2):    587 ;  0.00 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 10
REMARK   3     CHAIN NAMES                    : J I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     J      1       J     140      2
REMARK   3           1     I      1       I     140      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  10    J    (A):    560 ;  0.05 ;  0.05
REMARK   3   MEDIUM POSITIONAL 10    J    (A):    579 ;  0.25 ;  0.50
REMARK   3   TIGHT THERMAL     10    J (A**2):    560 ;  0.16 ;  0.50
REMARK   3   MEDIUM THERMAL    10    J (A**2):    579 ;  0.43 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 11
REMARK   3     CHAIN NAMES                    : K I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     K      1       K     140      2
REMARK   3           1     I      1       I     140      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  11    K    (A):    560 ;  0.02 ;  0.05
REMARK   3   MEDIUM POSITIONAL 11    K    (A):    569 ;  0.23 ;  0.50
REMARK   3   TIGHT THERMAL     11    K (A**2):    560 ;  0.14 ;  0.50
REMARK   3   MEDIUM THERMAL    11    K (A**2):    569 ;  0.36 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 12
REMARK   3     CHAIN NAMES                    : L I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     L      1       L     140      2
REMARK   3           1     I      1       I     140      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  12    L    (A):    560 ;  0.02 ;  0.05
REMARK   3   MEDIUM POSITIONAL 12    L    (A):    566 ;  0.24 ;  0.50
REMARK   3   TIGHT THERMAL     12    L (A**2):    560 ;  0.11 ;  0.50
REMARK   3   MEDIUM THERMAL    12    L (A**2):    566 ;  0.37 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 13
REMARK   3     CHAIN NAMES                    : M I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     M      1       M     140      2
REMARK   3           1     I      1       I     140      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  13    M    (A):    560 ;  0.03 ;  0.05
REMARK   3   MEDIUM POSITIONAL 13    M    (A):    567 ;  0.46 ;  0.50
REMARK   3   TIGHT THERMAL     13    M (A**2):    560 ;  0.24 ;  0.50
REMARK   3   MEDIUM THERMAL    13    M (A**2):    567 ;  0.55 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 14
REMARK   3     CHAIN NAMES                    : N I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     N      1       N     140      2
REMARK   3           1     I      1       I     140      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  14    N    (A):    560 ;  0.02 ;  0.05
REMARK   3   MEDIUM POSITIONAL 14    N    (A):    565 ;  0.25 ;  0.50
REMARK   3   TIGHT THERMAL     14    N (A**2):    560 ;  0.11 ;  0.50
REMARK   3   MEDIUM THERMAL    14    N (A**2):    565 ;  0.36 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 15
REMARK   3     CHAIN NAMES                    : O I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     O      1       O     140      2
REMARK   3           1     I      1       I     140      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  15    O    (A):    560 ;  0.02 ;  0.05
REMARK   3   MEDIUM POSITIONAL 15    O    (A):    573 ;  0.23 ;  0.50
REMARK   3   TIGHT THERMAL     15    O (A**2):    560 ;  0.13 ;  0.50
REMARK   3   MEDIUM THERMAL    15    O (A**2):    573 ;  0.41 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 16
REMARK   3     CHAIN NAMES                    : P I
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     P      1       P     140      2
REMARK   3           1     I      1       I     140      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL  16    P    (A):    560 ;  0.04 ;  0.05
REMARK   3   MEDIUM POSITIONAL 16    P    (A):    569 ;  0.28 ;  0.50
REMARK   3   TIGHT THERMAL     16    P (A**2):    560 ;  0.14 ;  0.50
REMARK   3   MEDIUM THERMAL    16    P (A**2):    569 ;  0.41 ;  2.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 2V6A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUL-07.
REMARK 100 THE PDBE ID CODE IS EBI-33194.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-3
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 781039
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.50
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0
REMARK 200  DATA REDUNDANCY                : 31.2
REMARK 200  R MERGE                    (I) : 0.08
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 20.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.9
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.52
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1GK8
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       64.95300
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      100.97500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       98.31450
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      100.97500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       64.95300
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       98.31450
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 GENERATING THE BIOMOLECULE
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: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 125620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 152130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -755.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350                    AND CHAINS: J, K, L, M, N, O, P
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLY 344 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLY 344 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, GLY 344 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, GLY 344 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, GLY 344 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, GLY 344 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, GLY 344 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, VAL 331 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, GLY 344 TO SER
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     VAL A     2
REMARK 465     PRO A     3
REMARK 465     GLN A     4
REMARK 465     THR A     5
REMARK 465     GLU A     6
REMARK 465     THR A     7
REMARK 465     LYS A     8
REMARK 465     MET B     1
REMARK 465     VAL B     2
REMARK 465     PRO B     3
REMARK 465     GLN B     4
REMARK 465     THR B     5
REMARK 465     GLU B     6
REMARK 465     THR B     7
REMARK 465     LYS B     8
REMARK 465     MET C     1
REMARK 465     VAL C     2
REMARK 465     PRO C     3
REMARK 465     GLN C     4
REMARK 465     THR C     5
REMARK 465     GLU C     6
REMARK 465     THR C     7
REMARK 465     LYS C     8
REMARK 465     MET D     1
REMARK 465     VAL D     2
REMARK 465     PRO D     3
REMARK 465     GLN D     4
REMARK 465     THR D     5
REMARK 465     GLU D     6
REMARK 465     THR D     7
REMARK 465     LYS D     8
REMARK 465     ALA D     9
REMARK 465     MET E     1
REMARK 465     VAL E     2
REMARK 465     PRO E     3
REMARK 465     GLN E     4
REMARK 465     THR E     5
REMARK 465     GLU E     6
REMARK 465     THR E     7
REMARK 465     LYS E     8
REMARK 465     ALA E     9
REMARK 465     GLY E    10
REMARK 465     MET F     1
REMARK 465     VAL F     2
REMARK 465     PRO F     3
REMARK 465     GLN F     4
REMARK 465     THR F     5
REMARK 465     GLU F     6
REMARK 465     THR F     7
REMARK 465     LYS F     8
REMARK 465     ALA F     9
REMARK 465     GLY F    10
REMARK 465     MET G     1
REMARK 465     VAL G     2
REMARK 465     PRO G     3
REMARK 465     GLN G     4
REMARK 465     THR G     5
REMARK 465     GLU G     6
REMARK 465     THR G     7
REMARK 465     LYS G     8
REMARK 465     ALA G     9
REMARK 465     GLY G    10
REMARK 465     MET H     1
REMARK 465     VAL H     2
REMARK 465     PRO H     3
REMARK 465     GLN H     4
REMARK 465     THR H     5
REMARK 465     GLU H     6
REMARK 465     THR H     7
REMARK 465     LYS H     8
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 449   CA  -  CB  -  SG  ANGL. DEV. =   7.8 DEGREES
REMARK 500    PRO B  91   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES
REMARK 500    CYS C 449   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES
REMARK 500    CYS D 449   CA  -  CB  -  SG  ANGL. DEV. =   8.9 DEGREES
REMARK 500    CYS F 449   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES
REMARK 500    CYS G 449   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES
REMARK 500    CYS H 449   CA  -  CB  -  SG  ANGL. DEV. =   7.7 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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  62      -79.79   -141.08
REMARK 500    THR A  65     -166.60   -129.37
REMARK 500    THR A  75     -166.64   -122.77
REMARK 500    CYS A 172      124.21   -173.53
REMARK 500    ASN A 207      -93.66   -122.58
REMARK 500    MET A 212      108.55   -166.19
REMARK 500    ALA A 296      131.56    -38.62
REMARK 500    MET A 297      -11.05     89.51
REMARK 500    ALA A 331      -51.78     72.72
REMARK 500    SER B  62      -79.23   -139.72
REMARK 500    THR B  65     -165.72   -128.11
REMARK 500    THR B  75     -166.04   -122.68
REMARK 500    CYS B 172      123.82   -172.24
REMARK 500    ASN B 207      -95.31   -123.69
REMARK 500    MET B 212      110.49   -164.64
REMARK 500    ALA B 296      133.58    -39.43
REMARK 500    MET B 297      -12.35     88.12
REMARK 500    ALA B 331      -48.98     70.48
REMARK 500    SER C  62      -79.74   -139.38
REMARK 500    THR C  65     -167.90   -129.17
REMARK 500    THR C  75     -167.33   -122.41
REMARK 500    CYS C 172      123.51   -172.22
REMARK 500    ASN C 207      -92.91   -123.04
REMARK 500    MET C 212      109.08   -165.47
REMARK 500    MET C 297       -9.11     86.72
REMARK 500    ALA C 331      -49.28     72.00
REMARK 500    SER D  62      -80.97   -138.16
REMARK 500    THR D  65     -164.66   -128.64
REMARK 500    THR D  75     -167.01   -120.65
REMARK 500    CYS D 172      125.67   -173.09
REMARK 500    ASN D 207      -93.35   -123.89
REMARK 500    MET D 212      109.57   -167.60
REMARK 500    MET D 297      -12.93     89.66
REMARK 500    ALA D 331      -50.88     70.75
REMARK 500    SER E  62      -78.82   -141.74
REMARK 500    THR E  65     -166.00   -129.74
REMARK 500    THR E  75     -169.66   -123.91
REMARK 500    CYS E 172      125.90   -174.04
REMARK 500    ASN E 207      -96.56   -125.31
REMARK 500    MET E 212      109.31   -165.73
REMARK 500    ALA E 296      131.61    -38.30
REMARK 500    MET E 297      -10.35     88.03
REMARK 500    ALA E 331      -51.80     73.61
REMARK 500    SER F  62      -78.08   -137.97
REMARK 500    THR F  75     -168.88   -123.30
REMARK 500    CYS F 172      125.50   -174.17
REMARK 500    ASN F 207      -94.83   -123.97
REMARK 500    MET F 212      109.88   -164.14
REMARK 500    MET F 297      -10.58     87.44
REMARK 500    ALA F 331      -52.48     70.14
REMARK 500    SER G  62      -78.63   -137.43
REMARK 500    THR G  75     -166.98   -121.02
REMARK 500    CYS G 172      126.20   -172.31
REMARK 500    ASN G 207      -95.29   -125.13
REMARK 500    MET G 212      109.69   -166.03
REMARK 500    MET G 297      -10.85     88.04
REMARK 500    ALA G 331      -51.50     70.58
REMARK 500    SER H  62      -80.75   -140.21
REMARK 500    THR H  75     -163.09   -123.29
REMARK 500    CYS H 172      125.75   -174.01
REMARK 500    ASN H 207      -90.60   -124.54
REMARK 500    MET H 212      111.19   -165.94
REMARK 500    MET H 297       -8.87     88.44
REMARK 500    ALA H 331      -52.19     69.04
REMARK 500    PHE I  12       42.72   -145.07
REMARK 500    GLU I  13     -141.92     62.74
REMARK 500    PHE I  15       -1.77     83.09
REMARK 500    LYS I  77     -124.37     57.42
REMARK 500    PHE J  12       41.25   -144.13
REMARK 500    GLU J  13     -141.83     62.69
REMARK 500    PHE J  15       -1.56     79.11
REMARK 500    LYS J  77     -121.65     54.46
REMARK 500    PHE K  12       42.34   -144.27
REMARK 500    GLU K  13     -141.38     60.66
REMARK 500    PHE K  15       -0.91     81.89
REMARK 500    LYS K  77     -122.99     53.41
REMARK 500    PHE L  12       44.05   -146.49
REMARK 500    GLU L  13     -143.56     58.76
REMARK 500    PHE L  15        0.08     83.98
REMARK 500    LYS L  77     -123.68     55.94
REMARK 500    PHE M  12       42.15   -145.30
REMARK 500    GLU M  13     -142.71     60.06
REMARK 500    PHE M  15       -3.95     85.21
REMARK 500    LYS M  77     -123.23     55.74
REMARK 500    PHE N  12       43.50   -143.89
REMARK 500    GLU N  13     -141.35     57.83
REMARK 500    PHE N  15       -0.62     80.14
REMARK 500    TRP N  73     -169.84   -108.41
REMARK 500    LYS N  77     -123.31     55.34
REMARK 500    PHE O  12       43.75   -142.85
REMARK 500    GLU O  13     -139.65     60.92
REMARK 500    PHE O  15       -1.21     82.97
REMARK 500    LYS O  77     -123.10     55.38
REMARK 500    PHE P  12       44.95   -142.64
REMARK 500    GLU P  13     -137.23     60.09
REMARK 500    PHE P  15       -0.23     82.13
REMARK 500    LYS P  77     -121.16     55.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M=MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE)
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A1476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 203   OD1
REMARK 620 2 GLU A 204   OE1  91.9
REMARK 620 3 CAP A1477   O3  173.0  89.0
REMARK 620 4 CAP A1477   O7   99.4  99.6  87.3
REMARK 620 5 KCX A 201   OQ1  86.0  88.3  87.0 170.1
REMARK 620 6 CAP A1477   O2  104.1 164.0  75.3  76.5  94.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B1476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP B1477   O2
REMARK 620 2 CAP B1477   O3   74.2
REMARK 620 3 KCX B 201   OQ1  94.2  85.6
REMARK 620 4 ASP B 203   OD1 103.2 174.8  90.1
REMARK 620 5 GLU B 204   OE1 163.7  90.6  90.7  92.3
REMARK 620 6 CAP B1477   O7   74.3  86.9 167.6  96.8  99.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C1476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX C 201   OQ1
REMARK 620 2 ASP C 203   OD1  87.7
REMARK 620 3 CAP C1477   O2   93.8 104.3
REMARK 620 4 CAP C1477   O7  167.8 100.4  75.4
REMARK 620 5 GLU C 204   OE1  89.7  91.5 163.9  99.1
REMARK 620 6 CAP C1477   O3   85.1 172.6  75.0  86.6  89.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG D1476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX D 201   OQ1
REMARK 620 2 GLU D 204   OE1  90.6
REMARK 620 3 CAP D1477   O3   86.6  89.9
REMARK 620 4 ASP D 203   OD1  86.9  91.5 173.4
REMARK 620 5 CAP D1477   O2   93.7 164.6  75.7 103.4
REMARK 620 6 CAP D1477   O7  169.1  98.5  87.4  98.8  75.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG E1476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP E1477   O2
REMARK 620 2 KCX E 201   OQ1  93.7
REMARK 620 3 ASP E 203   OD1 105.2  88.8
REMARK 620 4 CAP E1477   O3   75.2  85.5 174.3
REMARK 620 5 GLU E 204   OE1 163.7  90.4  90.6  89.4
REMARK 620 6 CAP E1477   O7   74.9 167.8  98.1  87.5  99.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG F1476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 203   OD1
REMARK 620 2 GLU F 204   OE1  91.7
REMARK 620 3 CAP F1477   O2  104.1 163.2
REMARK 620 4 CAP F1477   O7   97.4  97.5  75.2
REMARK 620 5 KCX F 201   OQ1  88.7  90.6  95.3 169.6
REMARK 620 6 CAP F1477   O3  175.8  88.4  76.2  86.7  87.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG G1476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP G1477   O3
REMARK 620 2 CAP G1477   O7   88.4
REMARK 620 3 KCX G 201   OQ1  85.3 169.2
REMARK 620 4 ASP G 203   OD1 173.1  97.7  88.2
REMARK 620 5 GLU G 204   OE1  91.3  99.5  89.4  91.0
REMARK 620 6 CAP G1477   O2   74.1  75.6  94.2 104.1 164.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG H1476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP H1477   O7
REMARK 620 2 ASP H 203   OD1  97.8
REMARK 620 3 GLU H 204   OE1  98.5  88.8
REMARK 620 4 CAP H1477   O3   86.7 175.5  90.0
REMARK 620 5 KCX H 201   OQ1 170.2  86.1  90.5  89.7
REMARK 620 6 CAP H1477   O2   75.7 106.6 164.0  75.0  94.7
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG F1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG G1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG H1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1142
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1141
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1142
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GK8   RELATED DB: PDB
REMARK 900  RUBISCO FROM CHLAMYDOMONAS REINHARDTII
REMARK 900 RELATED ID: 1UWA   RELATED DB: PDB
REMARK 900  L290F MUTANT RUBISCO FROM CHLAMYDOMONAS
REMARK 900 RELATED ID: 1UW9   RELATED DB: PDB
REMARK 900  L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT
REMARK 900 RELATED ID: 1UZH   RELATED DB: PDB
REMARK 900  A CHIMERIC CHLAMYDOMONAS, SPINACH RUBISCO
REMARK 900  ENZYME
REMARK 900 RELATED ID: 1IR2   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5
REMARK 900  -BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO) FROM
REMARK 900   GREEN ALGA,CHLAMYDOMONAS REINHARDTII COMPLEXED
REMARK 900   WITH 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE (
REMARK 900  2-CABP)
REMARK 900 RELATED ID: 1UZD   RELATED DB: PDB
REMARK 900  CHLAMYDOMONAS,SPINACH CHIMERIC RUBISCO
REMARK 900 RELATED ID: 2V63   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF RUBISCO FROM
REMARK 900  CHLAMYDOMONAS REINHARDTII WITH A LARGE-SUBUNIT
REMARK 900   V331A MUTATION
REMARK 900 RELATED ID: 2V67   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900  RUBISCO WITH A LARGE-SUBUNIT SUPRESSOR
REMARK 900  MUTATION T342I
REMARK 900 RELATED ID: 2V68   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900  RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A,
REMARK 900  T342I
REMARK 900 RELATED ID: 2V69   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII
REMARK 900  RUBISCO WITH A LARGE-SUBUNIT MUTATION D473E
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE UNIPROT DATABASE ENTRY FOR THIS SEQUENCE (P00877)
REMARK 999 HAS A VARIANT (LEU46PRO) WHICH OCCURS IN STRAIN 21GR
REMARK 999 AND 2137.
DBREF  2V6A A    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V6A B    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V6A C    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V6A D    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V6A E    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V6A F    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V6A G    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V6A H    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  2V6A I    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V6A J    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V6A K    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V6A L    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V6A M    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V6A N    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V6A O    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  2V6A P    1   140  UNP    P00873   RBS1_CHLRE      46    185
SEQADV 2V6A PRO A   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V6A ALA A  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V6A SER A  344  UNP  P00877    GLY   344 ENGINEERED MUTATION
SEQADV 2V6A PRO B   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V6A ALA B  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V6A SER B  344  UNP  P00877    GLY   344 ENGINEERED MUTATION
SEQADV 2V6A PRO C   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V6A ALA C  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V6A SER C  344  UNP  P00877    GLY   344 ENGINEERED MUTATION
SEQADV 2V6A PRO D   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V6A ALA D  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V6A SER D  344  UNP  P00877    GLY   344 ENGINEERED MUTATION
SEQADV 2V6A PRO E   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V6A ALA E  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V6A SER E  344  UNP  P00877    GLY   344 ENGINEERED MUTATION
SEQADV 2V6A PRO F   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V6A ALA F  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V6A SER F  344  UNP  P00877    GLY   344 ENGINEERED MUTATION
SEQADV 2V6A PRO G   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V6A ALA G  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V6A SER G  344  UNP  P00877    GLY   344 ENGINEERED MUTATION
SEQADV 2V6A PRO H   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 2V6A ALA H  331  UNP  P00877    VAL   331 ENGINEERED MUTATION
SEQADV 2V6A SER H  344  UNP  P00877    GLY   344 ENGINEERED MUTATION
SEQRES   1 A  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 A  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 A  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 A  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 A  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 A  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 A  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 A  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 A  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 A  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 A  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 A  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 A  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 A  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 A  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 A  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 A  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 A  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 A  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 A  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 A  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 A  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 A  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 A  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 A  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 A  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 A  475  ARG GLU VAL THR LEU SER PHE VAL ASP LEU MET ARG ASP
SEQRES  28 A  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 A  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 A  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 A  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 A  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 A  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 A  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 A  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 B  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 B  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 B  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 B  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 B  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 B  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 B  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 B  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 B  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 B  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 B  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 B  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 B  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 B  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 B  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 B  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 B  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 B  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 B  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 B  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 B  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 B  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 B  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 B  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 B  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 B  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 B  475  ARG GLU VAL THR LEU SER PHE VAL ASP LEU MET ARG ASP
SEQRES  28 B  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 B  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 B  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 B  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 B  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 B  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 B  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 B  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 B  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 B  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 C  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 C  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 C  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 C  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 C  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 C  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 C  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 C  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 C  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 C  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 C  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 C  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 C  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 C  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 C  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 C  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 C  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 C  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 C  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 C  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 C  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 C  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 C  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 C  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 C  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 C  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 C  475  ARG GLU VAL THR LEU SER PHE VAL ASP LEU MET ARG ASP
SEQRES  28 C  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 C  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 C  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 C  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 C  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 C  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 C  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 C  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 C  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 C  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 D  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 D  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 D  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 D  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 D  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 D  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 D  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 D  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 D  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 D  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 D  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 D  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 D  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 D  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 D  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 D  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 D  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 D  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 D  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 D  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 D  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 D  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 D  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 D  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 D  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 D  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 D  475  ARG GLU VAL THR LEU SER PHE VAL ASP LEU MET ARG ASP
SEQRES  28 D  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 D  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 D  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 D  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 D  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 D  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 D  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 D  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 D  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 D  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 E  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 E  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 E  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 E  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 E  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 E  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 E  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 E  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 E  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 E  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 E  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 E  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 E  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 E  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 E  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 E  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 E  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 E  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 E  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 E  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 E  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 E  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 E  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 E  475  ARG GLU VAL THR LEU SER PHE VAL ASP LEU MET ARG ASP
SEQRES  28 E  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 E  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 E  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 E  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 E  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 E  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 E  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 E  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 F  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 F  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 F  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 F  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 F  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 F  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 F  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 F  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 F  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 F  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 F  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 F  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 F  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 F  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 F  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 F  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 F  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 F  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 F  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 F  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 F  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 F  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 F  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 F  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 F  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 F  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 F  475  ARG GLU VAL THR LEU SER PHE VAL ASP LEU MET ARG ASP
SEQRES  28 F  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 F  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 F  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 F  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 F  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 F  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 F  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 F  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 F  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 F  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 G  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 G  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 G  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 G  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 G  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 G  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 G  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 G  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 G  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 G  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 G  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 G  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 G  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 G  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 G  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 G  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 G  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 G  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 G  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 G  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 G  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 G  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 G  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 G  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 G  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 G  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 G  475  ARG GLU VAL THR LEU SER PHE VAL ASP LEU MET ARG ASP
SEQRES  28 G  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 G  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 G  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 G  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 G  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 G  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 G  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 G  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 G  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 G  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 H  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 H  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 H  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 H  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 H  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 H  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 H  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 H  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 H  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 H  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 H  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 H  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 H  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 H  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 H  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 H  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 H  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 H  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 H  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 H  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 H  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 H  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 H  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 H  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 H  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 H  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 H  475  ARG GLU VAL THR LEU SER PHE VAL ASP LEU MET ARG ASP
SEQRES  28 H  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 H  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 H  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 H  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 H  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 H  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 H  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 H  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 H  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 H  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 I  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 I  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 I  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 I  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 I  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 I  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 I  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 I  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 I  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 I  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 I  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 J  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 J  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 J  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 J  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 J  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 J  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 J  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 J  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 J  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 J  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 J  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 K  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 K  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 K  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 K  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 K  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 K  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 K  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 K  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 K  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 K  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 K  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 L  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 L  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 L  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 L  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 L  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 L  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 L  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 L  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 L  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 L  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 L  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 M  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 M  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 M  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 M  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 M  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 M  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 M  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 M  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 M  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 M  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 M  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 N  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 N  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 N  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 N  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 N  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 N  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 N  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 N  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 N  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 N  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 N  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 O  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 O  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 O  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 O  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 O  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 O  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 O  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 O  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 O  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 O  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 O  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 P  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 P  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 P  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 P  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 P  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 P  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 P  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 P  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 P  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 P  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG
SEQRES  11 P  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL
MODRES 2V6A HYP A  104  PRO  4-HYDROXYPROLINE
MODRES 2V6A HYP A  151  PRO  4-HYDROXYPROLINE
MODRES 2V6A KCX A  201  LYS  LYSYL-CARBAMATE
MODRES 2V6A SMC A  256  CYS  S-METHYLCYSTEINE
MODRES 2V6A SMC A  369  CYS  S-METHYLCYSTEINE
MODRES 2V6A HYP B  104  PRO  4-HYDROXYPROLINE
MODRES 2V6A HYP B  151  PRO  4-HYDROXYPROLINE
MODRES 2V6A KCX B  201  LYS  LYSYL-CARBAMATE
MODRES 2V6A SMC B  256  CYS  S-METHYLCYSTEINE
MODRES 2V6A SMC B  369  CYS  S-METHYLCYSTEINE
MODRES 2V6A HYP C  104  PRO  4-HYDROXYPROLINE
MODRES 2V6A HYP C  151  PRO  4-HYDROXYPROLINE
MODRES 2V6A KCX C  201  LYS  LYSYL-CARBAMATE
MODRES 2V6A SMC C  256  CYS  S-METHYLCYSTEINE
MODRES 2V6A SMC C  369  CYS  S-METHYLCYSTEINE
MODRES 2V6A HYP D  104  PRO  4-HYDROXYPROLINE
MODRES 2V6A HYP D  151  PRO  4-HYDROXYPROLINE
MODRES 2V6A KCX D  201  LYS  LYSYL-CARBAMATE
MODRES 2V6A SMC D  256  CYS  S-METHYLCYSTEINE
MODRES 2V6A SMC D  369  CYS  S-METHYLCYSTEINE
MODRES 2V6A HYP E  104  PRO  4-HYDROXYPROLINE
MODRES 2V6A HYP E  151  PRO  4-HYDROXYPROLINE
MODRES 2V6A KCX E  201  LYS  LYSYL-CARBAMATE
MODRES 2V6A SMC E  256  CYS  S-METHYLCYSTEINE
MODRES 2V6A SMC E  369  CYS  S-METHYLCYSTEINE
MODRES 2V6A HYP F  104  PRO  4-HYDROXYPROLINE
MODRES 2V6A HYP F  151  PRO  4-HYDROXYPROLINE
MODRES 2V6A KCX F  201  LYS  LYSYL-CARBAMATE
MODRES 2V6A SMC F  256  CYS  S-METHYLCYSTEINE
MODRES 2V6A SMC F  369  CYS  S-METHYLCYSTEINE
MODRES 2V6A HYP G  104  PRO  4-HYDROXYPROLINE
MODRES 2V6A HYP G  151  PRO  4-HYDROXYPROLINE
MODRES 2V6A KCX G  201  LYS  LYSYL-CARBAMATE
MODRES 2V6A SMC G  256  CYS  S-METHYLCYSTEINE
MODRES 2V6A SMC G  369  CYS  S-METHYLCYSTEINE
MODRES 2V6A HYP H  104  PRO  4-HYDROXYPROLINE
MODRES 2V6A HYP H  151  PRO  4-HYDROXYPROLINE
MODRES 2V6A KCX H  201  LYS  LYSYL-CARBAMATE
MODRES 2V6A SMC H  256  CYS  S-METHYLCYSTEINE
MODRES 2V6A SMC H  369  CYS  S-METHYLCYSTEINE
MODRES 2V6A MME I    1  MET  N-METHYL METHIONINE
MODRES 2V6A MME J    1  MET  N-METHYL METHIONINE
MODRES 2V6A MME K    1  MET  N-METHYL METHIONINE
MODRES 2V6A MME L    1  MET  N-METHYL METHIONINE
MODRES 2V6A MME M    1  MET  N-METHYL METHIONINE
MODRES 2V6A MME N    1  MET  N-METHYL METHIONINE
MODRES 2V6A MME O    1  MET  N-METHYL METHIONINE
MODRES 2V6A MME P    1  MET  N-METHYL METHIONINE
HET    HYP  A 104       8
HET    HYP  A 151       8
HET    KCX  A 201      12
HET    SMC  A 256       7
HET    SMC  A 369       7
HET     MG  A1476       1
HET    CAP  A1477      21
HET    HYP  B 104       8
HET    HYP  B 151       8
HET    KCX  B 201      12
HET    SMC  B 256       7
HET    SMC  B 369       7
HET     MG  B1476       1
HET    CAP  B1477      21
HET    HYP  C 104       8
HET    HYP  C 151       8
HET    KCX  C 201      12
HET    SMC  C 256       7
HET    SMC  C 369       7
HET     MG  C1476       1
HET    CAP  C1477      21
HET    HYP  D 104       8
HET    HYP  D 151       8
HET    KCX  D 201      12
HET    SMC  D 256       7
HET    SMC  D 369       7
HET     MG  D1476       1
HET    CAP  D1477      21
HET    HYP  E 104       8
HET    HYP  E 151       8
HET    KCX  E 201      12
HET    SMC  E 256       7
HET    SMC  E 369       7
HET     MG  E1476       1
HET    CAP  E1477      21
HET    HYP  F 104       8
HET    HYP  F 151       8
HET    KCX  F 201      12
HET    SMC  F 256       7
HET    SMC  F 369       7
HET     MG  F1476       1
HET    CAP  F1477      21
HET    HYP  G 104       8
HET    HYP  G 151       8
HET    KCX  G 201      12
HET    SMC  G 256       7
HET    SMC  G 369       7
HET     MG  G1476       1
HET    CAP  G1477      21
HET    HYP  H 104       8
HET    HYP  H 151       8
HET    KCX  H 201      12
HET    SMC  H 256       7
HET    SMC  H 369       7
HET     MG  H1476       1
HET    CAP  H1477      21
HET    MME  I   1       9
HET    MME  J   1       9
HET    MME  K   1       9
HET    MME  L   1       9
HET    MME  M   1       9
HET    MME  N   1       9
HET    MME  O   1       9
HET    MME  P   1       9
HET    EDO  A1478       4
HET    EDO  A1479       4
HET    EDO  A1480       4
HET    EDO  A1481       4
HET    EDO  A1482       4
HET    EDO  C1478       4
HET    EDO  C1479       4
HET    EDO  C1480       4
HET    EDO  C1481       4
HET    EDO  C1482       4
HET    EDO  E1478       4
HET    EDO  E1479       4
HET    EDO  E1480       4
HET    EDO  E1481       4
HET    EDO  G1478       4
HET    EDO  G1479       4
HET    EDO  G1480       4
HET    EDO  G1481       4
HET    EDO  G1482       4
HET    EDO  I1141       4
HET    EDO  K1141       4
HET    EDO  K1142       4
HET    EDO  M1141       4
HET    EDO  M1142       4
HET    EDO  O1141       4
HET    EDO  O1142       4
HET    EDO  F1478       4
HET    EDO  A1483       4
HET    EDO  H1478       4
HET    EDO  B1478       4
HET    EDO  B1479       4
HET    EDO  B1480       4
HET    EDO  B1481       4
HET    EDO  B1482       4
HET    EDO  H1479       4
HET    EDO  H1480       4
HET    EDO  H1481       4
HET    EDO  H1482       4
HET    EDO  F1479       4
HET    EDO  F1480       4
HET    EDO  F1481       4
HET    EDO  F1482       4
HET    EDO  F1483       4
HET    EDO  D1478       4
HET    EDO  D1479       4
HET    EDO  D1480       4
HET    EDO  D1481       4
HET    EDO  J1141       4
HET    EDO  J1142       4
HET    EDO  P1141       4
HET    EDO  P1142       4
HET    EDO  N1141       4
HET    EDO  N1142       4
HET    EDO  C1483       4
HET    EDO  A1484       4
HET    EDO  I1142       4
HET    EDO  D1482       4
HET    EDO  L1141       4
HET    EDO  L1142       4
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM     MME N-METHYL METHIONINE
HETNAM     SMC S-METHYLCYSTEINE
HETNAM     HYP 4-HYDROXYPROLINE
HETNAM      MG MAGNESIUM ION
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID
HETSYN     EDO ETHYLENE GLYCOL
FORMUL  17  EDO    59(C2 H6 O2)
FORMUL  18  CAP    8(C6 H14 O13 P2)
FORMUL  19  MME    8(C6 H13 N O2 S)
FORMUL  20  SMC    16(C4 H9 N O2 S)
FORMUL  21  HYP    16(C5 H9 N O3)
FORMUL  22   MG    8(MG 2+)
FORMUL  23  KCX    8(C7 H14 N2 O4)
FORMUL  24  HOH   *3492(H2 O1)
HELIX    1   1 TYR A   20  TYR A   25  1                                   6
HELIX    2   2 PRO A   49  SER A   61  1                                  13
HELIX    3   3 VAL A   69  THR A   75  5                                   7
HELIX    4   4 SER A   76  LYS A   81  1                                   6
HELIX    5   5 HYP A  104  PHE A  108  5                                   5
HELIX    6   6 SER A  112  GLY A  122  1                                  11
HELIX    7   7 ASN A  123  GLY A  126  5                                   4
HELIX    8   8 PRO A  141  LYS A  146  1                                   6
HELIX    9   9 GLY A  154  ASN A  163  1                                  10
HELIX   10  10 SER A  181  GLY A  195  1                                  15
HELIX   11  11 ARG A  213  GLY A  233  1                                  21
HELIX   12  12 THR A  246  VAL A  255  1                                  10
HELIX   13  13 TYR A  269  GLY A  288  1                                  20
HELIX   14  14 MET A  297  ARG A  303  1                                   7
HELIX   15  15 HIS A  310  GLY A  322  1                                  13
HELIX   16  16 GLU A  338  ASP A  351  1                                  14
HELIX   17  17 ARG A  358  GLY A  361  5                                   4
HELIX   18  18 HIS A  383  TRP A  385  5                                   3
HELIX   19  19 HIS A  386  GLY A  395  1                                  10
HELIX   20  20 GLY A  403  GLY A  408  1                                   6
HELIX   21  21 GLY A  412  GLU A  433  1                                  22
HELIX   22  22 ASP A  436  LYS A  463  1                                  28
HELIX   23  23 TYR B   20  TYR B   25  1                                   6
HELIX   24  24 PRO B   49  SER B   61  1                                  13
HELIX   25  25 VAL B   69  THR B   75  5                                   7
HELIX   26  26 SER B   76  LYS B   81  1                                   6
HELIX   27  27 HYP B  104  PHE B  108  5                                   5
HELIX   28  28 SER B  112  GLY B  122  1                                  11
HELIX   29  29 ASN B  123  GLY B  126  5                                   4
HELIX   30  30 PRO B  141  LYS B  146  1                                   6
HELIX   31  31 GLY B  154  ASN B  163  1                                  10
HELIX   32  32 SER B  181  GLY B  195  1                                  15
HELIX   33  33 ARG B  213  GLY B  233  1                                  21
HELIX   34  34 THR B  246  VAL B  255  1                                  10
HELIX   35  35 TYR B  269  GLY B  288  1                                  20
HELIX   36  36 MET B  297  ARG B  303  1                                   7
HELIX   37  37 HIS B  310  GLY B  322  1                                  13
HELIX   38  38 GLU B  338  ASP B  351  1                                  14
HELIX   39  39 ARG B  358  GLY B  361  5                                   4
HELIX   40  40 HIS B  383  TRP B  385  5                                   3
HELIX   41  41 HIS B  386  GLY B  395  1                                  10
HELIX   42  42 GLY B  403  GLY B  408  1                                   6
HELIX   43  43 GLY B  412  GLU B  433  1                                  22
HELIX   44  44 ASP B  436  LYS B  463  1                                  28
HELIX   45  45 TYR C   20  TYR C   25  1                                   6
HELIX   46  46 PRO C   49  SER C   61  1                                  13
HELIX   47  47 VAL C   69  THR C   75  5                                   7
HELIX   48  48 SER C   76  LYS C   81  1                                   6
HELIX   49  49 HYP C  104  PHE C  108  5                                   5
HELIX   50  50 SER C  112  GLY C  122  1                                  11
HELIX   51  51 ASN C  123  GLY C  126  5                                   4
HELIX   52  52 PRO C  141  LYS C  146  1                                   6
HELIX   53  53 GLY C  154  ASN C  163  1                                  10
HELIX   54  54 SER C  181  GLY C  195  1                                  15
HELIX   55  55 ARG C  213  GLY C  233  1                                  21
HELIX   56  56 THR C  246  VAL C  255  1                                  10
HELIX   57  57 TYR C  269  GLY C  288  1                                  20
HELIX   58  58 MET C  297  ARG C  303  1                                   7
HELIX   59  59 HIS C  310  GLY C  322  1                                  13
HELIX   60  60 GLU C  338  ASP C  351  1                                  14
HELIX   61  61 ARG C  358  GLY C  361  5                                   4
HELIX   62  62 HIS C  383  TRP C  385  5                                   3
HELIX   63  63 HIS C  386  GLY C  395  1                                  10
HELIX   64  64 GLY C  403  GLY C  408  1                                   6
HELIX   65  65 GLY C  412  GLU C  433  1                                  22
HELIX   66  66 ASP C  436  LYS C  463  1                                  28
HELIX   67  67 TYR D   20  TYR D   25  1                                   6
HELIX   68  68 PRO D   49  SER D   61  1                                  13
HELIX   69  69 VAL D   69  THR D   75  5                                   7
HELIX   70  70 SER D   76  LYS D   81  1                                   6
HELIX   71  71 HYP D  104  PHE D  108  5                                   5
HELIX   72  72 SER D  112  GLY D  122  1                                  11
HELIX   73  73 ASN D  123  GLY D  126  5                                   4
HELIX   74  74 PRO D  141  LYS D  146  1                                   6
HELIX   75  75 GLY D  154  ASN D  163  1                                  10
HELIX   76  76 SER D  181  GLY D  195  1                                  15
HELIX   77  77 ARG D  213  GLY D  233  1                                  21
HELIX   78  78 THR D  246  VAL D  255  1                                  10
HELIX   79  79 TYR D  269  GLY D  288  1                                  20
HELIX   80  80 MET D  297  ARG D  303  1                                   7
HELIX   81  81 HIS D  310  GLY D  322  1                                  13
HELIX   82  82 GLU D  338  ASP D  351  1                                  14
HELIX   83  83 ARG D  358  GLY D  361  5                                   4
HELIX   84  84 HIS D  383  TRP D  385  5                                   3
HELIX   85  85 HIS D  386  GLY D  395  1                                  10
HELIX   86  86 GLY D  403  GLY D  408  1                                   6
HELIX   87  87 GLY D  412  GLU D  433  1                                  22
HELIX   88  88 ASP D  436  LYS D  463  1                                  28
HELIX   89  89 TYR E   20  TYR E   25  1                                   6
HELIX   90  90 PRO E   49  SER E   61  1                                  13
HELIX   91  91 VAL E   69  THR E   75  5                                   7
HELIX   92  92 SER E   76  LYS E   81  1                                   6
HELIX   93  93 HYP E  104  PHE E  108  5                                   5
HELIX   94  94 SER E  112  GLY E  122  1                                  11
HELIX   95  95 ASN E  123  GLY E  126  5                                   4
HELIX   96  96 PRO E  141  LYS E  146  1                                   6
HELIX   97  97 GLY E  154  ASN E  163  1                                  10
HELIX   98  98 SER E  181  GLY E  195  1                                  15
HELIX   99  99 ARG E  213  GLY E  233  1                                  21
HELIX  100 100 THR E  246  VAL E  255  1                                  10
HELIX  101 101 TYR E  269  GLY E  288  1                                  20
HELIX  102 102 MET E  297  ARG E  303  1                                   7
HELIX  103 103 HIS E  310  GLY E  322  1                                  13
HELIX  104 104 GLU E  338  ASP E  351  1                                  14
HELIX  105 105 ARG E  358  GLY E  361  5                                   4
HELIX  106 106 HIS E  383  TRP E  385  5                                   3
HELIX  107 107 HIS E  386  GLY E  395  1                                  10
HELIX  108 108 GLY E  403  GLY E  408  1                                   6
HELIX  109 109 GLY E  412  GLU E  433  1                                  22
HELIX  110 110 ASP E  436  LYS E  463  1                                  28
HELIX  111 111 TYR F   20  TYR F   25  1                                   6
HELIX  112 112 PRO F   49  SER F   61  1                                  13
HELIX  113 113 VAL F   69  THR F   75  5                                   7
HELIX  114 114 SER F   76  LYS F   81  1                                   6
HELIX  115 115 HYP F  104  PHE F  108  5                                   5
HELIX  116 116 SER F  112  GLY F  122  1                                  11
HELIX  117 117 ASN F  123  GLY F  126  5                                   4
HELIX  118 118 PRO F  141  LYS F  146  1                                   6
HELIX  119 119 GLY F  154  ASN F  163  1                                  10
HELIX  120 120 SER F  181  GLY F  195  1                                  15
HELIX  121 121 ARG F  213  GLY F  233  1                                  21
HELIX  122 122 THR F  246  VAL F  255  1                                  10
HELIX  123 123 TYR F  269  GLY F  288  1                                  20
HELIX  124 124 MET F  297  ARG F  303  1                                   7
HELIX  125 125 HIS F  310  GLY F  322  1                                  13
HELIX  126 126 GLU F  338  ASP F  351  1                                  14
HELIX  127 127 ARG F  358  GLY F  361  5                                   4
HELIX  128 128 HIS F  383  TRP F  385  5                                   3
HELIX  129 129 HIS F  386  GLY F  395  1                                  10
HELIX  130 130 GLY F  403  GLY F  408  1                                   6
HELIX  131 131 GLY F  412  GLU F  433  1                                  22
HELIX  132 132 ASP F  436  LYS F  463  1                                  28
HELIX  133 133 TYR G   20  TYR G   25  1                                   6
HELIX  134 134 PRO G   49  SER G   61  1                                  13
HELIX  135 135 VAL G   69  THR G   75  5                                   7
HELIX  136 136 SER G   76  LYS G   81  1                                   6
HELIX  137 137 HYP G  104  PHE G  108  5                                   5
HELIX  138 138 SER G  112  GLY G  122  1                                  11
HELIX  139 139 ASN G  123  GLY G  126  5                                   4
HELIX  140 140 PRO G  141  LYS G  146  1                                   6
HELIX  141 141 GLY G  154  ASN G  163  1                                  10
HELIX  142 142 SER G  181  GLY G  195  1                                  15
HELIX  143 143 ARG G  213  GLY G  233  1                                  21
HELIX  144 144 THR G  246  VAL G  255  1                                  10
HELIX  145 145 TYR G  269  GLY G  288  1                                  20
HELIX  146 146 MET G  297  ARG G  303  1                                   7
HELIX  147 147 HIS G  310  GLY G  322  1                                  13
HELIX  148 148 GLU G  338  ASP G  351  1                                  14
HELIX  149 149 ARG G  358  GLY G  361  5                                   4
HELIX  150 150 HIS G  383  TRP G  385  5                                   3
HELIX  151 151 HIS G  386  GLY G  395  1                                  10
HELIX  152 152 GLY G  403  GLY G  408  1                                   6
HELIX  153 153 GLY G  412  GLU G  433  1                                  22
HELIX  154 154 ASP G  436  LYS G  463  1                                  28
HELIX  155 155 TYR H   20  TYR H   25  1                                   6
HELIX  156 156 PRO H   49  SER H   61  1                                  13
HELIX  157 157 VAL H   69  THR H   75  5                                   7
HELIX  158 158 SER H   76  LYS H   81  1                                   6
HELIX  159 159 HYP H  104  PHE H  108  5                                   5
HELIX  160 160 SER H  112  GLY H  122  1                                  11
HELIX  161 161 ASN H  123  GLY H  126  5                                   4
HELIX  162 162 PRO H  141  LYS H  146  1                                   6
HELIX  163 163 GLY H  154  ASN H  163  1                                  10
HELIX  164 164 SER H  181  GLY H  195  1                                  15
HELIX  165 165 ARG H  213  GLY H  233  1                                  21
HELIX  166 166 THR H  246  VAL H  255  1                                  10
HELIX  167 167 TYR H  269  GLY H  288  1                                  20
HELIX  168 168 MET H  297  ARG H  303  1                                   7
HELIX  169 169 HIS H  310  GLY H  322  1                                  13
HELIX  170 170 GLU H  338  ASP H  351  1                                  14
HELIX  171 171 ARG H  358  GLY H  361  5                                   4
HELIX  172 172 HIS H  383  TRP H  385  5                                   3
HELIX  173 173 HIS H  386  GLY H  395  1                                  10
HELIX  174 174 GLY H  403  GLY H  408  1                                   6
HELIX  175 175 GLY H  412  GLU H  433  1                                  22
HELIX  176 176 ASP H  436  LYS H  463  1                                  28
HELIX  177 177 THR I   22  ASN I   36  1                                  15
HELIX  178 178 GLU I   46  ALA I   50  5                                   5
HELIX  179 179 ASN I   54  PHE I   60  5                                   7
HELIX  180 180 ASP I   85  PHE I  100  1                                  16
HELIX  181 181 PRO I  134  ARG I  138  5                                   5
HELIX  182 182 THR J   22  GLY J   37  1                                  16
HELIX  183 183 GLU J   46  ALA J   50  5                                   5
HELIX  184 184 ASN J   54  PHE J   60  5                                   7
HELIX  185 185 ASP J   85  PHE J  100  1                                  16
HELIX  186 186 PRO J  134  ARG J  138  5                                   5
HELIX  187 187 THR K   22  ASN K   36  1                                  15
HELIX  188 188 GLU K   46  ALA K   50  5                                   5
HELIX  189 189 ASN K   54  PHE K   60  5                                   7
HELIX  190 190 ASP K   85  PHE K  100  1                                  16
HELIX  191 191 PRO K  134  ARG K  138  5                                   5
HELIX  192 192 THR L   22  ASN L   36  1                                  15
HELIX  193 193 GLU L   46  ALA L   50  5                                   5
HELIX  194 194 ASN L   54  PHE L   60  5                                   7
HELIX  195 195 ASP L   85  PHE L  100  1                                  16
HELIX  196 196 PRO L  134  ARG L  138  5                                   5
HELIX  197 197 THR M   22  ASN M   36  1                                  15
HELIX  198 198 GLU M   46  ALA M   50  5                                   5
HELIX  199 199 ASN M   54  PHE M   60  5                                   7
HELIX  200 200 ASP M   85  PHE M  100  1                                  16
HELIX  201 201 PRO M  134  ARG M  138  5                                   5
HELIX  202 202 THR N   22  ASN N   36  1                                  15
HELIX  203 203 GLU N   46  ALA N   50  5                                   5
HELIX  204 204 ASN N   54  PHE N   60  5                                   7
HELIX  205 205 ASP N   85  PHE N  100  1                                  16
HELIX  206 206 PRO N  134  ARG N  138  5                                   5
HELIX  207 207 THR O   22  ASN O   36  1                                  15
HELIX  208 208 GLU O   46  ALA O   50  5                                   5
HELIX  209 209 ASN O   54  PHE O   60  5                                   7
HELIX  210 210 ASP O   85  PHE O  100  1                                  16
HELIX  211 211 PRO O  134  ARG O  138  5                                   5
HELIX  212 212 THR P   22  ASN P   36  1                                  15
HELIX  213 213 GLU P   46  ALA P   50  5                                   5
HELIX  214 214 ASN P   54  PHE P   60  5                                   7
HELIX  215 215 ASP P   85  PHE P  100  1                                  16
HELIX  216 216 PRO P  134  ARG P  138  5                                   5
SHEET    1  AA 5 ARG A  83  PRO A  89  0
SHEET    2  AA 5 TYR A  97  TYR A 103 -1  O  ILE A  98   N  GLU A  88
SHEET    3  AA 5 ILE A  36  PRO A  44 -1  O  ILE A  36   N  TYR A 103
SHEET    4  AA 5 LEU A 130  ARG A 139 -1  N  ARG A 131   O  THR A  43
SHEET    5  AA 5 GLY A 308  ILE A 309  1  O  GLY A 308   N  LEU A 135
SHEET    1  AB 8 LEU A 169  GLY A 171  0
SHEET    2  AB 8 CYS A 399  GLN A 401  1  O  LEU A 400   N  GLY A 171
SHEET    3  AB 8 MET A 375  SER A 379  1  O  PRO A 376   N  CYS A 399
SHEET    4  AB 8 HIS A 325  HIS A 327  1  O  LEU A 326   N  VAL A 377
SHEET    5  AB 8 LEU A 290  HIS A 294  1  O  ILE A 293   N  HIS A 327
SHEET    6  AB 8 ILE A 264  ASP A 268  1  O  ILE A 265   N  HIS A 292
SHEET    7  AB 8 GLY A 237  ASN A 241  1  O  LEU A 240   N  MET A 266
SHEET    8  AB 8 PHE A 199  KCX A 201  1  O  THR A 200   N  TYR A 239
SHEET    1  AC 2 TYR A 353  VAL A 354  0
SHEET    2  AC 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  VAL A 354
SHEET    1  BA 5 ARG B  83  PRO B  89  0
SHEET    2  BA 5 TYR B  97  TYR B 103 -1  O  ILE B  98   N  GLU B  88
SHEET    3  BA 5 ILE B  36  PRO B  44 -1  O  ILE B  36   N  TYR B 103
SHEET    4  BA 5 LEU B 130  ARG B 139 -1  N  ARG B 131   O  THR B  43
SHEET    5  BA 5 GLY B 308  ILE B 309  1  O  GLY B 308   N  LEU B 135
SHEET    1  BB 8 LEU B 169  GLY B 171  0
SHEET    2  BB 8 CYS B 399  GLN B 401  1  O  LEU B 400   N  GLY B 171
SHEET    3  BB 8 MET B 375  SER B 379  1  O  PRO B 376   N  CYS B 399
SHEET    4  BB 8 HIS B 325  HIS B 327  1  O  LEU B 326   N  VAL B 377
SHEET    5  BB 8 LEU B 290  HIS B 294  1  O  ILE B 293   N  HIS B 327
SHEET    6  BB 8 ILE B 264  ASP B 268  1  O  ILE B 265   N  HIS B 292
SHEET    7  BB 8 GLY B 237  ASN B 241  1  O  LEU B 240   N  MET B 266
SHEET    8  BB 8 PHE B 199  KCX B 201  1  O  THR B 200   N  TYR B 239
SHEET    1  BC 2 TYR B 353  VAL B 354  0
SHEET    2  BC 2 GLN B 366  ASP B 367 -1  O  GLN B 366   N  VAL B 354
SHEET    1  CA 5 ARG C  83  PRO C  89  0
SHEET    2  CA 5 TYR C  97  TYR C 103 -1  O  ILE C  98   N  GLU C  88
SHEET    3  CA 5 ILE C  36  PRO C  44 -1  O  ILE C  36   N  TYR C 103
SHEET    4  CA 5 LEU C 130  ARG C 139 -1  N  ARG C 131   O  THR C  43
SHEET    5  CA 5 GLY C 308  ILE C 309  1  O  GLY C 308   N  LEU C 135
SHEET    1  CB 8 LEU C 169  GLY C 171  0
SHEET    2  CB 8 CYS C 399  GLN C 401  1  O  LEU C 400   N  GLY C 171
SHEET    3  CB 8 MET C 375  SER C 379  1  O  PRO C 376   N  CYS C 399
SHEET    4  CB 8 HIS C 325  HIS C 327  1  O  LEU C 326   N  VAL C 377
SHEET    5  CB 8 LEU C 290  HIS C 294  1  O  ILE C 293   N  HIS C 327
SHEET    6  CB 8 ILE C 264  ASP C 268  1  O  ILE C 265   N  HIS C 292
SHEET    7  CB 8 GLY C 237  ASN C 241  1  O  LEU C 240   N  MET C 266
SHEET    8  CB 8 PHE C 199  KCX C 201  1  O  THR C 200   N  TYR C 239
SHEET    1  CC 2 TYR C 353  VAL C 354  0
SHEET    2  CC 2 GLN C 366  ASP C 367 -1  O  GLN C 366   N  VAL C 354
SHEET    1  DA 5 ARG D  83  PRO D  89  0
SHEET    2  DA 5 TYR D  97  TYR D 103 -1  O  ILE D  98   N  GLU D  88
SHEET    3  DA 5 ILE D  36  PRO D  44 -1  O  ILE D  36   N  TYR D 103
SHEET    4  DA 5 LEU D 130  ARG D 139 -1  N  ARG D 131   O  THR D  43
SHEET    5  DA 5 GLY D 308  ILE D 309  1  O  GLY D 308   N  LEU D 135
SHEET    1  DB 8 LEU D 169  GLY D 171  0
SHEET    2  DB 8 CYS D 399  GLN D 401  1  O  LEU D 400   N  GLY D 171
SHEET    3  DB 8 MET D 375  SER D 379  1  O  PRO D 376   N  CYS D 399
SHEET    4  DB 8 HIS D 325  HIS D 327  1  O  LEU D 326   N  VAL D 377
SHEET    5  DB 8 LEU D 290  HIS D 294  1  O  ILE D 293   N  HIS D 327
SHEET    6  DB 8 ILE D 264  ASP D 268  1  O  ILE D 265   N  HIS D 292
SHEET    7  DB 8 GLY D 237  ASN D 241  1  O  LEU D 240   N  MET D 266
SHEET    8  DB 8 PHE D 199  KCX D 201  1  O  THR D 200   N  TYR D 239
SHEET    1  DC 2 TYR D 353  VAL D 354  0
SHEET    2  DC 2 GLN D 366  ASP D 367 -1  O  GLN D 366   N  VAL D 354
SHEET    1  EA 5 ARG E  83  PRO E  89  0
SHEET    2  EA 5 TYR E  97  TYR E 103 -1  O  ILE E  98   N  GLU E  88
SHEET    3  EA 5 ILE E  36  PRO E  44 -1  O  ILE E  36   N  TYR E 103
SHEET    4  EA 5 LEU E 130  ARG E 139 -1  N  ARG E 131   O  THR E  43
SHEET    5  EA 5 GLY E 308  ILE E 309  1  O  GLY E 308   N  LEU E 135
SHEET    1  EB 8 LEU E 169  GLY E 171  0
SHEET    2  EB 8 CYS E 399  GLN E 401  1  O  LEU E 400   N  GLY E 171
SHEET    3  EB 8 MET E 375  SER E 379  1  O  PRO E 376   N  CYS E 399
SHEET    4  EB 8 HIS E 325  HIS E 327  1  O  LEU E 326   N  VAL E 377
SHEET    5  EB 8 LEU E 290  HIS E 294  1  O  ILE E 293   N  HIS E 327
SHEET    6  EB 8 ILE E 264  ASP E 268  1  O  ILE E 265   N  HIS E 292
SHEET    7  EB 8 GLY E 237  ASN E 241  1  O  LEU E 240   N  MET E 266
SHEET    8  EB 8 PHE E 199  KCX E 201  1  O  THR E 200   N  TYR E 239
SHEET    1  EC 2 TYR E 353  VAL E 354  0
SHEET    2  EC 2 GLN E 366  ASP E 367 -1  O  GLN E 366   N  VAL E 354
SHEET    1  FA 5 ARG F  83  PRO F  89  0
SHEET    2  FA 5 TYR F  97  TYR F 103 -1  O  ILE F  98   N  GLU F  88
SHEET    3  FA 5 ILE F  36  PRO F  44 -1  O  ILE F  36   N  TYR F 103
SHEET    4  FA 5 LEU F 130  ARG F 139 -1  N  ARG F 131   O  THR F  43
SHEET    5  FA 5 GLY F 308  ILE F 309  1  O  GLY F 308   N  LEU F 135
SHEET    1  FB 8 LEU F 169  GLY F 171  0
SHEET    2  FB 8 CYS F 399  GLN F 401  1  O  LEU F 400   N  GLY F 171
SHEET    3  FB 8 MET F 375  SER F 379  1  O  PRO F 376   N  CYS F 399
SHEET    4  FB 8 HIS F 325  HIS F 327  1  O  LEU F 326   N  VAL F 377
SHEET    5  FB 8 LEU F 290  HIS F 294  1  O  ILE F 293   N  HIS F 327
SHEET    6  FB 8 ILE F 264  ASP F 268  1  O  ILE F 265   N  HIS F 292
SHEET    7  FB 8 GLY F 237  ASN F 241  1  O  LEU F 240   N  MET F 266
SHEET    8  FB 8 PHE F 199  KCX F 201  1  O  THR F 200   N  TYR F 239
SHEET    1  FC 2 TYR F 353  VAL F 354  0
SHEET    2  FC 2 GLN F 366  ASP F 367 -1  O  GLN F 366   N  VAL F 354
SHEET    1  GA 5 ARG G  83  PRO G  89  0
SHEET    2  GA 5 TYR G  97  TYR G 103 -1  O  ILE G  98   N  GLU G  88
SHEET    3  GA 5 ILE G  36  PRO G  44 -1  O  ILE G  36   N  TYR G 103
SHEET    4  GA 5 LEU G 130  ARG G 139 -1  N  ARG G 131   O  THR G  43
SHEET    5  GA 5 GLY G 308  ILE G 309  1  O  GLY G 308   N  LEU G 135
SHEET    1  GB 8 LEU G 169  GLY G 171  0
SHEET    2  GB 8 CYS G 399  GLN G 401  1  O  LEU G 400   N  GLY G 171
SHEET    3  GB 8 MET G 375  SER G 379  1  O  PRO G 376   N  CYS G 399
SHEET    4  GB 8 HIS G 325  HIS G 327  1  O  LEU G 326   N  VAL G 377
SHEET    5  GB 8 LEU G 290  HIS G 294  1  O  ILE G 293   N  HIS G 327
SHEET    6  GB 8 ILE G 264  ASP G 268  1  O  ILE G 265   N  HIS G 292
SHEET    7  GB 8 GLY G 237  ASN G 241  1  O  LEU G 240   N  MET G 266
SHEET    8  GB 8 PHE G 199  KCX G 201  1  O  THR G 200   N  TYR G 239
SHEET    1  GC 2 TYR G 353  VAL G 354  0
SHEET    2  GC 2 GLN G 366  ASP G 367 -1  O  GLN G 366   N  VAL G 354
SHEET    1  HA 5 ARG H  83  PRO H  89  0
SHEET    2  HA 5 TYR H  97  TYR H 103 -1  O  ILE H  98   N  GLU H  88
SHEET    3  HA 5 ILE H  36  PRO H  44 -1  O  ILE H  36   N  TYR H 103
SHEET    4  HA 5 LEU H 130  ARG H 139 -1  N  ARG H 131   O  THR H  43
SHEET    5  HA 5 GLY H 308  ILE H 309  1  O  GLY H 308   N  LEU H 135
SHEET    1  HB 8 LEU H 169  GLY H 171  0
SHEET    2  HB 8 CYS H 399  GLN H 401  1  O  LEU H 400   N  GLY H 171
SHEET    3  HB 8 MET H 375  SER H 379  1  O  PRO H 376   N  CYS H 399
SHEET    4  HB 8 HIS H 325  HIS H 327  1  O  LEU H 326   N  VAL H 377
SHEET    5  HB 8 LEU H 290  HIS H 294  1  O  ILE H 293   N  HIS H 327
SHEET    6  HB 8 ILE H 264  ASP H 268  1  O  ILE H 265   N  HIS H 292
SHEET    7  HB 8 GLY H 237  ASN H 241  1  O  LEU H 240   N  MET H 266
SHEET    8  HB 8 PHE H 199  KCX H 201  1  O  THR H 200   N  TYR H 239
SHEET    1  HC 2 TYR H 353  VAL H 354  0
SHEET    2  HC 2 GLN H 366  ASP H 367 -1  O  GLN H 366   N  VAL H 354
SHEET    1  IA 4 THR I  74  TRP I  76  0
SHEET    2  IA 4 ILE I  39  ALA I  45 -1  O  LEU I  42   N  TRP I  76
SHEET    3  IA 4 TYR I 104  ASP I 111 -1  O  TYR I 104   N  ALA I  45
SHEET    4  IA 4 VAL I 116  GLN I 124 -1  O  VAL I 116   N  ASP I 111
SHEET    1  JA 4 THR J  74  TRP J  76  0
SHEET    2  JA 4 ILE J  39  ALA J  45 -1  O  LEU J  42   N  TRP J  76
SHEET    3  JA 4 TYR J 104  ASP J 111 -1  O  TYR J 104   N  ALA J  45
SHEET    4  JA 4 VAL J 116  GLN J 124 -1  O  VAL J 116   N  ASP J 111
SHEET    1  KA 4 THR K  74  TRP K  76  0
SHEET    2  KA 4 ILE K  39  ALA K  45 -1  O  LEU K  42   N  TRP K  76
SHEET    3  KA 4 TYR K 104  ASP K 111 -1  O  TYR K 104   N  ALA K  45
SHEET    4  KA 4 VAL K 116  GLN K 124 -1  O  VAL K 116   N  ASP K 111
SHEET    1  LA 4 THR L  74  TRP L  76  0
SHEET    2  LA 4 ILE L  39  ALA L  45 -1  O  LEU L  42   N  TRP L  76
SHEET    3  LA 4 TYR L 104  ASP L 111 -1  O  TYR L 104   N  ALA L  45
SHEET    4  LA 4 VAL L 116  GLN L 124 -1  O  VAL L 116   N  ASP L 111
SHEET    1  MA 4 THR M  74  TRP M  76  0
SHEET    2  MA 4 ILE M  39  ALA M  45 -1  O  LEU M  42   N  TRP M  76
SHEET    3  MA 4 TYR M 104  ASP M 111 -1  O  TYR M 104   N  ALA M  45
SHEET    4  MA 4 VAL M 116  GLN M 124 -1  O  VAL M 116   N  ASP M 111
SHEET    1  NA 4 THR N  74  TRP N  76  0
SHEET    2  NA 4 ILE N  39  ALA N  45 -1  O  LEU N  42   N  TRP N  76
SHEET    3  NA 4 TYR N 104  ASP N 111 -1  O  TYR N 104   N  ALA N  45
SHEET    4  NA 4 VAL N 116  GLN N 124 -1  O  VAL N 116   N  ASP N 111
SHEET    1  OA 4 THR O  74  TRP O  76  0
SHEET    2  OA 4 ILE O  39  ALA O  45 -1  O  LEU O  42   N  TRP O  76
SHEET    3  OA 4 TYR O 104  ASP O 111 -1  O  TYR O 104   N  ALA O  45
SHEET    4  OA 4 VAL O 116  GLN O 124 -1  O  VAL O 116   N  ASP O 111
SHEET    1  PA 4 THR P  74  TRP P  76  0
SHEET    2  PA 4 ILE P  39  ALA P  45 -1  O  LEU P  42   N  TRP P  76
SHEET    3  PA 4 TYR P 104  ASP P 111 -1  O  TYR P 104   N  ALA P  45
SHEET    4  PA 4 VAL P 116  GLN P 124 -1  O  VAL P 116   N  ASP P 111
SSBOND   1 CYS A  449    CYS A  459                          1555   1555  2.07
SSBOND   2 CYS B  449    CYS B  459                          1555   1555  2.07
SSBOND   3 CYS C  247    CYS D  247                          1555   1555  2.08
SSBOND   4 CYS C  449    CYS C  459                          1555   1555  2.06
SSBOND   5 CYS D  449    CYS D  459                          1555   1555  2.08
SSBOND   6 CYS E  247    CYS F  247                          1555   1555  2.07
SSBOND   7 CYS F  449    CYS F  459                          1555   1555  2.06
SSBOND   8 CYS G  247    CYS H  247                          1555   1555  2.09
SSBOND   9 CYS G  449    CYS G  459                          1555   1555  2.05
SSBOND  10 CYS H  449    CYS H  459                          1555   1555  2.05
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.34
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.32
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.33
LINK         C   HYP A 151                 N   PRO A 152     1555   1555  1.34
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.33
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.33
LINK         C   VAL A 255                 N   SMC A 256     1555   1555  1.33
LINK         C   SMC A 256                 N   ALA A 257     1555   1555  1.34
LINK         C   TRP A 368                 N   SMC A 369     1555   1555  1.33
LINK         C   SMC A 369                 N   SER A 370     1555   1555  1.33
LINK        MG    MG A1476                 OD1 ASP A 203     1555   1555  1.96
LINK        MG    MG A1476                 OE1 GLU A 204     1555   1555  2.06
LINK        MG    MG A1476                 O3  CAP A1477     1555   1555  2.19
LINK        MG    MG A1476                 O7  CAP A1477     1555   1555  2.10
LINK        MG    MG A1476                 OQ1 KCX A 201     1555   1555  2.05
LINK        MG    MG A1476                 O2  CAP A1477     1555   1555  2.25
LINK         C   TYR B 103                 N   HYP B 104     1555   1555  1.34
LINK         C   HYP B 104                 N   ILE B 105     1555   1555  1.33
LINK         C   GLY B 150                 N   HYP B 151     1555   1555  1.34
LINK         C   HYP B 151                 N   PRO B 152     1555   1555  1.35
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.33
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.33
LINK         C   VAL B 255                 N   SMC B 256     1555   1555  1.33
LINK         C   SMC B 256                 N   ALA B 257     1555   1555  1.33
LINK         C   TRP B 368                 N   SMC B 369     1555   1555  1.34
LINK         C   SMC B 369                 N   SER B 370     1555   1555  1.34
LINK        MG    MG B1476                 O2  CAP B1477     1555   1555  2.29
LINK        MG    MG B1476                 O3  CAP B1477     1555   1555  2.16
LINK        MG    MG B1476                 OQ1 KCX B 201     1555   1555  2.02
LINK        MG    MG B1476                 OD1 ASP B 203     1555   1555  1.97
LINK        MG    MG B1476                 OE1 GLU B 204     1555   1555  2.02
LINK        MG    MG B1476                 O7  CAP B1477     1555   1555  2.06
LINK         C   TYR C 103                 N   HYP C 104     1555   1555  1.35
LINK         C   HYP C 104                 N   ILE C 105     1555   1555  1.33
LINK         C   GLY C 150                 N   HYP C 151     1555   1555  1.34
LINK         C   HYP C 151                 N   PRO C 152     1555   1555  1.34
LINK         C   THR C 200                 N   KCX C 201     1555   1555  1.32
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.33
LINK         C   VAL C 255                 N   SMC C 256     1555   1555  1.33
LINK         C   SMC C 256                 N   ALA C 257     1555   1555  1.34
LINK         C   TRP C 368                 N   SMC C 369     1555   1555  1.34
LINK         C   SMC C 369                 N   SER C 370     1555   1555  1.34
LINK        MG    MG C1476                 OQ1 KCX C 201     1555   1555  2.08
LINK        MG    MG C1476                 OD1 ASP C 203     1555   1555  1.97
LINK        MG    MG C1476                 O2  CAP C1477     1555   1555  2.21
LINK        MG    MG C1476                 O7  CAP C1477     1555   1555  2.09
LINK        MG    MG C1476                 OE1 GLU C 204     1555   1555  2.03
LINK        MG    MG C1476                 O3  CAP C1477     1555   1555  2.19
LINK         C   TYR D 103                 N   HYP D 104     1555   1555  1.34
LINK         C   HYP D 104                 N   ILE D 105     1555   1555  1.33
LINK         C   GLY D 150                 N   HYP D 151     1555   1555  1.34
LINK         C   HYP D 151                 N   PRO D 152     1555   1555  1.34
LINK         C   THR D 200                 N   KCX D 201     1555   1555  1.32
LINK         C   KCX D 201                 N   ASP D 202     1555   1555  1.33
LINK         C   VAL D 255                 N   SMC D 256     1555   1555  1.33
LINK         C   SMC D 256                 N   ALA D 257     1555   1555  1.34
LINK         C   TRP D 368                 N   SMC D 369     1555   1555  1.34
LINK         C   SMC D 369                 N   SER D 370     1555   1555  1.33
LINK        MG    MG D1476                 OE1 GLU D 204     1555   1555  2.00
LINK        MG    MG D1476                 OQ1 KCX D 201     1555   1555  2.04
LINK        MG    MG D1476                 O2  CAP D1477     1555   1555  2.21
LINK        MG    MG D1476                 O7  CAP D1477     1555   1555  2.12
LINK        MG    MG D1476                 OD1 ASP D 203     1555   1555  1.97
LINK        MG    MG D1476                 O3  CAP D1477     1555   1555  2.16
LINK         C   TYR E 103                 N   HYP E 104     1555   1555  1.34
LINK         C   HYP E 104                 N   ILE E 105     1555   1555  1.33
LINK         C   GLY E 150                 N   HYP E 151     1555   1555  1.34
LINK         C   HYP E 151                 N   PRO E 152     1555   1555  1.34
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.33
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.33
LINK         C   VAL E 255                 N   SMC E 256     1555   1555  1.33
LINK         C   SMC E 256                 N   ALA E 257     1555   1555  1.34
LINK         C   TRP E 368                 N   SMC E 369     1555   1555  1.33
LINK         C   SMC E 369                 N   SER E 370     1555   1555  1.33
LINK        MG    MG E1476                 O3  CAP E1477     1555   1555  2.21
LINK        MG    MG E1476                 OD1 ASP E 203     1555   1555  1.95
LINK        MG    MG E1476                 OQ1 KCX E 201     1555   1555  2.07
LINK        MG    MG E1476                 O2  CAP E1477     1555   1555  2.20
LINK        MG    MG E1476                 O7  CAP E1477     1555   1555  2.11
LINK        MG    MG E1476                 OE1 GLU E 204     1555   1555  2.01
LINK         C   TYR F 103                 N   HYP F 104     1555   1555  1.34
LINK         C   HYP F 104                 N   ILE F 105     1555   1555  1.33
LINK         C   GLY F 150                 N   HYP F 151     1555   1555  1.35
LINK         C   HYP F 151                 N   PRO F 152     1555   1555  1.34
LINK         C   THR F 200                 N   KCX F 201     1555   1555  1.33
LINK         C   KCX F 201                 N   ASP F 202     1555   1555  1.33
LINK         C   VAL F 255                 N   SMC F 256     1555   1555  1.34
LINK         C   SMC F 256                 N   ALA F 257     1555   1555  1.33
LINK         C   TRP F 368                 N   SMC F 369     1555   1555  1.33
LINK         C   SMC F 369                 N   SER F 370     1555   1555  1.33
LINK        MG    MG F1476                 OQ1 KCX F 201     1555   1555  2.04
LINK        MG    MG F1476                 O3  CAP F1477     1555   1555  2.13
LINK        MG    MG F1476                 O7  CAP F1477     1555   1555  2.10
LINK        MG    MG F1476                 O2  CAP F1477     1555   1555  2.21
LINK        MG    MG F1476                 OE1 GLU F 204     1555   1555  2.07
LINK        MG    MG F1476                 OD1 ASP F 203     1555   1555  1.96
LINK         C   TYR G 103                 N   HYP G 104     1555   1555  1.34
LINK         C   HYP G 104                 N   ILE G 105     1555   1555  1.33
LINK         C   GLY G 150                 N   HYP G 151     1555   1555  1.33
LINK         C   HYP G 151                 N   PRO G 152     1555   1555  1.35
LINK         C   THR G 200                 N   KCX G 201     1555   1555  1.33
LINK         C   KCX G 201                 N   ASP G 202     1555   1555  1.33
LINK         C   VAL G 255                 N   SMC G 256     1555   1555  1.34
LINK         C   SMC G 256                 N   ALA G 257     1555   1555  1.34
LINK         C   TRP G 368                 N   SMC G 369     1555   1555  1.33
LINK         C   SMC G 369                 N   SER G 370     1555   1555  1.33
LINK        MG    MG G1476                 O2  CAP G1477     1555   1555  2.24
LINK        MG    MG G1476                 O3  CAP G1477     1555   1555  2.14
LINK        MG    MG G1476                 O7  CAP G1477     1555   1555  2.09
LINK        MG    MG G1476                 OQ1 KCX G 201     1555   1555  2.04
LINK        MG    MG G1476                 OD1 ASP G 203     1555   1555  1.98
LINK        MG    MG G1476                 OE1 GLU G 204     1555   1555  2.00
LINK         C   TYR H 103                 N   HYP H 104     1555   1555  1.34
LINK         C   HYP H 104                 N   ILE H 105     1555   1555  1.32
LINK         C   GLY H 150                 N   HYP H 151     1555   1555  1.34
LINK         C   HYP H 151                 N   PRO H 152     1555   1555  1.34
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.32
LINK         C   KCX H 201                 N   ASP H 202     1555   1555  1.33
LINK         C   VAL H 255                 N   SMC H 256     1555   1555  1.33
LINK         C   SMC H 256                 N   ALA H 257     1555   1555  1.33
LINK         C   TRP H 368                 N   SMC H 369     1555   1555  1.33
LINK         C   SMC H 369                 N   SER H 370     1555   1555  1.33
LINK        MG    MG H1476                 O2  CAP H1477     1555   1555  2.22
LINK        MG    MG H1476                 OQ1 KCX H 201     1555   1555  2.03
LINK        MG    MG H1476                 O3  CAP H1477     1555   1555  2.12
LINK        MG    MG H1476                 OE1 GLU H 204     1555   1555  2.03
LINK        MG    MG H1476                 OD1 ASP H 203     1555   1555  1.99
LINK        MG    MG H1476                 O7  CAP H1477     1555   1555  2.14
LINK         C   MME I   1                 N   MET I   2     1555   1555  1.33
LINK         C   MME J   1                 N   MET J   2     1555   1555  1.33
LINK         C   MME K   1                 N   MET K   2     1555   1555  1.33
LINK         C   MME L   1                 N   MET L   2     1555   1555  1.33
LINK         C   MME M   1                 N   MET M   2     1555   1555  1.33
LINK         C   MME N   1                 N   MET N   2     1555   1555  1.33
LINK         C   MME O   1                 N   MET O   2     1555   1555  1.33
LINK         C   MME P   1                 N   MET P   2     1555   1555  1.33
SITE     1 AC1  5 LYS A 177  KCX A 201  ASP A 203  GLU A 204
SITE     2 AC1  5 CAP A1477
SITE     1 AC2 28 THR A 173  LYS A 175  LYS A 177  KCX A 201
SITE     2 AC2 28 ASP A 203  GLU A 204  HIS A 294  ARG A 295
SITE     3 AC2 28 HIS A 327  LYS A 334  LEU A 335  SER A 379
SITE     4 AC2 28 GLY A 380  GLY A 381  GLY A 403  GLY A 404
SITE     5 AC2 28 HOH A1139  HOH A1315  HOH A1316  HOH A1317
SITE     6 AC2 28 HOH A1318  HOH A1319   MG A1476  GLU B  60
SITE     7 AC2 28 THR B  65  TRP B  66  ASN B 123  HOH B1109
SITE     1 AC3  5 LYS B 177  KCX B 201  ASP B 203  GLU B 204
SITE     2 AC3  5 CAP B1477
SITE     1 AC4 29 GLU A  60  THR A  65  TRP A  66  ASN A 123
SITE     2 AC4 29 HOH A1049  HOH A1103  THR B 173  LYS B 175
SITE     3 AC4 29 LYS B 177  KCX B 201  ASP B 203  GLU B 204
SITE     4 AC4 29 HIS B 294  ARG B 295  HIS B 327  LYS B 334
SITE     5 AC4 29 LEU B 335  SER B 379  GLY B 380  GLY B 381
SITE     6 AC4 29 GLY B 403  GLY B 404  HOH B1264  HOH B1326
SITE     7 AC4 29 HOH B1327  HOH B1328  HOH B1329  HOH B1330
SITE     8 AC4 29  MG B1476
SITE     1 AC5  5 LYS C 177  KCX C 201  ASP C 203  GLU C 204
SITE     2 AC5  5 CAP C1477
SITE     1 AC6 29 THR C 173  LYS C 175  LYS C 177  KCX C 201
SITE     2 AC6 29 ASP C 203  GLU C 204  HIS C 294  ARG C 295
SITE     3 AC6 29 HIS C 327  LYS C 334  LEU C 335  SER C 379
SITE     4 AC6 29 GLY C 380  GLY C 381  GLY C 403  GLY C 404
SITE     5 AC6 29 HOH C1136  HOH C1308  HOH C1309  HOH C1310
SITE     6 AC6 29 HOH C1311  HOH C1312   MG C1476  GLU D  60
SITE     7 AC6 29 THR D  65  TRP D  66  ASN D 123  HOH D1038
SITE     8 AC6 29 HOH D1098
SITE     1 AC7  4 KCX D 201  ASP D 203  GLU D 204  CAP D1477
SITE     1 AC8 30 GLU C  60  THR C  65  TRP C  66  ASN C 123
SITE     2 AC8 30 HOH C1044  HOH C1047  HOH C1105  THR D 173
SITE     3 AC8 30 LYS D 175  LYS D 177  KCX D 201  ASP D 203
SITE     4 AC8 30 GLU D 204  HIS D 294  ARG D 295  HIS D 327
SITE     5 AC8 30 LYS D 334  LEU D 335  SER D 379  GLY D 380
SITE     6 AC8 30 GLY D 381  GLY D 403  GLY D 404  HOH D1319
SITE     7 AC8 30 HOH D1320  HOH D1321  HOH D1322  HOH D1323
SITE     8 AC8 30 HOH D1324   MG D1476
SITE     1 AC9  5 LYS E 177  KCX E 201  ASP E 203  GLU E 204
SITE     2 AC9  5 CAP E1477
SITE     1 BC1 29 THR E 173  LYS E 175  LYS E 177  KCX E 201
SITE     2 BC1 29 ASP E 203  GLU E 204  HIS E 294  ARG E 295
SITE     3 BC1 29 HIS E 327  LYS E 334  LEU E 335  SER E 379
SITE     4 BC1 29 GLY E 380  GLY E 381  GLY E 403  GLY E 404
SITE     5 BC1 29 HOH E1270  HOH E1336  HOH E1337  HOH E1338
SITE     6 BC1 29 HOH E1339  HOH E1340   MG E1476  GLU F  60
SITE     7 BC1 29 THR F  65  TRP F  66  ASN F 123  HOH F1048
SITE     8 BC1 29 HOH F1107
SITE     1 BC2  5 LYS F 177  KCX F 201  ASP F 203  GLU F 204
SITE     2 BC2  5 CAP F1477
SITE     1 BC3 28 GLU E  60  THR E  65  TRP E  66  ASN E 123
SITE     2 BC3 28 HOH E1107  THR F 173  LYS F 175  LYS F 177
SITE     3 BC3 28 KCX F 201  ASP F 203  GLU F 204  HIS F 294
SITE     4 BC3 28 ARG F 295  HIS F 327  LYS F 334  LEU F 335
SITE     5 BC3 28 SER F 379  GLY F 380  GLY F 381  GLY F 403
SITE     6 BC3 28 GLY F 404  HOH F1264  HOH F1317  HOH F1318
SITE     7 BC3 28 HOH F1319  HOH F1320  HOH F1321   MG F1476
SITE     1 BC4  4 KCX G 201  ASP G 203  GLU G 204  CAP G1477
SITE     1 BC5 28 THR G 173  LYS G 175  LYS G 177  KCX G 201
SITE     2 BC5 28 ASP G 203  GLU G 204  HIS G 294  ARG G 295
SITE     3 BC5 28 HIS G 327  LYS G 334  LEU G 335  SER G 379
SITE     4 BC5 28 GLY G 380  GLY G 381  GLY G 403  GLY G 404
SITE     5 BC5 28 HOH G1136  HOH G1312  HOH G1313  HOH G1314
SITE     6 BC5 28 HOH G1315  HOH G1316   MG G1476  GLU H  60
SITE     7 BC5 28 THR H  65  TRP H  66  ASN H 123  HOH H1110
SITE     1 BC6  5 LYS H 177  KCX H 201  ASP H 203  GLU H 204
SITE     2 BC6  5 CAP H1477
SITE     1 BC7 30 GLU G  60  THR G  65  TRP G  66  ASN G 123
SITE     2 BC7 30 HOH G1043  HOH G1045  HOH G1102  THR H 173
SITE     3 BC7 30 LYS H 175  LYS H 177  KCX H 201  ASP H 203
SITE     4 BC7 30 GLU H 204  HIS H 294  ARG H 295  HIS H 327
SITE     5 BC7 30 LYS H 334  LEU H 335  SER H 379  GLY H 380
SITE     6 BC7 30 GLY H 381  GLY H 403  GLY H 404  HOH H1150
SITE     7 BC7 30 HOH H1320  HOH H1321  HOH H1322  HOH H1323
SITE     8 BC7 30 HOH H1324   MG H1476
SITE     1 BC8  7 TYR A  24  THR A  68  VAL A  69  ASP A  72
SITE     2 BC8  7 HOH A1059  HOH A1320  HOH A1321
SITE     1 BC9  9 GLY A  16  VAL A  17  LYS A  18  THR A  65
SITE     2 BC9  9 TRP A  66  THR A  67  THR A  68  HOH A1023
SITE     3 BC9  9 HOH A1321
SITE     1 CC1  3 GLU A  52  EDO A1484  HOH B1333
SITE     1 CC2  6 LYS A 466  PHE A 467  GLU A 468  PHE A 469
SITE     2 CC2  6 HOH A1322  HOH A1323
SITE     1 CC3  7 ARG A 295  HIS A 298  PHE A 311  SER A 328
SITE     2 CC3  7 GLU A 336  PHE A 345  HOH A1324
SITE     1 CC4  8 TYR C  24  GLY C  64  THR C  68  VAL C  69
SITE     2 CC4  8 ASP C  72  HOH C1049  HOH C1313  HOH C1314
SITE     1 CC5  8 VAL C  17  LYS C  18  THR C  65  TRP C  66
SITE     2 CC5  8 THR C  67  THR C  68  HOH C1314  HOH C1315
SITE     1 CC6  2 GLU C  52  HOH D1330
SITE     1 CC7  6 LYS C 466  PHE C 467  GLU C 468  PHE C 469
SITE     2 CC7  6 HOH C1316  HOH D1328
SITE     1 CC8  5 ARG C 295  PHE C 345  ASP C 473  HOH C1317
SITE     2 CC8  5 HOH C1318
SITE     1 CC9 10 TYR E  24  GLY E  64  THR E  68  VAL E  69
SITE     2 CC9 10 ASP E  72  LEU E  77  HOH E1057  HOH E1341
SITE     3 CC9 10 HOH E1342  EDO E1479
SITE     1 DC1  8 LYS E  18  THR E  65  TRP E  66  THR E  67
SITE     2 DC1  8 THR E  68  HOH E1021  HOH E1342  EDO E1478
SITE     1 DC2  3 GLU E  52  HOH E1010  HOH F1328
SITE     1 DC3  6 LYS E 466  PHE E 467  GLU E 468  PHE E 469
SITE     2 DC3  6 HOH E1343  HOH E1344
SITE     1 DC4  9 TYR G  24  GLY G  64  THR G  68  VAL G  69
SITE     2 DC4  9 ASP G  72  HOH G1317  HOH G1318  HOH G1319
SITE     3 DC4  9 EDO G1479
SITE     1 DC5 10 GLY G  16  VAL G  17  LYS G  18  THR G  65
SITE     2 DC5 10 TRP G  66  THR G  67  THR G  68  HOH G1012
SITE     3 DC5 10 HOH G1319  EDO G1478
SITE     1 DC6  2 GLU G  52  HOH H1330
SITE     1 DC7  6 LYS G 466  PHE G 467  GLU G 468  PHE G 469
SITE     2 DC7  6 HOH G1320  HOH G1321
SITE     1 DC8  7 ARG G 295  HIS G 298  PHE G 345  ASP G 473
SITE     2 DC8  7 HOH G1322  HOH G1323  HOH G1324
SITE     1 DC9  6 TYR C 226  LYS C 227  HOH C1166  LYS I  49
SITE     2 DC9  6 GLU I  55  HOH I1052
SITE     1 EC1  6 TYR E 226  HOH E1176  LYS K  49  GLU K  55
SITE     2 EC1  6 HOH K1056  HOH K1057
SITE     1 EC2  6 GLY K  37  TRP K  38  ILE K  39  PHE K  81
SITE     2 EC2  6 GLY K  82  CYS K  83
SITE     1 EC3  5 TYR G 226  LYS M  49  GLU M  55  HOH M1054
SITE     2 EC3  5 HOH M1112
SITE     1 EC4  5 GLY M  37  TRP M  38  ILE M  39  GLY M  82
SITE     2 EC4  5 CYS M  83
SITE     1 EC5  5 TYR A 226  LYS O  49  GLU O  55  HOH O1061
SITE     2 EC5  5 HOH O1113
SITE     1 EC6  6 GLY O  37  TRP O  38  ILE O  39  PHE O  81
SITE     2 EC6  6 GLY O  82  CYS O  83
SITE     1 EC7  4 LEU E 270  LEU F 270  HOH F1322  HOH F1323
SITE     1 EC8  4 LEU A 270  HOH A1325  HOH A1326  LEU B 270
SITE     1 EC9  4 LEU G 270  LEU H 270  HOH H1325  HOH H1326
SITE     1 FC1  9 TYR B  24  GLY B  64  THR B  68  VAL B  69
SITE     2 FC1  9 ASP B  72  HOH B1051  HOH B1057  HOH B1331
SITE     3 FC1  9 EDO B1479
SITE     1 FC2 10 GLY B  16  VAL B  17  LYS B  18  THR B  65
SITE     2 FC2 10 TRP B  66  THR B  67  THR B  68  HOH B1331
SITE     3 FC2 10 HOH B1332  EDO B1478
SITE     1 FC3  2 HOH A1322  GLU B  52
SITE     1 FC4  5 LYS B 466  PHE B 467  GLU B 468  PHE B 469
SITE     2 FC4  5 HOH B1333
SITE     1 FC5  5 ARG B 295  ASP B 302  GLU B 336  PHE B 345
SITE     2 FC5  5 HOH B1334
SITE     1 FC6  9 TYR H  24  GLY H  64  THR H  68  VAL H  69
SITE     2 FC6  9 ASP H  72  HOH H1051  HOH H1056  HOH H1327
SITE     3 FC6  9 EDO H1480
SITE     1 FC7 10 GLY H  16  VAL H  17  LYS H  18  THR H  65
SITE     2 FC7 10 TRP H  66  THR H  67  THR H  68  HOH H1327
SITE     3 FC7 10 HOH H1328  EDO H1479
SITE     1 FC8  2 HOH G1321  GLU H  52
SITE     1 FC9  5 LYS H 466  PHE H 467  GLU H 468  PHE H 469
SITE     2 FC9  5 HOH H1330
SITE     1 GC1  9 TYR F  24  GLY F  64  THR F  68  VAL F  69
SITE     2 GC1  9 ASP F  72  HOH F1058  HOH F1324  HOH F1326
SITE     3 GC1  9 EDO F1480
SITE     1 GC2  9 GLY F  16  LYS F  18  THR F  65  TRP F  66
SITE     2 GC2  9 THR F  67  THR F  68  HOH F1325  HOH F1326
SITE     3 GC2  9 EDO F1479
SITE     1 GC3  2 HOH E1343  GLU F  52
SITE     1 GC4  5 LYS F 466  PHE F 467  GLU F 468  PHE F 469
SITE     2 GC4  5 HOH F1328
SITE     1 GC5  6 ARG F 295  HIS F 298  GLU F 336  PHE F 345
SITE     2 GC5  6 HOH F1329  HOH F1330
SITE     1 GC6  9 TYR D  24  GLY D  64  THR D  68  VAL D  69
SITE     2 GC6  9 ASP D  72  HOH D1325  HOH D1326  HOH D1327
SITE     3 GC6  9 EDO D1479
SITE     1 GC7  9 GLY D  16  LYS D  18  THR D  65  TRP D  66
SITE     2 GC7  9 THR D  67  THR D  68  HOH D1016  HOH D1327
SITE     3 GC7  9 EDO D1478
SITE     1 GC8  3 GLU D  52  HOH D1006  HOH D1328
SITE     1 GC9  6 LYS D 466  PHE D 467  GLU D 468  PHE D 469
SITE     2 GC9  6 HOH D1329  HOH D1330
SITE     1 HC1  6 TYR H 226  HOH H1180  LYS J  49  GLU J  55
SITE     2 HC1  6 HOH J1057  HOH J1059
SITE     1 HC2  7 GLY J  37  TRP J  38  ILE J  39  PHE J  81
SITE     2 HC2  7 GLY J  82  CYS J  83  HOH J1106
SITE     1 HC3  5 TYR F 226  HOH F1173  LYS P  49  GLU P  55
SITE     2 HC3  5 HOH P1058
SITE     1 HC4  7 GLY P  37  TRP P  38  ILE P  39  PHE P  81
SITE     2 HC4  7 GLY P  82  CYS P  83  HOH P1100
SITE     1 HC5  7 TYR D 226  LYS D 227  LYS N  49  GLU N  55
SITE     2 HC5  7 HOH N1058  HOH N1059  HOH N1110
SITE     1 HC6  7 GLY N  37  TRP N  38  ILE N  39  PHE N  81
SITE     2 HC6  7 GLY N  82  CYS N  83  HOH N1111
SITE     1 HC7  4 LEU C 270  HOH C1319  HOH C1320  LEU D 270
SITE     1 HC8  4 GLY A  47  PRO A  49  HOH A1327  EDO A1480
SITE     1 HC9  4 GLY I  37  TRP I  38  ILE I  39  GLY I  82
SITE     1 IC1  6 ARG D 295  HIS D 298  PHE D 345  ASP D 473
SITE     2 IC1  6 HOH D1331  HOH D1332
SITE     1 IC2  6 TYR B 226  HOH B1181  LYS L  49  GLU L  55
SITE     2 IC2  6 HOH L1059  HOH L1060
SITE     1 IC3  7 GLY L  37  TRP L  38  ILE L  39  PHE L  81
SITE     2 IC3  7 GLY L  82  CYS L  83  HOH L1111
CRYST1  129.906  196.629  201.950  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      0.007698  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005086  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004952        0.00000
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1
MTRIX1   2  0.105300  0.704300 -0.702100       51.25000    1
MTRIX2   2  0.703600 -0.551700 -0.447900      150.00000    1
MTRIX3   2 -0.702800 -0.446800 -0.553600      231.00000    1
MTRIX1   3  0.430900 -0.058090  0.900500      -43.37000    1
MTRIX2   3 -0.802900  0.430800  0.412000       66.21000    1
MTRIX3   3 -0.411900 -0.900600  0.139000      193.10000    1
MTRIX1   4 -0.628700 -0.067550 -0.774700      178.00000    1
MTRIX2   4 -0.068450 -0.987500  0.141700      184.90000    1
MTRIX3   4 -0.774600  0.142100  0.616200       69.14000    1
MTRIX1   5 -0.139400 -0.860600  0.489800      107.80000    1
MTRIX2   5 -0.860600 -0.139400 -0.489800      209.20000    1
MTRIX3   5  0.489800 -0.489800 -0.721300      178.10000    1
MTRIX1   6 -0.964600  0.156200  0.212700       84.80000    1
MTRIX2   6  0.156400 -0.310700  0.937500       31.03000    1
MTRIX3   6  0.212500  0.937600  0.275300      -36.92000    1
MTRIX1   7  0.430300 -0.803400 -0.411700      151.30000    1
MTRIX2   7 -0.055740  0.431500 -0.900400      142.50000    1
MTRIX3   7  0.901000  0.410400  0.140900      -15.06000    1
MTRIX1   8 -0.232200  0.929300  0.287300      -42.22000    1
MTRIX2   8  0.930300  0.125900  0.344600       -3.61500    1
MTRIX3   8  0.284100  0.347300 -0.893700      125.00000    1
MTRIX1   9  0.103700  0.705100 -0.701500       51.09000    1
MTRIX2   9  0.704600 -0.549900 -0.448500      149.90000    1
MTRIX3   9 -0.701900 -0.447800 -0.553900      231.10000    1
MTRIX1  10  0.429500 -0.059760  0.901100      -43.19000    1
MTRIX2  10 -0.803800  0.429500  0.411600       66.39000    1
MTRIX3  10 -0.411600 -0.901100  0.136500      193.40000    1
MTRIX1  11 -0.629100 -0.067810 -0.774400      178.00000    1
MTRIX2  11 -0.068930 -0.987400  0.142500      184.70000    1
MTRIX3  11 -0.774300  0.143000  0.616500       69.03000    1
MTRIX1  12 -0.139100 -0.860300  0.490500      107.70000    1
MTRIX2  12 -0.861000 -0.139600 -0.489100      209.10000    1
MTRIX3  12  0.489300 -0.490300 -0.721200      178.20000    1
MTRIX1  13 -0.964500  0.157000  0.212300       84.77000    1
MTRIX2  13  0.156000 -0.310000  0.937800       30.94000    1
MTRIX3  13  0.213000  0.937700  0.274500      -36.88000    1
MTRIX1  14  0.430500 -0.802400 -0.413300      151.40000    1
MTRIX2  14 -0.054840  0.433800 -0.899300      142.20000    1
MTRIX3  14  0.900900  0.409800  0.142800      -15.17000    1
MTRIX1  15 -0.230400  0.929300  0.288500      -42.37000    1
MTRIX2  15  0.930100  0.123300  0.345900       -3.38100    1
MTRIX3  15  0.285900  0.348100 -0.892800      124.70000    1
      
PROCHECK
Go to PROCHECK summary
 References