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PDBsum entry 1uzh

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1uzh
Jmol
Contents
Protein chains
(+ 2 more) 465 a.a.
(+ 2 more) 122 a.a.
Ligands
CAP ×8
EDO ×50
Metals
_MG ×8
Waters ×2831
HEADER    LYASE                                   12-MAR-04   1UZH
TITLE     A CHIMERIC CHLAMYDOMONAS, SYNECHOCOCCUS RUBISCO ENZYME
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   3 CHAIN: A, B, E, H, K, O, R, V;
COMPND   4 SYNONYM: RUBISCO LARGE SUBUNIT, RIBULOSE-1,5 BISPHOSPHATE
COMPND   5  CARBOXYLASE LARGE CHAIN;
COMPND   6 EC: 4.1.1.39;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 2,
COMPND   9  RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN;
COMPND  10 CHAIN: I, C, F, J, P, T, M, W;
COMPND  11 SYNONYM: RUBISCO SMALL SUBUNIT 1,CHLOROPLAST, RUBISCO
COMPND  12  SMALL SUBUNIT 2,OXYGENASE, RIBULOSE-1,5 BISPHOSPHATE
COMPND  13  CARBOXYLASE/OXYGENASE;
COMPND  14 EC: 4.1.1.39;
COMPND  15 OTHER_DETAILS: LOOP BA-BB OF SMALL SUBUNIT CHLAMYDOMONAS
COMPND  16  RUBISCO, RESIDUES E47 - R71 HAS BEEN REPLACED WITH THE
COMPND  17  CORRESPONDING LOOP OF SYNECHOCOCCUSS, RESIDUES H47 - F53
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE   3 ORGANISM_TAXID: 3055;
SOURCE   4 MOL_ID: 2;
SOURCE   5 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII,
SOURCE   6  SYNECHOCOCCUS SP
KEYWDS    LYASE, RUBISCO, PHOTOSYNTHESIS, CARBON DIOXIDE FIXATION,
KEYWDS   2 PHOTORESPIRATION, OXIDOREDUCTASE, MONOOXYGENASE,
KEYWDS   3 CHLOROPLAST, TRANSIT PEPTIDE, MULTIGENE FAMILY
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.KARKEHABADI,R.J.SPREITZER,I.ANDERSSON
REVDAT   3   24-FEB-09 1UZH    1       VERSN
REVDAT   2   27-JUL-05 1UZH    1       JRNL
REVDAT   1   31-MAY-05 1UZH    0
JRNL        AUTH   S.KARKEHABADI,S.R.PEDDI,M.ANWARUZZAMAN,T.C.TAYLOR,
JRNL        AUTH 2 A.CEDERLUND,T.GENKOV,I.ANDERSSON,R.J.SPREITZER
JRNL        TITL   CHIMERIC SMALL SUBUNITS INFLUENCE CATALYSIS
JRNL        TITL 2 WITHOUT CAUSING GLOBAL CONFORMATIONAL CHANGES IN
JRNL        TITL 3 THE CRYSTAL STRUCTURE OF RIBULOSE-1,5-BISPHOSPHATE
JRNL        TITL 4 CARBOXYLASE/OXYGENASE
JRNL        REF    BIOCHEMISTRY                  V.  44  9851 2005
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   16026157
JRNL        DOI    10.1021/BI050537V
REMARK   2
REMARK   2 RESOLUTION.    2.2  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.3
REMARK   3   NUMBER OF REFLECTIONS             : 237038
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) : 0.162
REMARK   3   R VALUE            (WORKING SET) : 0.160
REMARK   3   FREE R VALUE                     : 0.193
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 12557
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 13878
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120
REMARK   3   BIN FREE R VALUE SET COUNT          : 679
REMARK   3   BIN FREE R VALUE                    : 0.2490
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 37014
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 712
REMARK   3   SOLVENT ATOMS            : 2831
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.18
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.94000
REMARK   3    B33 (A**2) : -0.94000
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): 0.274
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.186
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.124
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.913
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 38620 ; 0.013 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 52270 ; 1.235 ; 1.952
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4706 ; 5.889 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5536 ; 0.089 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 29648 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 19454 ; 0.200 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  3178 ; 0.140 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     5 ; 0.035 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    70 ; 0.344 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.170 ; 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): 23472 ; 1.084 ; 3.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 37683 ; 2.007 ; 5.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 15148 ; 3.142 ; 6.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 14585 ; 4.394 ; 8.000
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B E H K O R V
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     12       A     475      1
REMARK   3           1     B     12       B     475      1
REMARK   3           1     E     12       E     475      1
REMARK   3           1     H     12       H     475      1
REMARK   3           1     K     12       K     475      1
REMARK   3           1     O     12       O     475      1
REMARK   3           1     R     12       R     475      1
REMARK   3           1     V     12       V     475      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3603 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    B    (A):   3603 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    E    (A):   3603 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    H    (A):   3603 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    K    (A):   3603 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    O    (A):   3603 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    R    (A):   3603 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    V    (A):   3603 ;  0.04 ;  0.05
REMARK   3   TIGHT THERMAL      1    A (A**2):   3603 ;  0.14 ;  0.50
REMARK   3   TIGHT THERMAL      1    B (A**2):   3603 ;  0.14 ;  0.50
REMARK   3   TIGHT THERMAL      1    E (A**2):   3603 ;  0.14 ;  0.50
REMARK   3   TIGHT THERMAL      1    H (A**2):   3603 ;  0.15 ;  0.50
REMARK   3   TIGHT THERMAL      1    K (A**2):   3603 ;  0.14 ;  0.50
REMARK   3   TIGHT THERMAL      1    O (A**2):   3603 ;  0.14 ;  0.50
REMARK   3   TIGHT THERMAL      1    R (A**2):   3603 ;  0.14 ;  0.50
REMARK   3   TIGHT THERMAL      1    V (A**2):   3603 ;  0.15 ;  0.50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : I C F J P T M W
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     I      1       I     122      1
REMARK   3           1     C      1       C     122      1
REMARK   3           1     F      1       F     122      1
REMARK   3           1     J      1       J     122      1
REMARK   3           1     P      1       P     122      1
REMARK   3           1     T      1       T     122      1
REMARK   3           1     M      1       M     122      1
REMARK   3           1     W      1       W     122      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   2    I    (A):    989 ;  0.03 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    C    (A):    989 ;  0.03 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    F    (A):    989 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    J    (A):    989 ;  0.03 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    P    (A):    989 ;  0.03 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    T    (A):    989 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    M    (A):    989 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    W    (A):    989 ;  0.04 ;  0.05
REMARK   3   TIGHT THERMAL      2    I (A**2):    989 ;  0.11 ;  0.50
REMARK   3   TIGHT THERMAL      2    C (A**2):    989 ;  0.11 ;  0.50
REMARK   3   TIGHT THERMAL      2    F (A**2):    989 ;  0.11 ;  0.50
REMARK   3   TIGHT THERMAL      2    J (A**2):    989 ;  0.12 ;  0.50
REMARK   3   TIGHT THERMAL      2    P (A**2):    989 ;  0.11 ;  0.50
REMARK   3   TIGHT THERMAL      2    T (A**2):    989 ;  0.12 ;  0.50
REMARK   3   TIGHT THERMAL      2    M (A**2):    989 ;  0.11 ;  0.50
REMARK   3   TIGHT THERMAL      2    W (A**2):    989 ;  0.13 ;  0.50
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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: NULL
REMARK   4
REMARK   4 1UZH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAR-04.
REMARK 100 THE PDBE ID CODE IS EBI-14781.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-03
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID29
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97620
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   : 277345
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.2
REMARK 200  DATA REDUNDANCY                : 20.500
REMARK 200  R MERGE                    (I) : 0.14800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 8.6500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.6
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.44400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1GK8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES PH 7.5, 8-12% PEG 4
REMARK 280  50 MM NAHCO3, 5 MM MGCL2, 50 UM 2-CABP, 18 DEG C, 10-15 MG
REMARK 280  PROTEIN
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000      110.41000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      111.98450
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      110.41000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      111.98450
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 300
REMARK 300 DETAILS:FOR THE HETERO-ASSEMBLY DESCRIBED BY REMARK
REMARK 300  350
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 APPLY THE FOLLOWING TO CHAINS: A,  B, E, H, K, O, R, V, I,
REMARK 350                    AND CHAINS: C, F, J, P, T, M, W
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  RUBISCO CATALYZES TWO REACTIONS: THE CARBOXYLATION OF D-
REMARK 400  RIBULOSE 1,5-BISPHOSPHATE, THE PRIMARY EVENT IN
REMARK 400  PHOTOSYNTHETIC CARBON DIOXIDE FIXATION, AS WELL AS THE
REMARK 400  OXIDATIVE FRAGMENTATION OF THE PENTOSE SUBSTRATE IN THE
REMARK 400  PHOTORESPIRATION PROCESS. BOTH REACTIONS OCCUR SIMULTANEOUSLY
REMARK 400  AND IN COMPETITION AT THE SAME ACTIVE SITE.
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     ALA A     9
REMARK 465     GLY A    10
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 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     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     MET K     1
REMARK 465     VAL K     2
REMARK 465     PRO K     3
REMARK 465     GLN K     4
REMARK 465     THR K     5
REMARK 465     GLU K     6
REMARK 465     MET O     1
REMARK 465     VAL O     2
REMARK 465     PRO O     3
REMARK 465     GLN O     4
REMARK 465     THR O     5
REMARK 465     GLU O     6
REMARK 465     MET R     1
REMARK 465     VAL R     2
REMARK 465     PRO R     3
REMARK 465     GLN R     4
REMARK 465     THR R     5
REMARK 465     GLU R     6
REMARK 465     MET V     1
REMARK 465     VAL V     2
REMARK 465     PRO V     3
REMARK 465     GLN V     4
REMARK 465     THR V     5
REMARK 465     GLU V     6
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   NH1  ARG A    21  -  O    HOH A  2015              1.89
REMARK 500   OG1  THR B   471  -  O    HOH B  2299              1.89
REMARK 500   CG   MET H   375  -  O    HOH H  2185              2.00
REMARK 500   OG1  THR H   471  -  O    HOH H  2272              2.06
REMARK 500   OG1  THR O   471  -  O    HOH O  2273              1.99
REMARK 500   NZ   LYS R   450  -  O    HOH R  2278              2.14
REMARK 500   OG1  THR V   471  -  O    HOH V  2269              2.10
REMARK 500   O    HOH I  2060  -  O    HOH I  2064              2.14
REMARK 500   O    HOH R  2040  -  O    HOH H  2267              2.15
REMARK 500   O    HOH V  2138  -  O    HOH V  2142              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A 160   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP B 203   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP C 113   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ASP F 113   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ASP H 203   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ASP I 113   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP J 113   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ASP M 113   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP O 203   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP P  23   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP P 113   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES
REMARK 500    ASP T 113   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ASP V  33   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP V 203   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP V 352   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP W 113   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 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      -79.73   -141.53
REMARK 500    THR A  75     -164.36   -123.05
REMARK 500    CYS A 172      117.94   -178.36
REMARK 500    ASN A 207      -92.75   -120.97
REMARK 500    MET A 212      109.08   -162.48
REMARK 500    ALA A 296      131.29    -33.75
REMARK 500    MET A 297       -9.44     85.88
REMARK 500    VAL A 331      -54.17     69.33
REMARK 500    ASP A 357       93.72   -162.63
REMARK 500    THR A 406      -53.58   -121.34
REMARK 500    SER B  62      -81.95   -140.07
REMARK 500    THR B  75     -163.71   -124.61
REMARK 500    CYS B 172      122.55   -171.85
REMARK 500    ASN B 207      -90.41   -120.08
REMARK 500    MET B 212      108.43   -162.59
REMARK 500    ALA B 296      134.04    -37.80
REMARK 500    MET B 297      -13.64     87.42
REMARK 500    VAL B 331      -53.67     71.17
REMARK 500    ASP B 357       90.98   -162.68
REMARK 500    ASN C   8       59.68     33.84
REMARK 500    GLU C  13     -146.10     62.48
REMARK 500    PHE C  15       -2.14     85.79
REMARK 500    LYS C  59     -122.55     57.00
REMARK 500    SER E  62      -84.12   -138.42
REMARK 500    THR E  65     -168.04   -128.08
REMARK 500    THR E  75     -163.06   -121.10
REMARK 500    CYS E 172      121.45   -176.06
REMARK 500    ASN E 207      -94.44   -119.04
REMARK 500    MET E 212      111.07   -160.97
REMARK 500    ALA E 296      130.99    -34.20
REMARK 500    MET E 297      -14.54     86.61
REMARK 500    VAL E 331      -54.98     71.01
REMARK 500    ASP E 357       89.24   -163.80
REMARK 500    THR E 406      -56.69   -121.29
REMARK 500    PHE F  12       45.53   -140.09
REMARK 500    GLU F  13     -146.37     63.90
REMARK 500    PHE F  15       -3.86     83.94
REMARK 500    LYS F  59     -121.01     53.34
REMARK 500    SER H  62      -78.82   -137.78
REMARK 500    THR H  65     -167.17   -127.52
REMARK 500    THR H  75     -160.22   -120.08
REMARK 500    CYS H 172      120.80   -176.64
REMARK 500    ASN H 207      -94.93   -121.24
REMARK 500    ALA H 296      132.02    -33.01
REMARK 500    MET H 297       -9.67     86.54
REMARK 500    VAL H 331      -52.51     67.90
REMARK 500    ASP H 357       90.32   -161.69
REMARK 500    GLU I  13     -146.48     65.24
REMARK 500    PHE I  15       -3.75     86.71
REMARK 500    LYS I  59     -122.24     58.15
REMARK 500    PHE J  12       45.48   -141.11
REMARK 500    GLU J  13     -144.70     64.18
REMARK 500    PHE J  15       -3.17     85.63
REMARK 500    LYS J  59     -120.87     57.17
REMARK 500    SER K  62      -78.27   -137.37
REMARK 500    THR K  75     -165.14   -122.84
REMARK 500    CYS K 172      118.03   -178.82
REMARK 500    ASN K 207      -96.09   -122.13
REMARK 500    MET K 297      -10.92     90.11
REMARK 500    VAL K 331      -54.01     68.31
REMARK 500    ASP K 357       93.99   -162.02
REMARK 500    GLU M  13     -148.31     63.82
REMARK 500    PHE M  15       -3.31     85.35
REMARK 500    LYS M  59     -119.88     58.13
REMARK 500    SER O  62      -79.92   -136.78
REMARK 500    THR O  65     -169.97   -128.56
REMARK 500    THR O  75     -163.62   -121.77
REMARK 500    CYS O 172      119.51   -178.14
REMARK 500    ASN O 207      -96.37   -122.38
REMARK 500    MET O 212      106.40   -162.29
REMARK 500    MET O 297      -13.95     88.98
REMARK 500    VAL O 331      -52.92     71.36
REMARK 500    ASP O 357       90.93   -160.85
REMARK 500    ASN P   8       59.12     39.50
REMARK 500    PHE P  12       50.47   -142.08
REMARK 500    GLU P  13     -145.40     60.87
REMARK 500    PHE P  15       -3.93     85.91
REMARK 500    LYS P  59     -120.01     55.22
REMARK 500    SER R  62      -77.51   -138.56
REMARK 500    THR R  65     -167.27   -127.58
REMARK 500    THR R  75     -163.92   -124.51
REMARK 500    CYS R 172      120.04   -178.27
REMARK 500    ASN R 207      -95.55   -119.32
REMARK 500    MET R 212      111.46   -163.02
REMARK 500    ALA R 296      132.16    -35.03
REMARK 500    MET R 297       -8.71     84.30
REMARK 500    VAL R 331      -53.46     71.91
REMARK 500    GLU T  13     -147.84     62.85
REMARK 500    PHE T  15       -4.96     85.62
REMARK 500    LYS T  59     -122.12     59.05
REMARK 500    SER V  62      -79.16   -140.06
REMARK 500    THR V  75     -163.30   -124.35
REMARK 500    CYS V 172      118.03   -179.09
REMARK 500    ASN V 207      -94.12   -120.78
REMARK 500    MET V 212      109.86   -163.41
REMARK 500    ALA V 296      129.71    -32.30
REMARK 500    MET V 297      -11.18     87.39
REMARK 500    VAL V 331      -54.65     70.76
REMARK 500    ASP V 357       91.74   -161.57
REMARK 500    ASN W   8       56.23     37.44
REMARK 500    PHE W  12       47.11   -142.19
REMARK 500    GLU W  13     -147.30     62.45
REMARK 500    PHE W  15       -1.93     83.53
REMARK 500    LYS W  59     -121.73     58.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    SER T  16        25.0      L          L   OUTSIDE RANGE
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 A 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 201   OQ1
REMARK 620 2 ASP A 203   OD1 131.4
REMARK 620 3 GLU A 204   OE1 106.4  90.8
REMARK 620 4 CAP A 477   O2   77.4 105.7 154.4
REMARK 620 5 CAP A 477   O3   53.4 175.0  86.2  75.8
REMARK 620 6 CAP A 477   O7  134.4  90.1  88.0  72.9  85.8
REMARK 620 7 KCX A 201   OQ2  43.3  90.6  96.9 102.2  93.7 175.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP B 477   O7
REMARK 620 2 CAP B 477   O2   76.0
REMARK 620 3 KCX B 201   OQ2 171.2  98.1
REMARK 620 4 ASP B 203   OD1  96.6 105.3  91.3
REMARK 620 5 GLU B 204   OE1  93.3 161.8  90.6  90.4
REMARK 620 6 CAP B 477   O3   89.2  77.0  83.0 174.2  88.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG E 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP E 477   O2
REMARK 620 2 CAP E 477   O3   74.8
REMARK 620 3 CAP E 477   O7   73.5  81.1
REMARK 620 4 KCX E 201   OQ2  96.3  91.0 168.4
REMARK 620 5 ASP E 203   OD1 104.7 174.7  93.6  94.3
REMARK 620 6 GLU E 204   OE1 155.6  83.2  93.0  94.5  96.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG H 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX H 201   OQ2
REMARK 620 2 ASP H 203   OD1  89.6
REMARK 620 3 CAP H 477   O3   83.7 173.1
REMARK 620 4 GLU H 204   OE1  90.0  91.8  90.0
REMARK 620 5 CAP H 477   O2   95.1 106.5  72.4 161.0
REMARK 620 6 CAP H 477   O7  170.7  97.0  89.4  96.3  76.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG K 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU K 204   OE1
REMARK 620 2 ASP K 203   OD1  98.5
REMARK 620 3 CAP K 477   O2  156.7 103.7
REMARK 620 4 CAP K 477   O3   85.7 172.8  72.9
REMARK 620 5 CAP K 477   O7  104.2  91.2  68.8  93.3
REMARK 620 6 KCX K 201   OQ2  93.1  90.6  93.6  83.4 162.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG O 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX O 201   OQ2
REMARK 620 2 ASP O 203   OD1  91.5
REMARK 620 3 GLU O 204   OE1  93.8  94.0
REMARK 620 4 CAP O 477   O3   84.3 175.7  87.4
REMARK 620 5 CAP O 477   O7  165.7  98.1  95.9  85.8
REMARK 620 6 CAP O 477   O2   96.4 107.8 155.5  71.7  70.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG R 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX R 201   OQ2
REMARK 620 2 GLU R 204   OE1  91.9
REMARK 620 3 ASP R 203   OD1  93.5  93.5
REMARK 620 4 CAP R 477   O2   96.7 155.7 108.5
REMARK 620 5 CAP R 477   O3   84.0  88.5 176.8  70.0
REMARK 620 6 CAP R 477   O7  167.8  94.5  96.5  73.5  85.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG V 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP V 203   OD1
REMARK 620 2 GLU V 204   OE1  90.5
REMARK 620 3 CAP V 477   O2  105.1 161.6
REMARK 620 4 CAP V 477   O7   92.3  92.3  77.6
REMARK 620 5 KCX V 201   OQ2  87.9  91.9  98.4 175.9
REMARK 620 6 CAP V 477   O3  173.4  84.0  81.0  91.4  88.8
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 A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG H 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG K 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG O 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG R 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG V 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1123
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1123
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1123
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP K 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1123
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP O 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1123
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP R 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO T1123
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP V 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1477
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1478
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1479
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1480
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO W1123
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GK8   RELATED DB: PDB
REMARK 900  RUBISCO FROM CHLAMYDOMONAS REINHARDTII
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: 1UW9   RELATED DB: PDB
REMARK 900  L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT
REMARK 900 RELATED ID: 1UWA   RELATED DB: PDB
REMARK 900  L290F MUTANT RUBISCO FROM CHLAMYDOMONAS
REMARK 900 RELATED ID: 1UZD   RELATED DB: PDB
REMARK 900  CHLAMYDOMONAS,SPINACH CHIMERIC RUBISCO
REMARK 900 RELATED ID: 1AA1   RELATED DB: PDB
REMARK 900  ACTIVATED SPINACH RUBISCO IN COMPLEX WITH
REMARK 900  THE PRODUCT 3-PHOSPHOGLYCERATE
REMARK 900 RELATED ID: 1AUS   RELATED DB: PDB
REMARK 900  ACTIVATED UNLIGANDED SPINACH RUBISCO
REMARK 900 RELATED ID: 1IR1   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF SPINACH RIBULOSE-1,5-
REMARK 900  BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO)
REMARK 900  COMPLEXED WITH CO2, MG2+AND 2-
REMARK 900  CARBOXYARABINITOL-1,5-BISPHOSPHATE
REMARK 900 RELATED ID: 1UPM   RELATED DB: PDB
REMARK 900  ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-
REMARK 900  CARBOXYARABINITOL 2 BISPHOSPHAT AND CA2+.
REMARK 900 RELATED ID: 1UPP   RELATED DB: PDB
REMARK 900  SPINACH RUBISCO IN COMPLEX WITH 2-
REMARK 900  CARBOXYARABINITOL 2 BISPHOSPHATE AND CALCIUM.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 LOOP BA-BB OF SMALL SUBUNIT CHLAMYDOMONAS RUBISCO, RESIDUES
REMARK 999 47 - 71 (ADKAYVSNESAIRFGSVSCLYYDNR) HAS BEEN REPLACED WITH
REMARK 999 THE CORRESPONDING LOOP OF SYNECHOCOCCUSS RUBISCO, RESIDUES
REMARK 999 47 - 53 (HSNPEEF). SINCE THIS LOOP IN RUBISCO FROM
REMARK 999 SYNECHOCOCCUSS IS SMALLER, THE NUMBERING OF THE SMALL
REMARK 999 SUBUNIT IN THE COORDINATE FILE HAS BEEN CHANGED IN ORDER TO
REMARK 999 BE CONSEQUTIVE.
DBREF  1UZH A    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UZH B    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UZH E    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UZH H    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UZH K    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UZH O    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UZH R    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UZH V    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UZH I    1    46  UNP    P00873   RBS1_CHLRE      46     91
DBREF  1UZH I   47    53  UNP    P04716   RBS2_SPIOL      47     53
DBREF  1UZH I   54   122  UNP    P00873   RBS1_CHLRE     117    185
DBREF  1UZH C    1    46  UNP    P00873   RBS1_CHLRE      46     91
DBREF  1UZH C   47    53  UNP    P04716   RBS2_SPIOL      46     52
DBREF  1UZH C   54   122  UNP    P00873   RBS1_CHLRE     117    185
DBREF  1UZH F    1    46  UNP    P00873   RBS1_CHLRE      46     91
DBREF  1UZH F   47    53  UNP    P04716   RBS2_SPIOL      47     53
DBREF  1UZH F   54   122  UNP    P00873   RBS1_CHLRE     117    185
DBREF  1UZH J    1    46  UNP    P00873   RBS1_CHLRE      46     91
DBREF  1UZH J   47    53  UNP    P04716   RBS2_SPIOL      47     53
DBREF  1UZH J   54   122  UNP    P00873   RBS1_CHLRE     117    185
DBREF  1UZH P    1    46  UNP    P00873   RBS1_CHLRE      46     91
DBREF  1UZH P   47    53  UNP    P04716   RBS2_SPIOL      47     53
DBREF  1UZH P   54   122  UNP    P00873   RBS1_CHLRE     117    185
DBREF  1UZH T    1    46  UNP    P00873   RBS1_CHLRE      46     91
DBREF  1UZH T   47    53  UNP    P04716   RBS2_SPIOL      47     53
DBREF  1UZH T   54   122  UNP    P00873   RBS1_CHLRE     117    185
DBREF  1UZH M    1    46  UNP    P00873   RBS1_CHLRE      46     91
DBREF  1UZH M   47    53  UNP    P04716   RBS2_SPIOL      47     53
DBREF  1UZH M   54   122  UNP    P00873   RBS1_CHLRE     117    185
DBREF  1UZH W    1    46  UNP    P00873   RBS1_CHLRE      46     91
DBREF  1UZH W   47    53  UNP    P04716   RBS2_SPIOL      47     53
DBREF  1UZH W   54   122  UNP    P00873   RBS1_CHLRE     117    185
SEQADV 1UZH PRO A   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UZH PRO B   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UZH PRO E   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UZH PRO H   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UZH PRO K   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UZH PRO O   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UZH PRO R   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UZH PRO V   46  UNP  P00877    LEU    46 CONFLICT
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 VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 A  475  ARG GLU VAL THR LEU GLY 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 VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 B  475  ARG GLU VAL THR LEU GLY 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  122  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 C  122  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 C  122  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 C  122  PRO CYS LEU GLU PHE ALA GLU HIS SER ASN PRO GLU GLU
SEQRES   5 C  122  PHE TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS
SEQRES   6 C  122  ARG ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS
SEQRES   7 C  122  THR LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA
SEQRES   8 C  122  PHE ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU
SEQRES   9 C  122  VAL GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA
SEQRES  10 C  122  ASN LYS ARG SER VAL
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 VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 E  475  ARG GLU VAL THR LEU GLY 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  122  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 F  122  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 F  122  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 F  122  PRO CYS LEU GLU PHE ALA GLU HIS SER ASN PRO GLU GLU
SEQRES   5 F  122  PHE TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS
SEQRES   6 F  122  ARG ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS
SEQRES   7 F  122  THR LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA
SEQRES   8 F  122  PHE ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU
SEQRES   9 F  122  VAL GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA
SEQRES  10 F  122  ASN LYS ARG SER VAL
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 VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 H  475  ARG GLU VAL THR LEU GLY 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  122  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 I  122  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 I  122  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 I  122  PRO CYS LEU GLU PHE ALA GLU HIS SER ASN PRO GLU GLU
SEQRES   5 I  122  PHE TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS
SEQRES   6 I  122  ARG ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS
SEQRES   7 I  122  THR LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA
SEQRES   8 I  122  PHE ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU
SEQRES   9 I  122  VAL GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA
SEQRES  10 I  122  ASN LYS ARG SER VAL
SEQRES   1 J  122  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 J  122  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 J  122  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 J  122  PRO CYS LEU GLU PHE ALA GLU HIS SER ASN PRO GLU GLU
SEQRES   5 J  122  PHE TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS
SEQRES   6 J  122  ARG ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS
SEQRES   7 J  122  THR LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA
SEQRES   8 J  122  PHE ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU
SEQRES   9 J  122  VAL GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA
SEQRES  10 J  122  ASN LYS ARG SER VAL
SEQRES   1 K  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 K  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 K  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 K  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 K  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 K  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 K  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 K  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 K  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 K  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 K  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 K  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 K  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 K  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 K  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 K  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 K  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 K  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 K  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 K  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 K  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 K  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 K  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 K  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 K  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 K  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 K  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 K  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 K  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 K  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 K  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 K  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 K  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 K  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 K  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 K  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 K  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 M  122  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 M  122  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 M  122  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 M  122  PRO CYS LEU GLU PHE ALA GLU HIS SER ASN PRO GLU GLU
SEQRES   5 M  122  PHE TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS
SEQRES   6 M  122  ARG ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS
SEQRES   7 M  122  THR LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA
SEQRES   8 M  122  PHE ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU
SEQRES   9 M  122  VAL GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA
SEQRES  10 M  122  ASN LYS ARG SER VAL
SEQRES   1 O  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 O  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 O  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 O  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 O  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 O  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 O  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 O  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 O  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 O  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 O  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 O  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 O  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 O  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 O  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 O  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 O  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 O  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 O  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 O  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 O  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 O  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 O  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 O  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 O  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 O  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 O  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 O  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 O  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 O  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 O  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 O  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 O  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 O  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 O  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 O  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 O  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 P  122  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 P  122  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 P  122  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 P  122  PRO CYS LEU GLU PHE ALA GLU HIS SER ASN PRO GLU GLU
SEQRES   5 P  122  PHE TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS
SEQRES   6 P  122  ARG ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS
SEQRES   7 P  122  THR LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA
SEQRES   8 P  122  PHE ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU
SEQRES   9 P  122  VAL GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA
SEQRES  10 P  122  ASN LYS ARG SER VAL
SEQRES   1 R  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 R  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 R  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 R  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 R  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 R  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 R  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 R  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 R  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 R  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 R  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 R  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 R  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 R  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 R  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 R  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 R  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 R  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 R  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 R  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 R  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 R  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 R  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 R  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 R  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 R  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 R  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 R  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 R  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 R  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 R  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 R  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 R  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 R  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 R  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 R  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 R  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 T  122  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 T  122  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 T  122  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 T  122  PRO CYS LEU GLU PHE ALA GLU HIS SER ASN PRO GLU GLU
SEQRES   5 T  122  PHE TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS
SEQRES   6 T  122  ARG ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS
SEQRES   7 T  122  THR LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA
SEQRES   8 T  122  PHE ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU
SEQRES   9 T  122  VAL GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA
SEQRES  10 T  122  ASN LYS ARG SER VAL
SEQRES   1 V  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 V  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 V  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 V  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 V  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 V  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 V  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 V  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 V  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 V  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 V  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 V  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 V  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 V  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 V  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 V  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 V  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 V  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 V  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 V  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 V  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 V  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 V  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 V  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 V  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 V  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 V  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 V  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 V  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 V  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 V  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 V  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 V  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 V  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 V  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 V  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 V  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 W  122  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 W  122  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 W  122  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 W  122  PRO CYS LEU GLU PHE ALA GLU HIS SER ASN PRO GLU GLU
SEQRES   5 W  122  PHE TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS
SEQRES   6 W  122  ARG ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS
SEQRES   7 W  122  THR LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA
SEQRES   8 W  122  PHE ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU
SEQRES   9 W  122  VAL GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA
SEQRES  10 W  122  ASN LYS ARG SER VAL
MODRES 1UZH HYP A  104  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP A  151  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP B  104  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP B  151  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP E  104  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP E  151  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP H  104  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP H  151  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP K  104  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP K  151  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP O  104  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP O  151  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP R  104  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP R  151  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP V  104  PRO  4-HYDROXYPROLINE
MODRES 1UZH HYP V  151  PRO  4-HYDROXYPROLINE
MODRES 1UZH KCX A  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZH KCX B  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZH KCX E  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZH KCX H  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZH KCX K  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZH KCX O  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZH KCX R  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZH KCX V  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UZH SMC A  256  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC A  369  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC B  256  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC B  369  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC E  256  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC E  369  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC H  256  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC H  369  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC K  256  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC K  369  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC O  256  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC O  369  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC R  256  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC R  369  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC V  256  CYS  S- METHYLCYSTEINE
MODRES 1UZH SMC V  369  CYS  S- METHYLCYSTEINE
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    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    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    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    HYP  K 104       8
HET    HYP  K 151       8
HET    KCX  K 201      12
HET    SMC  K 256       7
HET    SMC  K 369       7
HET    HYP  O 104       8
HET    HYP  O 151       8
HET    KCX  O 201      12
HET    SMC  O 256       7
HET    SMC  O 369       7
HET    HYP  R 104       8
HET    HYP  R 151       8
HET    KCX  R 201      12
HET    SMC  R 256       7
HET    SMC  R 369       7
HET    HYP  V 104       8
HET    HYP  V 151       8
HET    KCX  V 201      12
HET    SMC  V 256       7
HET    SMC  V 369       7
HET     MG  A 476       1
HET     MG  B 476       1
HET     MG  E 476       1
HET     MG  H 476       1
HET     MG  K 476       1
HET     MG  O 476       1
HET     MG  R 476       1
HET     MG  V 476       1
HET    CAP  A 477      21
HET    EDO  A1476       4
HET    EDO  A1477       4
HET    EDO  A1478       4
HET    EDO  A1479       4
HET    EDO  A1480       4
HET    CAP  B 477      21
HET    EDO  B1476       4
HET    EDO  B1477       4
HET    EDO  B1478       4
HET    EDO  B1479       4
HET    EDO  B1480       4
HET    EDO  B1481       4
HET    EDO  C1123       4
HET    CAP  E 477      21
HET    EDO  E1476       4
HET    EDO  E1477       4
HET    EDO  E1478       4
HET    EDO  E1479       4
HET    EDO  E1480       4
HET    EDO  F1123       4
HET    CAP  H 477      21
HET    EDO  H1476       4
HET    EDO  H1477       4
HET    EDO  H1478       4
HET    EDO  H1479       4
HET    EDO  H1480       4
HET    EDO  H1481       4
HET    EDO  J1123       4
HET    CAP  K 477      21
HET    EDO  K1476       4
HET    EDO  K1477       4
HET    EDO  K1478       4
HET    EDO  K1479       4
HET    EDO  K1480       4
HET    EDO  M1123       4
HET    CAP  O 477      21
HET    EDO  O1476       4
HET    EDO  O1477       4
HET    EDO  O1478       4
HET    EDO  O1479       4
HET    EDO  O1480       4
HET    EDO  P1123       4
HET    CAP  R 477      21
HET    EDO  R1476       4
HET    EDO  R1477       4
HET    EDO  R1478       4
HET    EDO  R1479       4
HET    EDO  R1480       4
HET    EDO  T1123       4
HET    CAP  V 477      21
HET    EDO  V1476       4
HET    EDO  V1477       4
HET    EDO  V1478       4
HET    EDO  V1479       4
HET    EDO  V1480       4
HET    EDO  V1481       4
HET    EDO  W1123       4
HETNAM     HYP 4-HYDROXYPROLINE
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM     SMC S-METHYLCYSTEINE
HETNAM      MG MAGNESIUM ION
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   1  HYP    16(C5 H9 N O3)
FORMUL   1  KCX    8(C7 H14 N2 O4)
FORMUL   1  SMC    16(C4 H9 N O2 S)
FORMUL  17   MG    8(MG 2+)
FORMUL  25  CAP    8(C6 H14 O13 P2)
FORMUL  26  EDO    50(C2 H6 O2)
FORMUL  83  HOH   *2831(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  GLY A  261  1                                  16
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  GLY B  261  1                                  16
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 THR C   22  GLY C   37  1                                  16
HELIX   46  46 ASP C   67  PHE C   82  1                                  16
HELIX   47  47 PRO C  116  ARG C  120  5                                   5
HELIX   48  48 TYR E   20  TYR E   25  1                                   6
HELIX   49  49 PRO E   49  SER E   61  1                                  13
HELIX   50  50 VAL E   69  THR E   75  5                                   7
HELIX   51  51 SER E   76  LYS E   81  1                                   6
HELIX   52  52 HYP E  104  PHE E  108  5                                   5
HELIX   53  53 SER E  112  GLY E  122  1                                  11
HELIX   54  54 ASN E  123  GLY E  126  5                                   4
HELIX   55  55 PRO E  141  LYS E  146  1                                   6
HELIX   56  56 GLY E  154  ASN E  163  1                                  10
HELIX   57  57 SER E  181  ARG E  194  1                                  14
HELIX   58  58 ARG E  213  GLY E  233  1                                  21
HELIX   59  59 THR E  246  LEU E  260  1                                  15
HELIX   60  60 TYR E  269  GLY E  288  1                                  20
HELIX   61  61 MET E  297  ARG E  303  1                                   7
HELIX   62  62 HIS E  310  GLY E  322  1                                  13
HELIX   63  63 GLU E  338  ASP E  351  1                                  14
HELIX   64  64 ARG E  358  GLY E  361  5                                   4
HELIX   65  65 HIS E  383  TRP E  385  5                                   3
HELIX   66  66 HIS E  386  GLY E  395  1                                  10
HELIX   67  67 GLY E  403  GLY E  408  1                                   6
HELIX   68  68 GLY E  412  GLU E  433  1                                  22
HELIX   69  69 ASP E  436  LYS E  463  1                                  28
HELIX   70  70 THR F   22  GLY F   37  1                                  16
HELIX   71  71 ASP F   67  PHE F   82  1                                  16
HELIX   72  72 PRO F  116  ARG F  120  5                                   5
HELIX   73  73 TYR H   20  TYR H   25  1                                   6
HELIX   74  74 PRO H   49  SER H   61  1                                  13
HELIX   75  75 VAL H   69  THR H   75  5                                   7
HELIX   76  76 SER H   76  LYS H   81  1                                   6
HELIX   77  77 HYP H  104  PHE H  108  5                                   5
HELIX   78  78 SER H  112  GLY H  122  1                                  11
HELIX   79  79 ASN H  123  GLY H  126  5                                   4
HELIX   80  80 PRO H  141  LYS H  146  1                                   6
HELIX   81  81 GLY H  154  ASN H  163  1                                  10
HELIX   82  82 SER H  181  GLY H  195  1                                  15
HELIX   83  83 ARG H  213  GLY H  233  1                                  21
HELIX   84  84 THR H  246  GLY H  261  1                                  16
HELIX   85  85 TYR H  269  GLY H  288  1                                  20
HELIX   86  86 MET H  297  ARG H  303  1                                   7
HELIX   87  87 HIS H  310  GLY H  322  1                                  13
HELIX   88  88 GLU H  338  ASP H  351  1                                  14
HELIX   89  89 ARG H  358  GLY H  361  5                                   4
HELIX   90  90 HIS H  383  TRP H  385  5                                   3
HELIX   91  91 HIS H  386  GLY H  395  1                                  10
HELIX   92  92 GLY H  403  GLY H  408  1                                   6
HELIX   93  93 GLY H  412  GLU H  433  1                                  22
HELIX   94  94 ASP H  436  LYS H  463  1                                  28
HELIX   95  95 THR I   22  ASN I   36  1                                  15
HELIX   96  96 ASP I   67  PHE I   82  1                                  16
HELIX   97  97 PRO I  116  ARG I  120  5                                   5
HELIX   98  98 THR J   22  ASN J   36  1                                  15
HELIX   99  99 ASP J   67  PHE J   82  1                                  16
HELIX  100 100 PRO J  116  ARG J  120  5                                   5
HELIX  101 101 TYR K   20  TYR K   25  1                                   6
HELIX  102 102 PRO K   49  SER K   61  1                                  13
HELIX  103 103 VAL K   69  THR K   75  5                                   7
HELIX  104 104 SER K   76  LYS K   81  1                                   6
HELIX  105 105 HYP K  104  PHE K  108  5                                   5
HELIX  106 106 SER K  112  GLY K  122  1                                  11
HELIX  107 107 ASN K  123  GLY K  126  5                                   4
HELIX  108 108 PRO K  141  LYS K  146  1                                   6
HELIX  109 109 GLY K  154  ASN K  163  1                                  10
HELIX  110 110 SER K  181  GLY K  195  1                                  15
HELIX  111 111 ARG K  213  GLY K  233  1                                  21
HELIX  112 112 THR K  246  GLY K  261  1                                  16
HELIX  113 113 TYR K  269  GLY K  288  1                                  20
HELIX  114 114 MET K  297  ARG K  303  1                                   7
HELIX  115 115 HIS K  310  GLY K  322  1                                  13
HELIX  116 116 GLU K  338  ASP K  351  1                                  14
HELIX  117 117 ARG K  358  GLY K  361  5                                   4
HELIX  118 118 HIS K  383  TRP K  385  5                                   3
HELIX  119 119 HIS K  386  GLY K  395  1                                  10
HELIX  120 120 GLY K  403  GLY K  408  1                                   6
HELIX  121 121 GLY K  412  GLU K  433  1                                  22
HELIX  122 122 ASP K  436  LYS K  463  1                                  28
HELIX  123 123 THR M   22  GLY M   37  1                                  16
HELIX  124 124 ASP M   67  PHE M   82  1                                  16
HELIX  125 125 PRO M  116  ARG M  120  5                                   5
HELIX  126 126 TYR O   20  TYR O   25  1                                   6
HELIX  127 127 PRO O   49  SER O   61  1                                  13
HELIX  128 128 VAL O   69  THR O   75  5                                   7
HELIX  129 129 SER O   76  LYS O   81  1                                   6
HELIX  130 130 HYP O  104  PHE O  108  5                                   5
HELIX  131 131 SER O  112  GLY O  122  1                                  11
HELIX  132 132 ASN O  123  GLY O  126  5                                   4
HELIX  133 133 PRO O  141  LYS O  146  1                                   6
HELIX  134 134 GLY O  154  ASN O  163  1                                  10
HELIX  135 135 SER O  181  GLY O  195  1                                  15
HELIX  136 136 ARG O  213  GLY O  233  1                                  21
HELIX  137 137 THR O  246  GLY O  261  1                                  16
HELIX  138 138 TYR O  269  GLY O  288  1                                  20
HELIX  139 139 MET O  297  ARG O  303  1                                   7
HELIX  140 140 HIS O  310  GLY O  322  1                                  13
HELIX  141 141 GLU O  338  ASP O  351  1                                  14
HELIX  142 142 ARG O  358  GLY O  361  5                                   4
HELIX  143 143 HIS O  383  TRP O  385  5                                   3
HELIX  144 144 HIS O  386  GLY O  395  1                                  10
HELIX  145 145 GLY O  403  GLY O  408  1                                   6
HELIX  146 146 GLY O  412  GLU O  433  1                                  22
HELIX  147 147 ASP O  436  LYS O  463  1                                  28
HELIX  148 148 THR P   22  ASN P   36  1                                  15
HELIX  149 149 ASP P   67  PHE P   82  1                                  16
HELIX  150 150 PRO P  116  ARG P  120  5                                   5
HELIX  151 151 TYR R   20  TYR R   25  1                                   6
HELIX  152 152 PRO R   49  SER R   61  1                                  13
HELIX  153 153 VAL R   69  THR R   75  5                                   7
HELIX  154 154 SER R   76  LYS R   81  1                                   6
HELIX  155 155 HYP R  104  PHE R  108  5                                   5
HELIX  156 156 SER R  112  GLY R  122  1                                  11
HELIX  157 157 ASN R  123  GLY R  126  5                                   4
HELIX  158 158 PRO R  141  LYS R  146  1                                   6
HELIX  159 159 GLY R  154  ASN R  163  1                                  10
HELIX  160 160 SER R  181  GLY R  195  1                                  15
HELIX  161 161 ARG R  213  GLY R  233  1                                  21
HELIX  162 162 THR R  246  GLY R  261  1                                  16
HELIX  163 163 TYR R  269  GLY R  288  1                                  20
HELIX  164 164 MET R  297  ARG R  303  1                                   7
HELIX  165 165 HIS R  310  GLY R  322  1                                  13
HELIX  166 166 GLU R  338  ASP R  351  1                                  14
HELIX  167 167 ARG R  358  GLY R  361  5                                   4
HELIX  168 168 HIS R  383  TRP R  385  5                                   3
HELIX  169 169 HIS R  386  GLY R  395  1                                  10
HELIX  170 170 GLY R  403  GLY R  408  1                                   6
HELIX  171 171 GLY R  412  GLU R  433  1                                  22
HELIX  172 172 ASP R  436  LYS R  463  1                                  28
HELIX  173 173 THR T   22  ASN T   36  1                                  15
HELIX  174 174 ASP T   67  PHE T   82  1                                  16
HELIX  175 175 PRO T  116  ARG T  120  5                                   5
HELIX  176 176 TYR V   20  TYR V   25  1                                   6
HELIX  177 177 PRO V   49  SER V   61  1                                  13
HELIX  178 178 VAL V   69  THR V   75  5                                   7
HELIX  179 179 SER V   76  LYS V   81  1                                   6
HELIX  180 180 HYP V  104  PHE V  108  5                                   5
HELIX  181 181 SER V  112  GLY V  122  1                                  11
HELIX  182 182 ASN V  123  GLY V  126  5                                   4
HELIX  183 183 PRO V  141  LYS V  146  1                                   6
HELIX  184 184 GLY V  154  ASN V  163  1                                  10
HELIX  185 185 SER V  181  ARG V  194  1                                  14
HELIX  186 186 ARG V  213  GLY V  233  1                                  21
HELIX  187 187 THR V  246  GLY V  261  1                                  16
HELIX  188 188 TYR V  269  GLY V  288  1                                  20
HELIX  189 189 MET V  297  ARG V  303  1                                   7
HELIX  190 190 HIS V  310  GLY V  322  1                                  13
HELIX  191 191 GLU V  338  ASP V  351  1                                  14
HELIX  192 192 ARG V  358  GLY V  361  5                                   4
HELIX  193 193 HIS V  383  TRP V  385  5                                   3
HELIX  194 194 HIS V  386  GLY V  395  1                                  10
HELIX  195 195 GLY V  403  GLY V  408  1                                   6
HELIX  196 196 GLY V  412  GLU V  433  1                                  22
HELIX  197 197 ASP V  436  LYS V  463  1                                  28
HELIX  198 198 THR W   22  GLY W   37  1                                  16
HELIX  199 199 ASP W   67  PHE W   82  1                                  16
HELIX  200 200 PRO W  116  ARG W  120  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 4 THR C  56  TRP C  58  0
SHEET    2  CA 4 ILE C  39  ALA C  45 -1  O  LEU C  42   N  TRP C  58
SHEET    3  CA 4 TYR C  86  ASP C  93 -1  O  TYR C  86   N  ALA C  45
SHEET    4  CA 4 VAL C  98  GLN C 106 -1  O  VAL C  98   N  ASP C  93
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 4 THR F  56  TRP F  58  0
SHEET    2  FA 4 ILE F  39  ALA F  45 -1  O  LEU F  42   N  TRP F  58
SHEET    3  FA 4 TYR F  86  ASP F  93 -1  O  TYR F  86   N  ALA F  45
SHEET    4  FA 4 VAL F  98  GLN F 106 -1  O  VAL F  98   N  ASP F  93
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  56  TRP I  58  0
SHEET    2  IA 4 ILE I  39  ALA I  45 -1  O  LEU I  42   N  TRP I  58
SHEET    3  IA 4 TYR I  86  ASP I  93 -1  O  TYR I  86   N  ALA I  45
SHEET    4  IA 4 VAL I  98  GLN I 106 -1  O  VAL I  98   N  ASP I  93
SHEET    1  JA 4 THR J  56  TRP J  58  0
SHEET    2  JA 4 ILE J  39  ALA J  45 -1  O  LEU J  42   N  TRP J  58
SHEET    3  JA 4 TYR J  86  ASP J  93 -1  O  TYR J  86   N  ALA J  45
SHEET    4  JA 4 VAL J  98  GLN J 106 -1  O  VAL J  98   N  ASP J  93
SHEET    1  KA 5 ARG K  83  PRO K  89  0
SHEET    2  KA 5 TYR K  97  TYR K 103 -1  O  ILE K  98   N  GLU K  88
SHEET    3  KA 5 ILE K  36  PRO K  44 -1  O  ILE K  36   N  TYR K 103
SHEET    4  KA 5 LEU K 130  ARG K 139 -1  N  ARG K 131   O  THR K  43
SHEET    5  KA 5 GLY K 308  ILE K 309  1  O  GLY K 308   N  LEU K 135
SHEET    1  KB 8 LEU K 169  GLY K 171  0
SHEET    2  KB 8 CYS K 399  GLN K 401  1  O  LEU K 400   N  GLY K 171
SHEET    3  KB 8 MET K 375  SER K 379  1  O  PRO K 376   N  CYS K 399
SHEET    4  KB 8 HIS K 325  HIS K 327  1  O  LEU K 326   N  VAL K 377
SHEET    5  KB 8 LEU K 290  HIS K 294  1  O  ILE K 293   N  HIS K 327
SHEET    6  KB 8 ILE K 264  ASP K 268  1  O  ILE K 265   N  HIS K 292
SHEET    7  KB 8 GLY K 237  ASN K 241  1  O  LEU K 240   N  MET K 266
SHEET    8  KB 8 PHE K 199  KCX K 201  1  O  THR K 200   N  TYR K 239
SHEET    1  KC 2 TYR K 353  VAL K 354  0
SHEET    2  KC 2 GLN K 366  ASP K 367 -1  O  GLN K 366   N  VAL K 354
SHEET    1  MA 4 THR M  56  TRP M  58  0
SHEET    2  MA 4 ILE M  39  ALA M  45 -1  O  LEU M  42   N  TRP M  58
SHEET    3  MA 4 TYR M  86  ASP M  93 -1  O  TYR M  86   N  ALA M  45
SHEET    4  MA 4 VAL M  98  GLN M 106 -1  O  VAL M  98   N  ASP M  93
SHEET    1  OA 5 ARG O  83  PRO O  89  0
SHEET    2  OA 5 TYR O  97  TYR O 103 -1  O  ILE O  98   N  GLU O  88
SHEET    3  OA 5 ILE O  36  PRO O  44 -1  O  ILE O  36   N  TYR O 103
SHEET    4  OA 5 LEU O 130  ARG O 139 -1  N  ARG O 131   O  THR O  43
SHEET    5  OA 5 GLY O 308  ILE O 309  1  O  GLY O 308   N  LEU O 135
SHEET    1  OB 8 LEU O 169  GLY O 171  0
SHEET    2  OB 8 CYS O 399  GLN O 401  1  O  LEU O 400   N  GLY O 171
SHEET    3  OB 8 MET O 375  SER O 379  1  O  PRO O 376   N  CYS O 399
SHEET    4  OB 8 HIS O 325  HIS O 327  1  O  LEU O 326   N  VAL O 377
SHEET    5  OB 8 LEU O 290  HIS O 294  1  O  ILE O 293   N  HIS O 327
SHEET    6  OB 8 ILE O 264  ASP O 268  1  O  ILE O 265   N  HIS O 292
SHEET    7  OB 8 GLY O 237  ASN O 241  1  O  LEU O 240   N  MET O 266
SHEET    8  OB 8 PHE O 199  KCX O 201  1  O  THR O 200   N  TYR O 239
SHEET    1  OC 2 TYR O 353  VAL O 354  0
SHEET    2  OC 2 GLN O 366  ASP O 367 -1  O  GLN O 366   N  VAL O 354
SHEET    1  PA 4 THR P  56  TRP P  58  0
SHEET    2  PA 4 ILE P  39  ALA P  45 -1  O  LEU P  42   N  TRP P  58
SHEET    3  PA 4 TYR P  86  ASP P  93 -1  O  TYR P  86   N  ALA P  45
SHEET    4  PA 4 VAL P  98  GLN P 106 -1  O  VAL P  98   N  ASP P  93
SHEET    1  RA 5 ARG R  83  PRO R  89  0
SHEET    2  RA 5 TYR R  97  TYR R 103 -1  O  ILE R  98   N  GLU R  88
SHEET    3  RA 5 ILE R  36  PRO R  44 -1  O  ILE R  36   N  TYR R 103
SHEET    4  RA 5 LEU R 130  ARG R 139 -1  N  ARG R 131   O  THR R  43
SHEET    5  RA 5 GLY R 308  ILE R 309  1  O  GLY R 308   N  LEU R 135
SHEET    1  RB 8 LEU R 169  GLY R 171  0
SHEET    2  RB 8 CYS R 399  GLN R 401  1  O  LEU R 400   N  GLY R 171
SHEET    3  RB 8 MET R 375  SER R 379  1  O  PRO R 376   N  CYS R 399
SHEET    4  RB 8 HIS R 325  HIS R 327  1  O  LEU R 326   N  VAL R 377
SHEET    5  RB 8 LEU R 290  HIS R 294  1  O  ILE R 293   N  HIS R 327
SHEET    6  RB 8 ILE R 264  ASP R 268  1  O  ILE R 265   N  HIS R 292
SHEET    7  RB 8 GLY R 237  ASN R 241  1  O  LEU R 240   N  MET R 266
SHEET    8  RB 8 PHE R 199  KCX R 201  1  O  THR R 200   N  TYR R 239
SHEET    1  RC 2 TYR R 353  VAL R 354  0
SHEET    2  RC 2 GLN R 366  ASP R 367 -1  O  GLN R 366   N  VAL R 354
SHEET    1  TA 4 THR T  56  TRP T  58  0
SHEET    2  TA 4 ILE T  39  ALA T  45 -1  O  LEU T  42   N  TRP T  58
SHEET    3  TA 4 TYR T  86  ASP T  93 -1  O  TYR T  86   N  ALA T  45
SHEET    4  TA 4 VAL T  98  GLN T 106 -1  O  VAL T  98   N  ASP T  93
SHEET    1  VA 5 ARG V  83  PRO V  89  0
SHEET    2  VA 5 TYR V  97  TYR V 103 -1  O  ILE V  98   N  GLU V  88
SHEET    3  VA 5 ILE V  36  PRO V  44 -1  O  ILE V  36   N  TYR V 103
SHEET    4  VA 5 LEU V 130  ARG V 139 -1  N  ARG V 131   O  THR V  43
SHEET    5  VA 5 GLY V 308  ILE V 309  1  O  GLY V 308   N  LEU V 135
SHEET    1  VB 8 LEU V 169  GLY V 171  0
SHEET    2  VB 8 CYS V 399  GLN V 401  1  O  LEU V 400   N  GLY V 171
SHEET    3  VB 8 MET V 375  SER V 379  1  O  PRO V 376   N  CYS V 399
SHEET    4  VB 8 HIS V 325  HIS V 327  1  O  LEU V 326   N  VAL V 377
SHEET    5  VB 8 LEU V 290  HIS V 294  1  O  ILE V 293   N  HIS V 327
SHEET    6  VB 8 ILE V 264  ASP V 268  1  O  ILE V 265   N  HIS V 292
SHEET    7  VB 8 GLY V 237  ASN V 241  1  O  LEU V 240   N  MET V 266
SHEET    8  VB 8 PHE V 199  KCX V 201  1  O  THR V 200   N  TYR V 239
SHEET    1  VC 2 TYR V 353  VAL V 354  0
SHEET    2  VC 2 GLN V 366  ASP V 367 -1  O  GLN V 366   N  VAL V 354
SHEET    1  WA 4 THR W  56  TRP W  58  0
SHEET    2  WA 4 ILE W  39  ALA W  45 -1  O  LEU W  42   N  TRP W  58
SHEET    3  WA 4 TYR W  86  ASP W  93 -1  O  TYR W  86   N  ALA W  45
SHEET    4  WA 4 VAL W  98  GLN W 106 -1  O  VAL W  98   N  ASP W  93
SSBOND   1 CYS A  247    CYS B  247                          1555   1555  2.06
SSBOND   2 CYS A  449    CYS A  459                          1555   1555  2.04
SSBOND   3 CYS B  449    CYS B  459                          1555   1555  2.05
SSBOND   4 CYS E  247    CYS K  247                          1555   1555  2.06
SSBOND   5 CYS E  449    CYS E  459                          1555   1555  2.03
SSBOND   6 CYS H  247    CYS R  247                          1555   1555  2.06
SSBOND   7 CYS H  449    CYS H  459                          1555   1555  2.05
SSBOND   8 CYS K  449    CYS K  459                          1555   1555  2.05
SSBOND   9 CYS O  247    CYS V  247                          1555   1555  2.06
SSBOND  10 CYS O  449    CYS O  459                          1555   1555  2.05
SSBOND  11 CYS R  449    CYS R  459                          1555   1555  2.05
SSBOND  12 CYS V  449    CYS V  459                          1555   1555  2.04
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.33
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.33
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.34
LINK         C   HYP A 151                 N   PRO A 152     1555   1555  1.33
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.32
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.33
LINK         OQ2 KCX A 201                MG    MG A 476     1555   1555  1.96
LINK         C   VAL A 255                 N   SMC A 256     1555   1555  1.34
LINK         C   SMC A 256                 N   ALA A 257     1555   1555  1.33
LINK         C   TRP A 368                 N   SMC A 369     1555   1555  1.34
LINK         C   SMC A 369                 N   SER A 370     1555   1555  1.33
LINK        MG    MG A 476                 OQ1 KCX A 201     1555   1555  3.11
LINK        MG    MG A 476                 OD1 ASP A 203     1555   1555  2.04
LINK        MG    MG A 476                 OE1 GLU A 204     1555   1555  2.11
LINK        MG    MG A 476                 O2  CAP A 477     1555   1555  2.31
LINK        MG    MG A 476                 O3  CAP A 477     1555   1555  2.09
LINK        MG    MG A 476                 O7  CAP A 477     1555   1555  2.28
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  1.32
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.32
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.33
LINK         C   VAL B 255                 N   SMC B 256     1555   1555  1.32
LINK         C   SMC B 256                 N   ALA B 257     1555   1555  1.34
LINK         C   TRP B 368                 N   SMC B 369     1555   1555  1.35
LINK         C   SMC B 369                 N   SER B 370     1555   1555  1.34
LINK        MG    MG B 476                 O7  CAP B 477     1555   1555  2.13
LINK        MG    MG B 476                 O2  CAP B 477     1555   1555  2.20
LINK        MG    MG B 476                 OQ2 KCX B 201     1555   1555  2.05
LINK        MG    MG B 476                 OD1 ASP B 203     1555   1555  2.07
LINK        MG    MG B 476                 OE1 GLU B 204     1555   1555  2.07
LINK        MG    MG B 476                 O3  CAP B 477     1555   1555  2.14
LINK         C   TYR E 103                 N   HYP E 104     1555   1555  1.33
LINK         C   HYP E 104                 N   ILE E 105     1555   1555  1.33
LINK         C   GLY E 150                 N   HYP E 151     1555   1555  1.33
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         OQ2 KCX E 201                MG    MG E 476     1555   1555  2.03
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  1.33
LINK         C   TRP E 368                 N   SMC E 369     1555   1555  1.34
LINK         C   SMC E 369                 N   SER E 370     1555   1555  1.34
LINK        MG    MG E 476                 O7  CAP E 477     1555   1555  2.04
LINK        MG    MG E 476                 OD1 ASP E 203     1555   1555  1.96
LINK        MG    MG E 476                 OE1 GLU E 204     1555   1555  2.03
LINK        MG    MG E 476                 O3  CAP E 477     1555   1555  2.17
LINK        MG    MG E 476                 O2  CAP E 477     1555   1555  2.39
LINK         C   TYR H 103                 N   HYP H 104     1555   1555  1.33
LINK         C   HYP H 104                 N   ILE H 105     1555   1555  1.33
LINK         C   GLY H 150                 N   HYP H 151     1555   1555  1.33
LINK         C   HYP H 151                 N   PRO H 152     1555   1555  1.33
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.34
LINK         C   KCX H 201                 N   ASP H 202     1555   1555  1.34
LINK         C   VAL H 255                 N   SMC H 256     1555   1555  1.33
LINK         C   SMC H 256                 N   ALA H 257     1555   1555  1.34
LINK         C   TRP H 368                 N   SMC H 369     1555   1555  1.34
LINK         C   SMC H 369                 N   SER H 370     1555   1555  1.35
LINK        MG    MG H 476                 OQ2 KCX H 201     1555   1555  2.07
LINK        MG    MG H 476                 OD1 ASP H 203     1555   1555  2.02
LINK        MG    MG H 476                 OE1 GLU H 204     1555   1555  2.09
LINK        MG    MG H 476                 O2  CAP H 477     1555   1555  2.39
LINK        MG    MG H 476                 O7  CAP H 477     1555   1555  2.00
LINK        MG    MG H 476                 O3  CAP H 477     1555   1555  2.20
LINK         C   TYR K 103                 N   HYP K 104     1555   1555  1.33
LINK         C   HYP K 104                 N   ILE K 105     1555   1555  1.33
LINK         C   GLY K 150                 N   HYP K 151     1555   1555  1.33
LINK         C   HYP K 151                 N   PRO K 152     1555   1555  1.32
LINK         C   THR K 200                 N   KCX K 201     1555   1555  1.34
LINK         C   KCX K 201                 N   ASP K 202     1555   1555  1.33
LINK         C   VAL K 255                 N   SMC K 256     1555   1555  1.33
LINK         C   SMC K 256                 N   ALA K 257     1555   1555  1.33
LINK         C   TRP K 368                 N   SMC K 369     1555   1555  1.34
LINK         C   SMC K 369                 N   SER K 370     1555   1555  1.34
LINK        MG    MG K 476                 O7  CAP K 477     1555   1555  2.15
LINK        MG    MG K 476                 O3  CAP K 477     1555   1555  2.18
LINK        MG    MG K 476                 O2  CAP K 477     1555   1555  2.36
LINK        MG    MG K 476                 OD1 ASP K 203     1555   1555  1.99
LINK        MG    MG K 476                 OE1 GLU K 204     1555   1555  2.04
LINK        MG    MG K 476                 OQ2 KCX K 201     1555   1555  2.07
LINK         C   TYR O 103                 N   HYP O 104     1555   1555  1.32
LINK         C   HYP O 104                 N   ILE O 105     1555   1555  1.33
LINK         C   GLY O 150                 N   HYP O 151     1555   1555  1.33
LINK         C   HYP O 151                 N   PRO O 152     1555   1555  1.33
LINK         C   THR O 200                 N   KCX O 201     1555   1555  1.33
LINK         C   KCX O 201                 N   ASP O 202     1555   1555  1.33
LINK         C   VAL O 255                 N   SMC O 256     1555   1555  1.33
LINK         C   SMC O 256                 N   ALA O 257     1555   1555  1.34
LINK         C   TRP O 368                 N   SMC O 369     1555   1555  1.34
LINK         C   SMC O 369                 N   SER O 370     1555   1555  1.33
LINK        MG    MG O 476                 OE1 GLU O 204     1555   1555  2.04
LINK        MG    MG O 476                 O2  CAP O 477     1555   1555  2.33
LINK        MG    MG O 476                 O7  CAP O 477     1555   1555  2.16
LINK        MG    MG O 476                 O3  CAP O 477     1555   1555  2.20
LINK        MG    MG O 476                 OQ2 KCX O 201     1555   1555  2.06
LINK        MG    MG O 476                 OD1 ASP O 203     1555   1555  1.94
LINK         C   TYR R 103                 N   HYP R 104     1555   1555  1.33
LINK         C   HYP R 104                 N   ILE R 105     1555   1555  1.33
LINK         C   GLY R 150                 N   HYP R 151     1555   1555  1.34
LINK         C   HYP R 151                 N   PRO R 152     1555   1555  1.34
LINK         C   THR R 200                 N   KCX R 201     1555   1555  1.33
LINK         OQ2 KCX R 201                MG    MG R 476     1555   1555  2.04
LINK         C   KCX R 201                 N   ASP R 202     1555   1555  1.33
LINK         C   VAL R 255                 N   SMC R 256     1555   1555  1.34
LINK         C   SMC R 256                 N   ALA R 257     1555   1555  1.33
LINK         C   TRP R 368                 N   SMC R 369     1555   1555  1.34
LINK         C   SMC R 369                 N   SER R 370     1555   1555  1.33
LINK        MG    MG R 476                 O7  CAP R 477     1555   1555  2.30
LINK        MG    MG R 476                 O3  CAP R 477     1555   1555  2.26
LINK        MG    MG R 476                 OD1 ASP R 203     1555   1555  1.96
LINK        MG    MG R 476                 O2  CAP R 477     1555   1555  2.32
LINK        MG    MG R 476                 OE1 GLU R 204     1555   1555  2.05
LINK         C   TYR V 103                 N   HYP V 104     1555   1555  1.33
LINK         C   HYP V 104                 N   ILE V 105     1555   1555  1.33
LINK         C   GLY V 150                 N   HYP V 151     1555   1555  1.33
LINK         C   HYP V 151                 N   PRO V 152     1555   1555  1.34
LINK         C   THR V 200                 N   KCX V 201     1555   1555  1.33
LINK         OQ2 KCX V 201                MG    MG V 476     1555   1555  1.98
LINK         C   KCX V 201                 N   ASP V 202     1555   1555  1.34
LINK         C   VAL V 255                 N   SMC V 256     1555   1555  1.35
LINK         C   SMC V 256                 N   ALA V 257     1555   1555  1.34
LINK         C   TRP V 368                 N   SMC V 369     1555   1555  1.34
LINK         C   SMC V 369                 N   SER V 370     1555   1555  1.34
LINK        MG    MG V 476                 O7  CAP V 477     1555   1555  2.13
LINK        MG    MG V 476                 O3  CAP V 477     1555   1555  2.06
LINK        MG    MG V 476                 O2  CAP V 477     1555   1555  2.12
LINK        MG    MG V 476                 OE1 GLU V 204     1555   1555  2.14
LINK        MG    MG V 476                 OD1 ASP V 203     1555   1555  2.04
CISPEP   1 LYS A  175    PRO A  176          0        -1.34
CISPEP   2 LYS B  175    PRO B  176          0        -3.73
CISPEP   3 LYS E  175    PRO E  176          0        -1.35
CISPEP   4 LYS H  175    PRO H  176          0        -5.17
CISPEP   5 LYS K  175    PRO K  176          0        -2.45
CISPEP   6 LYS O  175    PRO O  176          0        -2.30
CISPEP   7 LYS R  175    PRO R  176          0        -1.46
CISPEP   8 LYS V  175    PRO V  176          0        -2.50
SITE     1 AC1  4 KCX A 201  ASP A 203  GLU A 204  CAP A 477
SITE     1 AC2  5 LYS B 177  KCX B 201  ASP B 203  GLU B 204
SITE     2 AC2  5 CAP B 477
SITE     1 AC3  4 KCX E 201  ASP E 203  GLU E 204  CAP E 477
SITE     1 AC4  5 LYS H 177  KCX H 201  ASP H 203  GLU H 204
SITE     2 AC4  5 CAP H 477
SITE     1 AC5  4 KCX K 201  ASP K 203  GLU K 204  CAP K 477
SITE     1 AC6  4 KCX O 201  ASP O 203  GLU O 204  CAP O 477
SITE     1 AC7  5 LYS R 177  KCX R 201  ASP R 203  GLU R 204
SITE     2 AC7  5 CAP R 477
SITE     1 AC8  4 KCX V 201  ASP V 203  GLU V 204  CAP V 477
SITE     1 AC9 29 THR A 173  LYS A 175  LYS A 177  KCX A 201
SITE     2 AC9 29 ASP A 203  GLU A 204  HIS A 294  ARG A 295
SITE     3 AC9 29 HIS A 327  LYS A 334  LEU A 335  SER A 379
SITE     4 AC9 29 GLY A 380  GLY A 381  GLY A 403  GLY A 404
SITE     5 AC9 29  MG A 476  HOH A2119  HOH A2121  HOH A2188
SITE     6 AC9 29 HOH A2285  HOH A2286  HOH A2287  HOH A2288
SITE     7 AC9 29 GLU B  60  THR B  65  TRP B  66  ASN B 123
SITE     8 AC9 29 HOH B2096
SITE     1 BC1  8 TYR A  24  GLY A  64  THR A  68  VAL A  69
SITE     2 BC1  8 ASP A  72  HOH A2045  HOH A2289  HOH A2290
SITE     1 BC2  7 LYS A  18  THR A  65  TRP A  66  THR A  67
SITE     2 BC2  7 THR A  68  HOH A2290  HOH A2291
SITE     1 BC3  2 GLU A  52  HOH B2315
SITE     1 BC4  4 LYS A 466  GLU A 468  PHE A 469  HOH B2313
SITE     1 BC5  5 ARG A 295  ASP A 473  HOH A2292  HOH A2293
SITE     2 BC5  5 HOH A2294
SITE     1 BC6 30 GLU A  60  THR A  65  TRP A  66  ASN A 123
SITE     2 BC6 30 HOH A2043  THR B 173  LYS B 175  LYS B 177
SITE     3 BC6 30 KCX B 201  ASP B 203  GLU B 204  HIS B 294
SITE     4 BC6 30 ARG B 295  HIS B 327  LYS B 334  LEU B 335
SITE     5 BC6 30 SER B 379  GLY B 380  GLY B 381  GLY B 403
SITE     6 BC6 30 GLY B 404   MG B 476  HOH B2129  HOH B2189
SITE     7 BC6 30 HOH B2243  HOH B2244  HOH B2305  HOH B2306
SITE     8 BC6 30 HOH B2307  HOH B2308
SITE     1 BC7  4 LEU A 270  LEU B 270  HOH B2180  HOH B2309
SITE     1 BC8  9 TYR B  24  GLY B  64  THR B  68  VAL B  69
SITE     2 BC8  9 ASP B  72  EDO B1478  HOH B2052  HOH B2310
SITE     3 BC8  9 HOH B2311
SITE     1 BC9  8 LYS B  18  THR B  65  TRP B  66  THR B  67
SITE     2 BC9  8 THR B  68  EDO B1477  HOH B2310  HOH B2312
SITE     1 CC1  2 GLU B  52  HOH B2313
SITE     1 CC2  5 LYS B 466  PHE B 467  GLU B 468  PHE B 469
SITE     2 CC2  5 HOH B2315
SITE     1 CC3  8 HIS B 298  PHE B 311  GLU B 336  ASP B 473
SITE     2 CC3  8 HOH B2191  HOH B2208  HOH B2316  HOH B2317
SITE     1 CC4  4 GLY C  37  ILE C  39  GLY C  64  CYS C  65
SITE     1 CC5 30 THR E 173  LYS E 175  LYS E 177  KCX E 201
SITE     2 CC5 30 ASP E 203  GLU E 204  HIS E 294  ARG E 295
SITE     3 CC5 30 HIS E 327  LYS E 334  LEU E 335  SER E 379
SITE     4 CC5 30 GLY E 380  GLY E 381  GLY E 403  GLY E 404
SITE     5 CC5 30  MG E 476  HOH E2112  HOH E2229  HOH E2238
SITE     6 CC5 30 HOH E2283  HOH E2284  HOH E2285  HOH E2286
SITE     7 CC5 30 HOH E2287  GLU K  60  THR K  65  TRP K  66
SITE     8 CC5 30 ASN K 123  HOH K2032
SITE     1 CC6  8 TYR E  24  THR E  68  VAL E  69  ASP E  72
SITE     2 CC6  8 EDO E1477  HOH E2037  HOH E2288  HOH E2289
SITE     1 CC7  8 LYS E  18  THR E  65  TRP E  66  THR E  67
SITE     2 CC7  8 THR E  68  EDO E1476  HOH E2007  HOH E2289
SITE     1 CC8  3 TYR E  20  GLU E  52  HOH K2276
SITE     1 CC9  4 LYS E 466  GLU E 468  PHE E 469  HOH E2290
SITE     1 DC1  4 LEU E 270  HOH E2291  HOH E2292  LEU K 270
SITE     1 DC2  5 GLY F  37  TRP F  38  ILE F  39  GLY F  64
SITE     2 DC2  5 HOH F2070
SITE     1 DC3 28 THR H 173  LYS H 175  LYS H 177  KCX H 201
SITE     2 DC3 28 ASP H 203  GLU H 204  HIS H 294  ARG H 295
SITE     3 DC3 28 HIS H 327  LYS H 334  LEU H 335  SER H 379
SITE     4 DC3 28 GLY H 380  GLY H 381  GLY H 403  GLY H 404
SITE     5 DC3 28  MG H 476  HOH H2220  HOH H2236  HOH H2277
SITE     6 DC3 28 HOH H2278  HOH H2279  HOH H2280  HOH H2281
SITE     7 DC3 28 GLU R  60  THR R  65  TRP R  66  ASN R 123
SITE     1 DC4  4 LEU H 270  HOH H2282  HOH H2283  LEU R 270
SITE     1 DC5  9 TYR H  24  GLY H  64  THR H  68  VAL H  69
SITE     2 DC5  9 ASP H  72  LEU H  77  HOH H2042  HOH H2043
SITE     3 DC5  9 HOH H2284
SITE     1 DC6  7 LYS H  18  THR H  65  TRP H  66  THR H  67
SITE     2 DC6  7 THR H  68  HOH H2017  HOH H2042
SITE     1 DC7  3 TYR H  20  GLU H  52  HOH R2307
SITE     1 DC8  8 ARG B 439  LYS H 466  PHE H 467  PHE H 469
SITE     2 DC8  8 HOH H2266  HOH H2286  HOH H2287  EDO R1478
SITE     1 DC9  7 HIS H 298  PHE H 311  PHE H 345  ASP H 473
SITE     2 DC9  7 HOH H2173  HOH H2274  HOH H2288
SITE     1 EC1  5 GLY J  37  TRP J  38  ILE J  39  GLY J  64
SITE     2 EC1  5 CYS J  65
SITE     1 EC2 29 GLU E  60  THR E  65  TRP E  66  ASN E 123
SITE     2 EC2 29 THR K 173  LYS K 175  LYS K 177  KCX K 201
SITE     3 EC2 29 ASP K 203  GLU K 204  HIS K 294  ARG K 295
SITE     4 EC2 29 HIS K 327  LYS K 334  LEU K 335  SER K 379
SITE     5 EC2 29 GLY K 380  GLY K 381  GLY K 403  GLY K 404
SITE     6 EC2 29  MG K 476  HOH K2111  HOH K2171  HOH K2268
SITE     7 EC2 29 HOH K2269  HOH K2270  HOH K2271  HOH K2272
SITE     8 EC2 29 HOH K2273
SITE     1 EC3  8 TYR K  24  THR K  68  VAL K  69  ASP K  72
SITE     2 EC3  8 EDO K1477  HOH K2034  HOH K2037  HOH K2042
SITE     1 EC4  8 LYS K  18  THR K  65  TRP K  66  THR K  67
SITE     2 EC4  8 THR K  68  EDO K1476  HOH K2034  HOH K2274
SITE     1 EC5  3 HOH E2290  GLU K  52  HOH K2275
SITE     1 EC6  5 LYS K 466  PHE K 467  GLU K 468  PHE K 469
SITE     2 EC6  5 HOH K2276
SITE     1 EC7  7 HIS K 298  PHE K 311  GLU K 336  ASP K 473
SITE     2 EC7  7 HOH K2277  HOH K2278  HOH K2279
SITE     1 EC8  4 GLY M  37  TRP M  38  GLY M  64  CYS M  65
SITE     1 EC9 28 THR O 173  LYS O 175  LYS O 177  KCX O 201
SITE     2 EC9 28 ASP O 203  GLU O 204  HIS O 294  ARG O 295
SITE     3 EC9 28 HIS O 327  LYS O 334  LEU O 335  SER O 379
SITE     4 EC9 28 GLY O 380  GLY O 381  GLY O 403  GLY O 404
SITE     5 EC9 28  MG O 476  HOH O2230  HOH O2279  HOH O2280
SITE     6 EC9 28 HOH O2281  HOH O2282  HOH O2283  GLU V  60
SITE     7 EC9 28 THR V  65  TRP V  66  ASN V 123  HOH V2079
SITE     1 FC1  8 TYR O  24  THR O  68  VAL O  69  ASP O  72
SITE     2 FC1  8 EDO O1477  HOH O2032  HOH O2039  HOH O2284
SITE     1 FC2  8 LYS O  18  THR O  65  TRP O  66  THR O  67
SITE     2 FC2  8 THR O  68  EDO O1476  HOH O2284  HOH O2285
SITE     1 FC3  2 GLU O  52  HOH V2281
SITE     1 FC4  4 LYS O 466  GLU O 468  PHE O 469  HOH O2286
SITE     1 FC5  6 ARG O 295  SER O 328  GLU O 336  ASP O 473
SITE     2 FC5  6 HOH O2193  HOH O2201
SITE     1 FC6  6 GLY P  37  TRP P  38  ILE P  39  PHE P  63
SITE     2 FC6  6 GLY P  64  CYS P  65
SITE     1 FC7 29 GLU H  60  THR H  65  TRP H  66  ASN H 123
SITE     2 FC7 29 HOH H2084  THR R 173  LYS R 175  LYS R 177
SITE     3 FC7 29 KCX R 201  ASP R 203  GLU R 204  HIS R 294
SITE     4 FC7 29 ARG R 295  HIS R 327  LYS R 334  LEU R 335
SITE     5 FC7 29 SER R 379  GLY R 380  GLY R 381  GLY R 403
SITE     6 FC7 29 GLY R 404   MG R 476  HOH R2297  HOH R2298
SITE     7 FC7 29 HOH R2299  HOH R2300  HOH R2301  HOH R2302
SITE     8 FC7 29 HOH R2303
SITE     1 FC8  7 TYR R  24  THR R  68  VAL R  69  ASP R  72
SITE     2 FC8  7 HOH R2045  HOH R2304  HOH R2305
SITE     1 FC9  7 LYS R  18  THR R  65  TRP R  66  THR R  67
SITE     2 FC9  7 THR R  68  HOH R2016  HOH R2045
SITE     1 GC1  2 EDO H1480  GLU R  52
SITE     1 GC2  6 LYS R 466  PHE R 467  GLU R 468  PHE R 469
SITE     2 GC2  6 HOH R2306  HOH R2307
SITE     1 GC3  6 HIS R 298  PHE R 345  ASP R 473  HOH R2195
SITE     2 GC3  6 HOH R2197  HOH R2214
SITE     1 GC4  7 GLY T  37  TRP T  38  ILE T  39  GLY T  64
SITE     2 GC4  7 CYS T  65  HOH T2072  HOH T2073
SITE     1 GC5 29 GLU O  60  THR O  65  TRP O  66  ASN O 123
SITE     2 GC5 29 HOH O2029  THR V 173  LYS V 175  LYS V 177
SITE     3 GC5 29 KCX V 201  ASP V 203  GLU V 204  HIS V 294
SITE     4 GC5 29 ARG V 295  HIS V 327  LYS V 334  LEU V 335
SITE     5 GC5 29 SER V 379  GLY V 380  GLY V 381  GLY V 403
SITE     6 GC5 29 GLY V 404   MG V 476  HOH V2107  HOH V2176
SITE     7 GC5 29 HOH V2223  HOH V2224  HOH V2274  HOH V2275
SITE     8 GC5 29 HOH V2276
SITE     1 GC6  4 LEU O 270  LEU V 270  HOH V2277  HOH V2278
SITE     1 GC7  8 TYR V  24  THR V  68  VAL V  69  ASP V  72
SITE     2 GC7  8 EDO V1478  HOH V2040  HOH V2279  HOH V2280
SITE     1 GC8  9 VAL V  17  LYS V  18  THR V  65  TRP V  66
SITE     2 GC8  9 THR V  67  THR V  68  EDO V1477  HOH V2016
SITE     3 GC8  9 HOH V2280
SITE     1 GC9  3 HOH O2286  GLU V  52  HOH V2007
SITE     1 HC1  6 ARG E 439  LYS V 466  PHE V 467  GLU V 468
SITE     2 HC1  6 PHE V 469  HOH V2281
SITE     1 HC2  5 ARG V 295  SER V 328  GLU V 336  ASP V 473
SITE     2 HC2  5 HOH V2187
SITE     1 HC3  6 GLY W  37  TRP W  38  ILE W  39  PHE W  63
SITE     2 HC3  6 GLY W  64  CYS W  65
CRYST1  220.820  223.969  111.752  90.00  90.00  90.00 P 21 21 2    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      0.004528  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004465  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008948        0.00000
MTRIX1   1  0.950100  0.303000  0.074330      -12.68000    1
MTRIX2   1  0.302900 -0.952900  0.011750       68.85000    1
MTRIX3   1  0.074390  0.011360 -0.997200       51.71000    1
MTRIX1   2 -0.302400  0.953200  0.001929       41.80000    1
MTRIX2   2  0.953200  0.302400  0.001161      -30.84000    1
MTRIX3   2  0.000523  0.002189 -1.000000       57.09000    1
MTRIX1   3 -0.953400 -0.301400  0.013010      141.60001    1
MTRIX2   3 -0.301600  0.950800 -0.071260       23.96000    1
MTRIX3   3  0.009109 -0.071860 -0.997400       59.81000    1
MTRIX1   4  0.000223  0.997300 -0.073190       22.08000    1
MTRIX2   4 -0.999900 -0.000675 -0.012240      111.60000    1
MTRIX3   4 -0.012260  0.073190  0.997200       -2.45800    1
MTRIX1   5  0.007167 -0.999900 -0.014760      111.20000    1
MTRIX2   5  0.997500  0.006105  0.070810      -22.26000    1
MTRIX3   5 -0.070710 -0.015230  0.997400        5.47800    1
MTRIX1   6 -0.996600 -0.003438 -0.082920      133.50000    1
MTRIX2   6 -0.001574 -0.998200  0.060300       89.63000    1
MTRIX3   6 -0.082980  0.060220  0.994700        2.84100    1
MTRIX1   7  0.303400 -0.949300  0.081980       86.64000    1
MTRIX2   7 -0.949300 -0.308600 -0.060400      123.80000    1
MTRIX3   7  0.082640 -0.059490 -0.994800       54.30000    1
MTRIX1   8  0.948400  0.307600  0.076170      -12.83000    1
MTRIX2   8  0.307900 -0.951400  0.008797       68.61000    1
MTRIX3   8  0.075170  0.015110 -0.997100       51.54000    1
MTRIX1   9 -0.306400  0.951900  0.001248       42.11000    1
MTRIX2   9  0.951900  0.306400  0.000044      -30.79000    1
MTRIX3   9 -0.000340  0.001202 -1.000000       57.17000    1
MTRIX1  10 -0.952000 -0.305600  0.014310      141.70000    1
MTRIX2  10 -0.305800  0.949100 -0.074750       24.46000    1
MTRIX3  10  0.009259 -0.075540 -0.997100       59.98000    1
MTRIX1  11  0.003915  0.997200 -0.074740       21.90000    1
MTRIX2  11 -1.000000  0.003271 -0.008736      111.30000    1
MTRIX3  11 -0.008467  0.007478  0.997200       -2.74900    1
MTRIX1  12 -0.000288 -0.999900 -0.015380      111.70000    1
MTRIX2  12  0.997200 -0.001435  0.074650      -21.88000    1
MTRIX3  12 -0.074660 -0.015310  0.997100        5.74300    1
MTRIX1  13 -0.996700 -0.002425 -0.081240      133.39999    1
MTRIX2  13 -0.002427 -0.998200  0.059570       89.75000    1
MTRIX3  13 -0.081240  0.059570  0.994900        2.76400    1
MTRIX1  14  0.302800 -0.949300  0.084050       86.72000    1
MTRIX2  14 -0.949600 -0.308000 -0.058070      123.80000    1
MTRIX3  14  0.081010 -0.062230 -0.994800       54.66000    1
      
PROCHECK
Go to PROCHECK summary
 References