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PDBsum entry 2ybv

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Top Page protein metals Protein-protein interface(s) links
Lyase PDB id
2ybv
Jmol
Contents
Protein chains
(+ 2 more) 428 a.a.
(+ 2 more) 104 a.a.
Metals
_CL ×15
Waters ×832
HEADER    LYASE                                   10-MAR-11   2YBV
TITLE     STRUCTURE OF RUBISCO FROM THERMOSYNECHOCOCCUS ELONGATUS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   3 CHAIN: A, C, E, G, I, K, M, O;
COMPND   4 EC: 4.1.1.39;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL SUBUNIT;
COMPND   8 CHAIN: B, D, F, H, J, L, N, P;
COMPND   9 EC: 4.1.1.39;
COMPND  10 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE   3 ORGANISM_TAXID: 197221;
SOURCE   4 STRAIN: BP-1;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DH5[ALPHA];
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PUC18RBCLXSTH.EL;
SOURCE  10 MOL_ID: 2;
SOURCE  11 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE  12 ORGANISM_TAXID: 197221;
SOURCE  13 STRAIN: BP-1;
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: DH5[ALPHA];
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PUC18RBCLXSTH.EL
KEYWDS    CO2/O2 SPECIFICITY, CARBON DIOXIDE FIXATION, PHOTOSYNTHESIS,
KEYWDS   2 THERMOSTABILITY, PHOTORESPIRATION, MONOOXYGENASE, HYDROXYLATION,
KEYWDS   3 OXIDOREDUCTASE, LYASE, RUBISCO, CHLOROPLAST, CALVIN CYCLE,
KEYWDS   4 THERMOPHILIC CYANOBACTERIA
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.TERLECKA,V.WILHELMI,W.BIALEK,B.GUBERNATOR,A.SZCZEPANIAK,E.HOFMANN
REVDAT   1   28-MAR-12 2YBV    0
JRNL        AUTH   B.TERLECKA,V.WILHELMI,W.BIALEK,B.GUBERNATOR,A.SZCZEPANIAK,
JRNL        AUTH 2 E.HOFMANN
JRNL        TITL   STRUCTURE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE
JRNL        TITL 2 OXYGENASE FROM THERMOSYNECHOCOCCUS ELONGATUS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0088
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) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.84
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.00
REMARK   3   NUMBER OF REFLECTIONS             : 240880
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) : 0.19763
REMARK   3   R VALUE            (WORKING SET) : 0.19577
REMARK   3   FREE R VALUE                     : 0.23167
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1
REMARK   3   FREE R VALUE TEST SET COUNT      : 12992
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) : 2.300
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.360
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 18689
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.249
REMARK   3   BIN FREE R VALUE SET COUNT          : 0
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 33736
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 15
REMARK   3   SOLVENT ATOMS            : 832
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.196
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.45
REMARK   3    B22 (A**2) : -0.77
REMARK   3    B33 (A**2) : -0.23
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.69
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.266
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.205
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.145
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.896
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.914
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 34572 ; 0.022 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 46880 ; 1.782 ; 1.948
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4224 ; 6.630 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1688 ;33.881 ;23.649
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5664 ;14.816 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   256 ;14.538 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5024 ; 0.126 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 26744 ; 0.009 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 21160 ; 0.900 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 34008 ; 1.756 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13412 ; 2.661 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12872 ; 4.279 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A C E G I K M O
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     23       A     459      2
REMARK   3           1     C     23       C     459      2
REMARK   3           1     E     23       E     459      2
REMARK   3           1     G     23       G     459      2
REMARK   3           1     I     23       I     459      2
REMARK   3           1     K     23       K     459      2
REMARK   3           1     M     23       M     459      2
REMARK   3           1     O     23       O     459      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1712 ;  0.06 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    C    (A):   1712 ;  0.06 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    E    (A):   1712 ;  0.05 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    G    (A):   1712 ;  0.05 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    I    (A):   1712 ;  0.06 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    K    (A):   1712 ;  0.06 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    M    (A):   1712 ;  0.06 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    O    (A):   1712 ;  0.06 ;  0.05
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1636 ;  0.11 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1636 ;  0.10 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1636 ;  0.10 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    G    (A):   1636 ;  0.09 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    I    (A):   1636 ;  0.09 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    K    (A):   1636 ;  0.08 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    M    (A):   1636 ;  0.11 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    O    (A):   1636 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    A (A**2):   1712 ;  0.21 ;  0.50
REMARK   3   TIGHT THERMAL      1    C (A**2):   1712 ;  0.19 ;  0.50
REMARK   3   TIGHT THERMAL      1    E (A**2):   1712 ;  0.21 ;  0.50
REMARK   3   TIGHT THERMAL      1    G (A**2):   1712 ;  0.23 ;  0.50
REMARK   3   TIGHT THERMAL      1    I (A**2):   1712 ;  0.22 ;  0.50
REMARK   3   TIGHT THERMAL      1    K (A**2):   1712 ;  0.22 ;  0.50
REMARK   3   TIGHT THERMAL      1    M (A**2):   1712 ;  0.21 ;  0.50
REMARK   3   TIGHT THERMAL      1    O (A**2):   1712 ;  0.21 ;  0.50
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1636 ;  0.22 ;  2.00
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1636 ;  0.21 ;  2.00
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1636 ;  0.23 ;  2.00
REMARK   3   MEDIUM THERMAL     1    G (A**2):   1636 ;  0.21 ;  2.00
REMARK   3   MEDIUM THERMAL     1    I (A**2):   1636 ;  0.23 ;  2.00
REMARK   3   MEDIUM THERMAL     1    K (A**2):   1636 ;  0.20 ;  2.00
REMARK   3   MEDIUM THERMAL     1    M (A**2):   1636 ;  0.21 ;  2.00
REMARK   3   MEDIUM THERMAL     1    O (A**2):   1636 ;  0.22 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : B D F H J L N P
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     B     31       B      39      2
REMARK   3           1     D     31       D      39      2
REMARK   3           1     F     31       F      39      2
REMARK   3           1     H     31       H      39      2
REMARK   3           1     J     31       J      39      2
REMARK   3           1     L     31       L      39      2
REMARK   3           1     N     31       N      39      2
REMARK   3           1     P     31       P      39      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   2    B    (A):     36 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    D    (A):     36 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    F    (A):     36 ;  0.03 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    H    (A):     36 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    J    (A):     36 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    L    (A):     36 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    N    (A):     36 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    P    (A):     36 ;  0.05 ;  0.05
REMARK   3   MEDIUM POSITIONAL  2    B    (A):     33 ;  0.05 ;  0.50
REMARK   3   MEDIUM POSITIONAL  2    D    (A):     33 ;  0.05 ;  0.50
REMARK   3   MEDIUM POSITIONAL  2    F    (A):     33 ;  0.05 ;  0.50
REMARK   3   MEDIUM POSITIONAL  2    H    (A):     33 ;  0.06 ;  0.50
REMARK   3   MEDIUM POSITIONAL  2    J    (A):     33 ;  0.06 ;  0.50
REMARK   3   MEDIUM POSITIONAL  2    L    (A):     33 ;  0.06 ;  0.50
REMARK   3   MEDIUM POSITIONAL  2    N    (A):     33 ;  0.06 ;  0.50
REMARK   3   MEDIUM POSITIONAL  2    P    (A):     33 ;  0.06 ;  0.50
REMARK   3   TIGHT THERMAL      2    B (A**2):     36 ;  0.15 ;  0.50
REMARK   3   TIGHT THERMAL      2    D (A**2):     36 ;  0.10 ;  0.50
REMARK   3   TIGHT THERMAL      2    F (A**2):     36 ;  0.24 ;  0.50
REMARK   3   TIGHT THERMAL      2    H (A**2):     36 ;  0.18 ;  0.50
REMARK   3   TIGHT THERMAL      2    J (A**2):     36 ;  0.16 ;  0.50
REMARK   3   TIGHT THERMAL      2    L (A**2):     36 ;  0.19 ;  0.50
REMARK   3   TIGHT THERMAL      2    N (A**2):     36 ;  0.18 ;  0.50
REMARK   3   TIGHT THERMAL      2    P (A**2):     36 ;  0.10 ;  0.50
REMARK   3   MEDIUM THERMAL     2    B (A**2):     33 ;  0.11 ;  2.00
REMARK   3   MEDIUM THERMAL     2    D (A**2):     33 ;  0.10 ;  2.00
REMARK   3   MEDIUM THERMAL     2    F (A**2):     33 ;  0.18 ;  2.00
REMARK   3   MEDIUM THERMAL     2    H (A**2):     33 ;  0.14 ;  2.00
REMARK   3   MEDIUM THERMAL     2    J (A**2):     33 ;  0.17 ;  2.00
REMARK   3   MEDIUM THERMAL     2    L (A**2):     33 ;  0.12 ;  2.00
REMARK   3   MEDIUM THERMAL     2    N (A**2):     33 ;  0.10 ;  2.00
REMARK   3   MEDIUM THERMAL     2    P (A**2):     33 ;  0.11 ;  2.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 2YBV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-SEP-11.
REMARK 100 THE PDBE ID CODE IS EBI-46194.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X10SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9919
REMARK 200  MONOCHROMATOR                  : SI
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 253864
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.30
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 7.3
REMARK 200  R MERGE                    (I) : 0.17
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.11
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.2
REMARK 200  R MERGE FOR SHELL          (I) : 0.43
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.80
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3RUB
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG8000, 20% PEG200, 10% GLYCEROL,
REMARK 280  100MM HEPES, PH 7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       81.73500
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 79650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 124090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -335.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I, B, P, C, K, D, J, E, M, L,
REMARK 350                    AND CHAINS: F, G, O, H, N
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     ALA A     2
REMARK 465     TYR A     3
REMARK 465     THR A     4
REMARK 465     GLN A     5
REMARK 465     SER A     6
REMARK 465     LYS A     7
REMARK 465     SER A     8
REMARK 465     GLN A     9
REMARK 465     LYS A    10
REMARK 465     VAL A    11
REMARK 465     GLY A    12
REMARK 465     TYR A    13
REMARK 465     GLN A    14
REMARK 465     ALA A    15
REMARK 465     GLY A    16
REMARK 465     VAL A    17
REMARK 465     LYS A    18
REMARK 465     ASP A    19
REMARK 465     TYR A    20
REMARK 465     ARG A    21
REMARK 465     LEU A    22
REMARK 465     THR A    65
REMARK 465     TRP A    66
REMARK 465     THR A    67
REMARK 465     THR A    68
REMARK 465     VAL A    69
REMARK 465     GLY A   404
REMARK 465     GLY A   405
REMARK 465     THR A   406
REMARK 465     LEU A   407
REMARK 465     GLU A   460
REMARK 465     LEU A   461
REMARK 465     TRP A   462
REMARK 465     LYS A   463
REMARK 465     GLU A   464
REMARK 465     ILE A   465
REMARK 465     LYS A   466
REMARK 465     PHE A   467
REMARK 465     GLU A   468
REMARK 465     PHE A   469
REMARK 465     GLU A   470
REMARK 465     ALA A   471
REMARK 465     GLN A   472
REMARK 465     ASP A   473
REMARK 465     THR A   474
REMARK 465     ILE A   475
REMARK 465     MET B     1
REMARK 465     LYS B     2
REMARK 465     ASN B   107
REMARK 465     GLN B   108
REMARK 465     ALA B   109
REMARK 465     ASN B   110
REMARK 465     SER B   111
REMARK 465     GLY B   112
REMARK 465     TYR B   113
REMARK 465     SER B   114
REMARK 465     GLY B   115
REMARK 465     TYR B   116
REMARK 465     ARG B   117
REMARK 465     TYR B   118
REMARK 465     MET C     1
REMARK 465     ALA C     2
REMARK 465     TYR C     3
REMARK 465     THR C     4
REMARK 465     GLN C     5
REMARK 465     SER C     6
REMARK 465     LYS C     7
REMARK 465     SER C     8
REMARK 465     GLN C     9
REMARK 465     LYS C    10
REMARK 465     VAL C    11
REMARK 465     GLY C    12
REMARK 465     TYR C    13
REMARK 465     GLN C    14
REMARK 465     ALA C    15
REMARK 465     GLY C    16
REMARK 465     VAL C    17
REMARK 465     LYS C    18
REMARK 465     ASP C    19
REMARK 465     TYR C    20
REMARK 465     ARG C    21
REMARK 465     LEU C    22
REMARK 465     THR C    65
REMARK 465     TRP C    66
REMARK 465     THR C    67
REMARK 465     THR C    68
REMARK 465     VAL C    69
REMARK 465     GLY C   404
REMARK 465     GLY C   405
REMARK 465     THR C   406
REMARK 465     LEU C   407
REMARK 465     GLU C   460
REMARK 465     LEU C   461
REMARK 465     TRP C   462
REMARK 465     LYS C   463
REMARK 465     GLU C   464
REMARK 465     ILE C   465
REMARK 465     LYS C   466
REMARK 465     PHE C   467
REMARK 465     GLU C   468
REMARK 465     PHE C   469
REMARK 465     GLU C   470
REMARK 465     ALA C   471
REMARK 465     GLN C   472
REMARK 465     ASP C   473
REMARK 465     THR C   474
REMARK 465     ILE C   475
REMARK 465     MET D     1
REMARK 465     LYS D     2
REMARK 465     ASN D   107
REMARK 465     GLN D   108
REMARK 465     ALA D   109
REMARK 465     ASN D   110
REMARK 465     SER D   111
REMARK 465     GLY D   112
REMARK 465     TYR D   113
REMARK 465     SER D   114
REMARK 465     GLY D   115
REMARK 465     TYR D   116
REMARK 465     ARG D   117
REMARK 465     TYR D   118
REMARK 465     MET E     1
REMARK 465     ALA E     2
REMARK 465     TYR E     3
REMARK 465     THR E     4
REMARK 465     GLN E     5
REMARK 465     SER E     6
REMARK 465     LYS E     7
REMARK 465     SER E     8
REMARK 465     GLN E     9
REMARK 465     LYS E    10
REMARK 465     VAL E    11
REMARK 465     GLY E    12
REMARK 465     TYR E    13
REMARK 465     GLN E    14
REMARK 465     ALA E    15
REMARK 465     GLY E    16
REMARK 465     VAL E    17
REMARK 465     LYS E    18
REMARK 465     ASP E    19
REMARK 465     TYR E    20
REMARK 465     ARG E    21
REMARK 465     LEU E    22
REMARK 465     THR E    65
REMARK 465     TRP E    66
REMARK 465     THR E    67
REMARK 465     THR E    68
REMARK 465     VAL E    69
REMARK 465     GLY E   404
REMARK 465     GLY E   405
REMARK 465     THR E   406
REMARK 465     LEU E   407
REMARK 465     GLU E   460
REMARK 465     LEU E   461
REMARK 465     TRP E   462
REMARK 465     LYS E   463
REMARK 465     GLU E   464
REMARK 465     ILE E   465
REMARK 465     LYS E   466
REMARK 465     PHE E   467
REMARK 465     GLU E   468
REMARK 465     PHE E   469
REMARK 465     GLU E   470
REMARK 465     ALA E   471
REMARK 465     GLN E   472
REMARK 465     ASP E   473
REMARK 465     THR E   474
REMARK 465     ILE E   475
REMARK 465     MET F     1
REMARK 465     LYS F     2
REMARK 465     ASN F   107
REMARK 465     GLN F   108
REMARK 465     ALA F   109
REMARK 465     ASN F   110
REMARK 465     SER F   111
REMARK 465     GLY F   112
REMARK 465     TYR F   113
REMARK 465     SER F   114
REMARK 465     GLY F   115
REMARK 465     TYR F   116
REMARK 465     ARG F   117
REMARK 465     TYR F   118
REMARK 465     MET G     1
REMARK 465     ALA G     2
REMARK 465     TYR G     3
REMARK 465     THR G     4
REMARK 465     GLN G     5
REMARK 465     SER G     6
REMARK 465     LYS G     7
REMARK 465     SER G     8
REMARK 465     GLN G     9
REMARK 465     LYS G    10
REMARK 465     VAL G    11
REMARK 465     GLY G    12
REMARK 465     TYR G    13
REMARK 465     GLN G    14
REMARK 465     ALA G    15
REMARK 465     GLY G    16
REMARK 465     VAL G    17
REMARK 465     LYS G    18
REMARK 465     ASP G    19
REMARK 465     TYR G    20
REMARK 465     ARG G    21
REMARK 465     LEU G    22
REMARK 465     THR G    65
REMARK 465     TRP G    66
REMARK 465     THR G    67
REMARK 465     THR G    68
REMARK 465     VAL G    69
REMARK 465     GLY G   404
REMARK 465     GLY G   405
REMARK 465     THR G   406
REMARK 465     LEU G   407
REMARK 465     GLU G   460
REMARK 465     LEU G   461
REMARK 465     TRP G   462
REMARK 465     LYS G   463
REMARK 465     GLU G   464
REMARK 465     ILE G   465
REMARK 465     LYS G   466
REMARK 465     PHE G   467
REMARK 465     GLU G   468
REMARK 465     PHE G   469
REMARK 465     GLU G   470
REMARK 465     ALA G   471
REMARK 465     GLN G   472
REMARK 465     ASP G   473
REMARK 465     THR G   474
REMARK 465     ILE G   475
REMARK 465     MET H     1
REMARK 465     LYS H     2
REMARK 465     ASN H   107
REMARK 465     GLN H   108
REMARK 465     ALA H   109
REMARK 465     ASN H   110
REMARK 465     SER H   111
REMARK 465     GLY H   112
REMARK 465     TYR H   113
REMARK 465     SER H   114
REMARK 465     GLY H   115
REMARK 465     TYR H   116
REMARK 465     ARG H   117
REMARK 465     TYR H   118
REMARK 465     MET I     1
REMARK 465     ALA I     2
REMARK 465     TYR I     3
REMARK 465     THR I     4
REMARK 465     GLN I     5
REMARK 465     SER I     6
REMARK 465     LYS I     7
REMARK 465     SER I     8
REMARK 465     GLN I     9
REMARK 465     LYS I    10
REMARK 465     VAL I    11
REMARK 465     GLY I    12
REMARK 465     TYR I    13
REMARK 465     GLN I    14
REMARK 465     ALA I    15
REMARK 465     GLY I    16
REMARK 465     VAL I    17
REMARK 465     LYS I    18
REMARK 465     ASP I    19
REMARK 465     TYR I    20
REMARK 465     ARG I    21
REMARK 465     LEU I    22
REMARK 465     THR I    65
REMARK 465     TRP I    66
REMARK 465     THR I    67
REMARK 465     THR I    68
REMARK 465     VAL I    69
REMARK 465     GLY I   404
REMARK 465     GLY I   405
REMARK 465     THR I   406
REMARK 465     LEU I   407
REMARK 465     GLU I   460
REMARK 465     LEU I   461
REMARK 465     TRP I   462
REMARK 465     LYS I   463
REMARK 465     GLU I   464
REMARK 465     ILE I   465
REMARK 465     LYS I   466
REMARK 465     PHE I   467
REMARK 465     GLU I   468
REMARK 465     PHE I   469
REMARK 465     GLU I   470
REMARK 465     ALA I   471
REMARK 465     GLN I   472
REMARK 465     ASP I   473
REMARK 465     THR I   474
REMARK 465     ILE I   475
REMARK 465     MET J     1
REMARK 465     LYS J     2
REMARK 465     ASN J   107
REMARK 465     GLN J   108
REMARK 465     ALA J   109
REMARK 465     ASN J   110
REMARK 465     SER J   111
REMARK 465     GLY J   112
REMARK 465     TYR J   113
REMARK 465     SER J   114
REMARK 465     GLY J   115
REMARK 465     TYR J   116
REMARK 465     ARG J   117
REMARK 465     TYR J   118
REMARK 465     MET K     1
REMARK 465     ALA K     2
REMARK 465     TYR K     3
REMARK 465     THR K     4
REMARK 465     GLN K     5
REMARK 465     SER K     6
REMARK 465     LYS K     7
REMARK 465     SER K     8
REMARK 465     GLN K     9
REMARK 465     LYS K    10
REMARK 465     VAL K    11
REMARK 465     GLY K    12
REMARK 465     TYR K    13
REMARK 465     GLN K    14
REMARK 465     ALA K    15
REMARK 465     GLY K    16
REMARK 465     VAL K    17
REMARK 465     LYS K    18
REMARK 465     ASP K    19
REMARK 465     TYR K    20
REMARK 465     ARG K    21
REMARK 465     LEU K    22
REMARK 465     THR K    65
REMARK 465     TRP K    66
REMARK 465     THR K    67
REMARK 465     THR K    68
REMARK 465     VAL K    69
REMARK 465     GLY K   404
REMARK 465     GLY K   405
REMARK 465     THR K   406
REMARK 465     LEU K   407
REMARK 465     GLU K   460
REMARK 465     LEU K   461
REMARK 465     TRP K   462
REMARK 465     LYS K   463
REMARK 465     GLU K   464
REMARK 465     ILE K   465
REMARK 465     LYS K   466
REMARK 465     PHE K   467
REMARK 465     GLU K   468
REMARK 465     PHE K   469
REMARK 465     GLU K   470
REMARK 465     ALA K   471
REMARK 465     GLN K   472
REMARK 465     ASP K   473
REMARK 465     THR K   474
REMARK 465     ILE K   475
REMARK 465     MET L     1
REMARK 465     LYS L     2
REMARK 465     ASN L   107
REMARK 465     GLN L   108
REMARK 465     ALA L   109
REMARK 465     ASN L   110
REMARK 465     SER L   111
REMARK 465     GLY L   112
REMARK 465     TYR L   113
REMARK 465     SER L   114
REMARK 465     GLY L   115
REMARK 465     TYR L   116
REMARK 465     ARG L   117
REMARK 465     TYR L   118
REMARK 465     MET M     1
REMARK 465     ALA M     2
REMARK 465     TYR M     3
REMARK 465     THR M     4
REMARK 465     GLN M     5
REMARK 465     SER M     6
REMARK 465     LYS M     7
REMARK 465     SER M     8
REMARK 465     GLN M     9
REMARK 465     LYS M    10
REMARK 465     VAL M    11
REMARK 465     GLY M    12
REMARK 465     TYR M    13
REMARK 465     GLN M    14
REMARK 465     ALA M    15
REMARK 465     GLY M    16
REMARK 465     VAL M    17
REMARK 465     LYS M    18
REMARK 465     ASP M    19
REMARK 465     TYR M    20
REMARK 465     ARG M    21
REMARK 465     LEU M    22
REMARK 465     THR M    65
REMARK 465     TRP M    66
REMARK 465     THR M    67
REMARK 465     THR M    68
REMARK 465     VAL M    69
REMARK 465     GLY M   404
REMARK 465     GLY M   405
REMARK 465     THR M   406
REMARK 465     LEU M   407
REMARK 465     GLU M   460
REMARK 465     LEU M   461
REMARK 465     TRP M   462
REMARK 465     LYS M   463
REMARK 465     GLU M   464
REMARK 465     ILE M   465
REMARK 465     LYS M   466
REMARK 465     PHE M   467
REMARK 465     GLU M   468
REMARK 465     PHE M   469
REMARK 465     GLU M   470
REMARK 465     ALA M   471
REMARK 465     GLN M   472
REMARK 465     ASP M   473
REMARK 465     THR M   474
REMARK 465     ILE M   475
REMARK 465     MET N     1
REMARK 465     LYS N     2
REMARK 465     ASN N   107
REMARK 465     GLN N   108
REMARK 465     ALA N   109
REMARK 465     ASN N   110
REMARK 465     SER N   111
REMARK 465     GLY N   112
REMARK 465     TYR N   113
REMARK 465     SER N   114
REMARK 465     GLY N   115
REMARK 465     TYR N   116
REMARK 465     ARG N   117
REMARK 465     TYR N   118
REMARK 465     MET O     1
REMARK 465     ALA O     2
REMARK 465     TYR O     3
REMARK 465     THR O     4
REMARK 465     GLN O     5
REMARK 465     SER O     6
REMARK 465     LYS O     7
REMARK 465     SER O     8
REMARK 465     GLN O     9
REMARK 465     LYS O    10
REMARK 465     VAL O    11
REMARK 465     GLY O    12
REMARK 465     TYR O    13
REMARK 465     GLN O    14
REMARK 465     ALA O    15
REMARK 465     GLY O    16
REMARK 465     VAL O    17
REMARK 465     LYS O    18
REMARK 465     ASP O    19
REMARK 465     TYR O    20
REMARK 465     ARG O    21
REMARK 465     LEU O    22
REMARK 465     THR O    65
REMARK 465     TRP O    66
REMARK 465     THR O    67
REMARK 465     THR O    68
REMARK 465     VAL O    69
REMARK 465     GLY O   404
REMARK 465     GLY O   405
REMARK 465     THR O   406
REMARK 465     LEU O   407
REMARK 465     GLU O   460
REMARK 465     LEU O   461
REMARK 465     TRP O   462
REMARK 465     LYS O   463
REMARK 465     GLU O   464
REMARK 465     ILE O   465
REMARK 465     LYS O   466
REMARK 465     PHE O   467
REMARK 465     GLU O   468
REMARK 465     PHE O   469
REMARK 465     GLU O   470
REMARK 465     ALA O   471
REMARK 465     GLN O   472
REMARK 465     ASP O   473
REMARK 465     THR O   474
REMARK 465     ILE O   475
REMARK 465     MET P     1
REMARK 465     LYS P     2
REMARK 465     ASN P   107
REMARK 465     GLN P   108
REMARK 465     ALA P   109
REMARK 465     ASN P   110
REMARK 465     SER P   111
REMARK 465     GLY P   112
REMARK 465     TYR P   113
REMARK 465     SER P   114
REMARK 465     GLY P   115
REMARK 465     TYR P   116
REMARK 465     ARG P   117
REMARK 465     TYR P   118
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   OG   SER C   181     O    HOH A  2045              2.17
REMARK 500   OG   SER M   370     O    HOH M  2071              2.19
REMARK 500   OE1  GLU O   204     O    HOH O  2043              2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   OE2  GLU A    52     NH2  ARG C   439     2656     2.18
REMARK 500   NH2  ARG A   439     OE2  GLU C    52     2656     2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    ARG A 139   CZ    ARG A 139   NH1    -0.117
REMARK 500    ARG A 139   CZ    ARG A 139   NH2    -0.112
REMARK 500    CYS A 172   CB    CYS A 172   SG      0.125
REMARK 500    PHE A 218   CE1   PHE A 218   CZ     -0.126
REMARK 500    PHE A 218   CE2   PHE A 218   CZ     -0.141
REMARK 500    PHE A 218   CG    PHE A 218   CD1    -0.100
REMARK 500    PHE A 218   CG    PHE A 218   CD2    -0.127
REMARK 500    CYS C 172   CB    CYS C 172   SG      0.149
REMARK 500    PHE C 218   CE1   PHE C 218   CZ     -0.139
REMARK 500    PHE C 218   CG    PHE C 218   CD1    -0.096
REMARK 500    PHE C 218   CG    PHE C 218   CD2    -0.124
REMARK 500    CYS C 247   CB    CYS C 247   SG      0.102
REMARK 500    ARG E 139   CZ    ARG E 139   NH1    -0.098
REMARK 500    ARG E 139   CZ    ARG E 139   NH2    -0.101
REMARK 500    CYS E 172   CB    CYS E 172   SG      0.114
REMARK 500    CYS E 247   CB    CYS E 247   SG      0.099
REMARK 500    PHE E 311   CE2   PHE E 311   CZ      0.118
REMARK 500    ARG E 421   CZ    ARG E 421   NH1    -0.081
REMARK 500    GLU F  41   CG    GLU F  41   CD      0.097
REMARK 500    CYS G 172   CA    CYS G 172   CB      0.081
REMARK 500    CYS G 172   CB    CYS G 172   SG      0.137
REMARK 500    ARG G 421   CZ    ARG G 421   NH1    -0.089
REMARK 500    ARG G 421   CZ    ARG G 421   NH2    -0.098
REMARK 500    CYS I 172   CB    CYS I 172   SG      0.129
REMARK 500    ARG I 421   CZ    ARG I 421   NH2    -0.109
REMARK 500    CYS K 172   CB    CYS K 172   SG      0.178
REMARK 500    PHE K 218   CE2   PHE K 218   CZ     -0.120
REMARK 500    CYS M 172   CB    CYS M 172   SG      0.104
REMARK 500    PHE M 218   CE1   PHE M 218   CZ     -0.151
REMARK 500    PHE M 218   CE2   PHE M 218   CZ     -0.177
REMARK 500    PHE M 218   CG    PHE M 218   CD2    -0.130
REMARK 500    ARG M 421   CZ    ARG M 421   NH2    -0.088
REMARK 500    CYS O 172   CB    CYS O 172   SG      0.144
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    ARG A 139   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES
REMARK 500    ARG A 139   NE  -  CZ  -  NH2 ANGL. DEV. =   6.9 DEGREES
REMARK 500    ARG A 139   NH1 -  CZ  -  NH2 ANGL. DEV. = -13.8 DEGREES
REMARK 500    CYS A 172   CA  -  CB  -  SG  ANGL. DEV. =   8.4 DEGREES
REMARK 500    ASP A 268   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ARG A 421   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A 421   NE  -  CZ  -  NH2 ANGL. DEV. =   4.3 DEGREES
REMARK 500    ARG A 421   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES
REMARK 500    ARG C 139   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES
REMARK 500    CYS C 172   CA  -  CB  -  SG  ANGL. DEV. =   7.8 DEGREES
REMARK 500    ARG C 253   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG C 253   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG C 421   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG E 139   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ARG E 139   NE  -  CZ  -  NH2 ANGL. DEV. =   7.5 DEGREES
REMARK 500    ARG E 139   NH1 -  CZ  -  NH2 ANGL. DEV. = -13.6 DEGREES
REMARK 500    ARG E 421   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG E 421   NE  -  CZ  -  NH2 ANGL. DEV. =   4.4 DEGREES
REMARK 500    ARG E 421   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.9 DEGREES
REMARK 500    ARG G 215   CD  -  NE  -  CZ  ANGL. DEV. =  15.8 DEGREES
REMARK 500    ARG G 215   NE  -  CZ  -  NH1 ANGL. DEV. =   9.5 DEGREES
REMARK 500    ARG G 215   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.6 DEGREES
REMARK 500    ARG G 421   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG G 421   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG G 421   NH1 -  CZ  -  NH2 ANGL. DEV. =  -9.2 DEGREES
REMARK 500    ARG I 139   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ASP I 367   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG I 421   NE  -  CZ  -  NH1 ANGL. DEV. =   7.8 DEGREES
REMARK 500    ARG I 421   NE  -  CZ  -  NH2 ANGL. DEV. =   5.2 DEGREES
REMARK 500    ARG I 421   NH1 -  CZ  -  NH2 ANGL. DEV. = -13.0 DEGREES
REMARK 500    ARG K 139   NE  -  CZ  -  NH2 ANGL. DEV. =   4.8 DEGREES
REMARK 500    CYS K 172   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES
REMARK 500    ARG K 421   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG K 421   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG K 421   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES
REMARK 500    ARG M 139   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG M 421   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ARG M 421   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG M 421   NH1 -  CZ  -  NH2 ANGL. DEV. = -10.6 DEGREES
REMARK 500    ARG O 139   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG O 421   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  62     -117.45   -141.79
REMARK 500    HIS A 153      -63.00   -131.19
REMARK 500    ASN A 207      -88.42   -123.95
REMARK 500    GLN A 212      103.14   -172.39
REMARK 500    ALA A 296      123.41    -27.66
REMARK 500    MET A 297       -1.48     89.12
REMARK 500    ASP A 357       86.95   -166.42
REMARK 500    TYR B  10       34.97   -149.93
REMARK 500    GLU B  11     -151.21     67.72
REMARK 500    PHE B  13       -6.52     83.19
REMARK 500    LYS B  57     -125.33     57.66
REMARK 500    ASN B  62       37.52    159.48
REMARK 500    SER B 100       83.93   -177.30
REMARK 500    SER C  62     -113.98   -145.07
REMARK 500    HIS C 153      -65.69   -128.76
REMARK 500    ASN C 207      -88.69   -124.82
REMARK 500    GLN C 212       98.68   -173.36
REMARK 500    ALA C 296      131.47    -34.72
REMARK 500    MET C 297       -6.73     85.59
REMARK 500    LEU C 335      150.83    -48.12
REMARK 500    ASP C 357       85.62   -164.14
REMARK 500    TYR D  10       38.11   -150.35
REMARK 500    GLU D  11     -146.97     64.72
REMARK 500    PHE D  13       -9.50     82.29
REMARK 500    LYS D  57     -121.24     44.04
REMARK 500    ASN D  62       55.33    150.49
REMARK 500    ILE D  93      -73.60    -45.63
REMARK 500    SER D 100       92.16   -176.42
REMARK 500    SER E  62     -112.39   -142.71
REMARK 500    ALA E 129        1.00    -68.88
REMARK 500    HIS E 153      -63.52   -133.01
REMARK 500    ASN E 207      -91.62   -123.39
REMARK 500    GLN E 212      100.12   -170.49
REMARK 500    ALA E 296      130.30    -31.62
REMARK 500    MET E 297       -5.09     84.70
REMARK 500    ASP E 357       91.47   -165.99
REMARK 500    TYR F  10       42.85   -143.19
REMARK 500    GLU F  11     -147.89     59.84
REMARK 500    PHE F  13       -7.06     80.53
REMARK 500    LYS F  57     -123.52     56.27
REMARK 500    ASN F  62       65.13   -174.68
REMARK 500    ILE F  93      -82.75    -50.00
REMARK 500    SER F 100       97.38   -161.00
REMARK 500    SER G  62     -113.70   -138.58
REMARK 500    HIS G 153      -65.84   -131.16
REMARK 500    ASN G 207      -89.96   -122.04
REMARK 500    GLN G 212      100.02   -171.21
REMARK 500    TYR G 239       92.69    -68.91
REMARK 500    ALA G 296      127.43    -27.59
REMARK 500    MET G 297       -5.98     86.42
REMARK 500
REMARK 500 THIS ENTRY HAS     124 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG G 215         0.10    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PHE B  61        23.0      L          L   OUTSIDE RANGE
REMARK 500    PHE C 345        24.7      L          L   OUTSIDE RANGE
REMARK 500    PHE D  61        23.3      L          L   OUTSIDE RANGE
REMARK 500    PHE F  61        20.1      L          L   OUTSIDE RANGE
REMARK 500    PHE H  61        23.2      L          L   OUTSIDE RANGE
REMARK 500    PHE I 345        24.5      L          L   OUTSIDE RANGE
REMARK 500    PHE K 345        24.1      L          L   OUTSIDE RANGE
REMARK 500    PHE L  61        21.9      L          L   OUTSIDE RANGE
REMARK 500    PHE N  61        22.9      L          L   OUTSIDE RANGE
REMARK 500    PHE P  61        22.0      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "CB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "EB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "GB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "IB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "KB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "MB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "OB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL E1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL G1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL G1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL I1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL I1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL K1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL K1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL M1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL M1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL O1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL O1461
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZXW   RELATED DB: PDB
REMARK 900  STRUCTURE OF ACTIVATED RUBISCO FROM THERMOSYNECHOCOCCUS
REMARK 900  ELONGATUS COMPLEXED WITH 2-CARBOXYARABINITOL-1,5-
REMARK 900  DIPHOSPHATE
DBREF  2YBV A    1   475  UNP    Q8DIS5   RBL_THEEB        1    475
DBREF  2YBV B    1   118  UNP    Q8DIS7   Q8DIS7_THEEB     1    118
DBREF  2YBV C    1   475  UNP    Q8DIS5   RBL_THEEB        1    475
DBREF  2YBV D    1   118  UNP    Q8DIS7   Q8DIS7_THEEB     1    118
DBREF  2YBV E    1   475  UNP    Q8DIS5   RBL_THEEB        1    475
DBREF  2YBV F    1   118  UNP    Q8DIS7   Q8DIS7_THEEB     1    118
DBREF  2YBV G    1   475  UNP    Q8DIS5   RBL_THEEB        1    475
DBREF  2YBV H    1   118  UNP    Q8DIS7   Q8DIS7_THEEB     1    118
DBREF  2YBV I    1   475  UNP    Q8DIS5   RBL_THEEB        1    475
DBREF  2YBV J    1   118  UNP    Q8DIS7   Q8DIS7_THEEB     1    118
DBREF  2YBV K    1   475  UNP    Q8DIS5   RBL_THEEB        1    475
DBREF  2YBV L    1   118  UNP    Q8DIS7   Q8DIS7_THEEB     1    118
DBREF  2YBV M    1   475  UNP    Q8DIS5   RBL_THEEB        1    475
DBREF  2YBV N    1   118  UNP    Q8DIS7   Q8DIS7_THEEB     1    118
DBREF  2YBV O    1   475  UNP    Q8DIS5   RBL_THEEB        1    475
DBREF  2YBV P    1   118  UNP    Q8DIS7   Q8DIS7_THEEB     1    118
SEQRES   1 A  475  MET ALA TYR THR GLN SER LYS SER GLN LYS VAL GLY TYR
SEQRES   2 A  475  GLN ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 A  475  PRO ASP TYR THR PRO LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 A  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PHE GLU GLU
SEQRES   5 A  475  ALA ALA ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 A  475  TRP THR THR VAL TRP THR ASP LEU LEU THR ASP LEU ASP
SEQRES   7 A  475  ARG TYR LYS GLY CYS CYS TYR ASP ILE GLU PRO LEU PRO
SEQRES   8 A  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR ILE ALA TYR PRO
SEQRES   9 A  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET LEU
SEQRES  10 A  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 A  475  LYS ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 A  475  TYR LEU LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 A  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO 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 LYS ASP ASP GLU ASN ILE ASN SER
SEQRES  17 A  475  GLN PRO PHE GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 A  475  ALA ASP ALA ILE HIS LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 A  475  ILE LYS GLY HIS TYR LEU ASN VAL THR ALA PRO THR CYS
SEQRES  20 A  475  GLU GLU MET LEU LYS ARG ALA GLU PHE ALA LYS GLU LEU
SEQRES  21 A  475  GLU MET PRO ILE ILE MET HIS ASP PHE LEU THR ALA GLY
SEQRES  22 A  475  PHE THR ALA ASN THR THR LEU SER LYS TRP CYS ARG ASP
SEQRES  23 A  475  ASN GLY MET LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 A  475  VAL MET ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 A  475  VAL LEU ALA LYS CYS LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 A  475  ILE HIS THR GLY THR VAL VAL GLY LYS LEU GLU GLY ASP
SEQRES  27 A  475  LYS ALA VAL THR LEU GLY PHE VAL ASP LEU LEU ARG GLU
SEQRES  28 A  475  ASN TYR ILE GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 A  475  THR GLN ASP TRP ALA SER MET PRO GLY VAL MET ALA VAL
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 A  475  VAL ASP ILE PHE GLY ASP ASP ALA VAL 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 THR ALA ASN ARG VAL ALA LEU GLU ALA CYS ILE GLN
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU MET ARG GLU GLY GLY
SEQRES  35 A  475  ASP ILE ILE ARG GLU ALA ALA ARG TRP SER PRO GLU LEU
SEQRES  36 A  475  ALA ALA ALA CYS GLU LEU TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 A  475  PHE GLU ALA GLN ASP THR ILE
SEQRES   1 B  118  MET LYS THR LEU PRO LYS GLU ARG ARG TYR GLU THR PHE
SEQRES   2 B  118  SER TYR LEU PRO PRO LEU SER ASP ALA GLN ILE ALA ARG
SEQRES   3 B  118  GLN ILE GLN TYR ALA ILE ASP GLN GLY TYR HIS PRO CYS
SEQRES   4 B  118  VAL GLU PHE ASN GLU THR SER ASN ALA GLU ILE ARG TYR
SEQRES   5 B  118  TRP THR MET TRP LYS LEU PRO LEU PHE ASN CYS THR ASN
SEQRES   6 B  118  ALA GLN ASP VAL LEU ASN GLU VAL GLN GLN CYS ARG SER
SEQRES   7 B  118  GLU TYR PRO ASN CYS PHE ILE ARG VAL VAL ALA PHE ASP
SEQRES   8 B  118  ASN ILE LYS GLN CYS GLN VAL MET SER PHE ILE VAL TYR
SEQRES   9 B  118  LYS PRO ASN GLN ALA ASN SER GLY TYR SER GLY TYR ARG
SEQRES  10 B  118  TYR
SEQRES   1 C  475  MET ALA TYR THR GLN SER LYS SER GLN LYS VAL GLY TYR
SEQRES   2 C  475  GLN ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 C  475  PRO ASP TYR THR PRO LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 C  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PHE GLU GLU
SEQRES   5 C  475  ALA ALA ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 C  475  TRP THR THR VAL TRP THR ASP LEU LEU THR ASP LEU ASP
SEQRES   7 C  475  ARG TYR LYS GLY CYS CYS TYR ASP ILE GLU PRO LEU PRO
SEQRES   8 C  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR ILE ALA TYR PRO
SEQRES   9 C  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET LEU
SEQRES  10 C  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 C  475  LYS ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 C  475  TYR LEU LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 C  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 C  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 C  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 C  475  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN ILE ASN SER
SEQRES  17 C  475  GLN PRO PHE GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 C  475  ALA ASP ALA ILE HIS LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 C  475  ILE LYS GLY HIS TYR LEU ASN VAL THR ALA PRO THR CYS
SEQRES  20 C  475  GLU GLU MET LEU LYS ARG ALA GLU PHE ALA LYS GLU LEU
SEQRES  21 C  475  GLU MET PRO ILE ILE MET HIS ASP PHE LEU THR ALA GLY
SEQRES  22 C  475  PHE THR ALA ASN THR THR LEU SER LYS TRP CYS ARG ASP
SEQRES  23 C  475  ASN GLY MET LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 C  475  VAL MET ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 C  475  VAL LEU ALA LYS CYS LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 C  475  ILE HIS THR GLY THR VAL VAL GLY LYS LEU GLU GLY ASP
SEQRES  27 C  475  LYS ALA VAL THR LEU GLY PHE VAL ASP LEU LEU ARG GLU
SEQRES  28 C  475  ASN TYR ILE GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 C  475  THR GLN ASP TRP ALA SER MET PRO GLY VAL MET ALA VAL
SEQRES  30 C  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 C  475  VAL ASP ILE PHE GLY ASP ASP ALA VAL LEU GLN PHE GLY
SEQRES  32 C  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 C  475  ALA THR ALA ASN ARG VAL ALA LEU GLU ALA CYS ILE GLN
SEQRES  34 C  475  ALA ARG ASN GLU GLY ARG ASP LEU MET ARG GLU GLY GLY
SEQRES  35 C  475  ASP ILE ILE ARG GLU ALA ALA ARG TRP SER PRO GLU LEU
SEQRES  36 C  475  ALA ALA ALA CYS GLU LEU TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 C  475  PHE GLU ALA GLN ASP THR ILE
SEQRES   1 D  118  MET LYS THR LEU PRO LYS GLU ARG ARG TYR GLU THR PHE
SEQRES   2 D  118  SER TYR LEU PRO PRO LEU SER ASP ALA GLN ILE ALA ARG
SEQRES   3 D  118  GLN ILE GLN TYR ALA ILE ASP GLN GLY TYR HIS PRO CYS
SEQRES   4 D  118  VAL GLU PHE ASN GLU THR SER ASN ALA GLU ILE ARG TYR
SEQRES   5 D  118  TRP THR MET TRP LYS LEU PRO LEU PHE ASN CYS THR ASN
SEQRES   6 D  118  ALA GLN ASP VAL LEU ASN GLU VAL GLN GLN CYS ARG SER
SEQRES   7 D  118  GLU TYR PRO ASN CYS PHE ILE ARG VAL VAL ALA PHE ASP
SEQRES   8 D  118  ASN ILE LYS GLN CYS GLN VAL MET SER PHE ILE VAL TYR
SEQRES   9 D  118  LYS PRO ASN GLN ALA ASN SER GLY TYR SER GLY TYR ARG
SEQRES  10 D  118  TYR
SEQRES   1 E  475  MET ALA TYR THR GLN SER LYS SER GLN LYS VAL GLY TYR
SEQRES   2 E  475  GLN ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 E  475  PRO ASP TYR THR PRO LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 E  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PHE GLU GLU
SEQRES   5 E  475  ALA ALA ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP LEU LEU THR ASP LEU ASP
SEQRES   7 E  475  ARG TYR LYS GLY CYS CYS TYR ASP ILE GLU PRO LEU PRO
SEQRES   8 E  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR ILE ALA TYR PRO
SEQRES   9 E  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET LEU
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 E  475  LYS ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 E  475  TYR LEU LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO 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 LYS ASP ASP GLU ASN ILE ASN SER
SEQRES  17 E  475  GLN PRO PHE GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 E  475  ALA ASP ALA ILE HIS LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 E  475  ILE LYS GLY HIS TYR LEU ASN VAL THR ALA PRO THR CYS
SEQRES  20 E  475  GLU GLU MET LEU LYS ARG ALA GLU PHE ALA LYS GLU LEU
SEQRES  21 E  475  GLU MET PRO ILE ILE MET HIS ASP PHE LEU THR ALA GLY
SEQRES  22 E  475  PHE THR ALA ASN THR THR LEU SER LYS TRP CYS ARG ASP
SEQRES  23 E  475  ASN GLY MET LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 E  475  VAL MET ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 E  475  VAL LEU ALA LYS CYS LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 E  475  ILE HIS THR GLY THR VAL VAL GLY LYS LEU GLU GLY ASP
SEQRES  27 E  475  LYS ALA VAL THR LEU GLY PHE VAL ASP LEU LEU ARG GLU
SEQRES  28 E  475  ASN TYR ILE GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 E  475  THR GLN ASP TRP ALA SER MET PRO GLY VAL MET ALA VAL
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 E  475  VAL ASP ILE PHE GLY ASP ASP ALA VAL 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 THR ALA ASN ARG VAL ALA LEU GLU ALA CYS ILE GLN
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU MET ARG GLU GLY GLY
SEQRES  35 E  475  ASP ILE ILE ARG GLU ALA ALA ARG TRP SER PRO GLU LEU
SEQRES  36 E  475  ALA ALA ALA CYS GLU LEU TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 E  475  PHE GLU ALA GLN ASP THR ILE
SEQRES   1 F  118  MET LYS THR LEU PRO LYS GLU ARG ARG TYR GLU THR PHE
SEQRES   2 F  118  SER TYR LEU PRO PRO LEU SER ASP ALA GLN ILE ALA ARG
SEQRES   3 F  118  GLN ILE GLN TYR ALA ILE ASP GLN GLY TYR HIS PRO CYS
SEQRES   4 F  118  VAL GLU PHE ASN GLU THR SER ASN ALA GLU ILE ARG TYR
SEQRES   5 F  118  TRP THR MET TRP LYS LEU PRO LEU PHE ASN CYS THR ASN
SEQRES   6 F  118  ALA GLN ASP VAL LEU ASN GLU VAL GLN GLN CYS ARG SER
SEQRES   7 F  118  GLU TYR PRO ASN CYS PHE ILE ARG VAL VAL ALA PHE ASP
SEQRES   8 F  118  ASN ILE LYS GLN CYS GLN VAL MET SER PHE ILE VAL TYR
SEQRES   9 F  118  LYS PRO ASN GLN ALA ASN SER GLY TYR SER GLY TYR ARG
SEQRES  10 F  118  TYR
SEQRES   1 G  475  MET ALA TYR THR GLN SER LYS SER GLN LYS VAL GLY TYR
SEQRES   2 G  475  GLN ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 G  475  PRO ASP TYR THR PRO LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 G  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PHE GLU GLU
SEQRES   5 G  475  ALA ALA ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 G  475  TRP THR THR VAL TRP THR ASP LEU LEU THR ASP LEU ASP
SEQRES   7 G  475  ARG TYR LYS GLY CYS CYS TYR ASP ILE GLU PRO LEU PRO
SEQRES   8 G  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR ILE ALA TYR PRO
SEQRES   9 G  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET LEU
SEQRES  10 G  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 G  475  LYS ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 G  475  TYR LEU LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 G  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 G  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 G  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 G  475  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN ILE ASN SER
SEQRES  17 G  475  GLN PRO PHE GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 G  475  ALA ASP ALA ILE HIS LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 G  475  ILE LYS GLY HIS TYR LEU ASN VAL THR ALA PRO THR CYS
SEQRES  20 G  475  GLU GLU MET LEU LYS ARG ALA GLU PHE ALA LYS GLU LEU
SEQRES  21 G  475  GLU MET PRO ILE ILE MET HIS ASP PHE LEU THR ALA GLY
SEQRES  22 G  475  PHE THR ALA ASN THR THR LEU SER LYS TRP CYS ARG ASP
SEQRES  23 G  475  ASN GLY MET LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 G  475  VAL MET ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 G  475  VAL LEU ALA LYS CYS LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 G  475  ILE HIS THR GLY THR VAL VAL GLY LYS LEU GLU GLY ASP
SEQRES  27 G  475  LYS ALA VAL THR LEU GLY PHE VAL ASP LEU LEU ARG GLU
SEQRES  28 G  475  ASN TYR ILE GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 G  475  THR GLN ASP TRP ALA SER MET PRO GLY VAL MET ALA VAL
SEQRES  30 G  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 G  475  VAL ASP ILE PHE GLY ASP ASP ALA VAL LEU GLN PHE GLY
SEQRES  32 G  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 G  475  ALA THR ALA ASN ARG VAL ALA LEU GLU ALA CYS ILE GLN
SEQRES  34 G  475  ALA ARG ASN GLU GLY ARG ASP LEU MET ARG GLU GLY GLY
SEQRES  35 G  475  ASP ILE ILE ARG GLU ALA ALA ARG TRP SER PRO GLU LEU
SEQRES  36 G  475  ALA ALA ALA CYS GLU LEU TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 G  475  PHE GLU ALA GLN ASP THR ILE
SEQRES   1 H  118  MET LYS THR LEU PRO LYS GLU ARG ARG TYR GLU THR PHE
SEQRES   2 H  118  SER TYR LEU PRO PRO LEU SER ASP ALA GLN ILE ALA ARG
SEQRES   3 H  118  GLN ILE GLN TYR ALA ILE ASP GLN GLY TYR HIS PRO CYS
SEQRES   4 H  118  VAL GLU PHE ASN GLU THR SER ASN ALA GLU ILE ARG TYR
SEQRES   5 H  118  TRP THR MET TRP LYS LEU PRO LEU PHE ASN CYS THR ASN
SEQRES   6 H  118  ALA GLN ASP VAL LEU ASN GLU VAL GLN GLN CYS ARG SER
SEQRES   7 H  118  GLU TYR PRO ASN CYS PHE ILE ARG VAL VAL ALA PHE ASP
SEQRES   8 H  118  ASN ILE LYS GLN CYS GLN VAL MET SER PHE ILE VAL TYR
SEQRES   9 H  118  LYS PRO ASN GLN ALA ASN SER GLY TYR SER GLY TYR ARG
SEQRES  10 H  118  TYR
SEQRES   1 I  475  MET ALA TYR THR GLN SER LYS SER GLN LYS VAL GLY TYR
SEQRES   2 I  475  GLN ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 I  475  PRO ASP TYR THR PRO LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 I  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PHE GLU GLU
SEQRES   5 I  475  ALA ALA ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 I  475  TRP THR THR VAL TRP THR ASP LEU LEU THR ASP LEU ASP
SEQRES   7 I  475  ARG TYR LYS GLY CYS CYS TYR ASP ILE GLU PRO LEU PRO
SEQRES   8 I  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR ILE ALA TYR PRO
SEQRES   9 I  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET LEU
SEQRES  10 I  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 I  475  LYS ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 I  475  TYR LEU LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 I  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 I  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 I  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 I  475  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN ILE ASN SER
SEQRES  17 I  475  GLN PRO PHE GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 I  475  ALA ASP ALA ILE HIS LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 I  475  ILE LYS GLY HIS TYR LEU ASN VAL THR ALA PRO THR CYS
SEQRES  20 I  475  GLU GLU MET LEU LYS ARG ALA GLU PHE ALA LYS GLU LEU
SEQRES  21 I  475  GLU MET PRO ILE ILE MET HIS ASP PHE LEU THR ALA GLY
SEQRES  22 I  475  PHE THR ALA ASN THR THR LEU SER LYS TRP CYS ARG ASP
SEQRES  23 I  475  ASN GLY MET LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 I  475  VAL MET ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 I  475  VAL LEU ALA LYS CYS LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 I  475  ILE HIS THR GLY THR VAL VAL GLY LYS LEU GLU GLY ASP
SEQRES  27 I  475  LYS ALA VAL THR LEU GLY PHE VAL ASP LEU LEU ARG GLU
SEQRES  28 I  475  ASN TYR ILE GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 I  475  THR GLN ASP TRP ALA SER MET PRO GLY VAL MET ALA VAL
SEQRES  30 I  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 I  475  VAL ASP ILE PHE GLY ASP ASP ALA VAL LEU GLN PHE GLY
SEQRES  32 I  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 I  475  ALA THR ALA ASN ARG VAL ALA LEU GLU ALA CYS ILE GLN
SEQRES  34 I  475  ALA ARG ASN GLU GLY ARG ASP LEU MET ARG GLU GLY GLY
SEQRES  35 I  475  ASP ILE ILE ARG GLU ALA ALA ARG TRP SER PRO GLU LEU
SEQRES  36 I  475  ALA ALA ALA CYS GLU LEU TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 I  475  PHE GLU ALA GLN ASP THR ILE
SEQRES   1 J  118  MET LYS THR LEU PRO LYS GLU ARG ARG TYR GLU THR PHE
SEQRES   2 J  118  SER TYR LEU PRO PRO LEU SER ASP ALA GLN ILE ALA ARG
SEQRES   3 J  118  GLN ILE GLN TYR ALA ILE ASP GLN GLY TYR HIS PRO CYS
SEQRES   4 J  118  VAL GLU PHE ASN GLU THR SER ASN ALA GLU ILE ARG TYR
SEQRES   5 J  118  TRP THR MET TRP LYS LEU PRO LEU PHE ASN CYS THR ASN
SEQRES   6 J  118  ALA GLN ASP VAL LEU ASN GLU VAL GLN GLN CYS ARG SER
SEQRES   7 J  118  GLU TYR PRO ASN CYS PHE ILE ARG VAL VAL ALA PHE ASP
SEQRES   8 J  118  ASN ILE LYS GLN CYS GLN VAL MET SER PHE ILE VAL TYR
SEQRES   9 J  118  LYS PRO ASN GLN ALA ASN SER GLY TYR SER GLY TYR ARG
SEQRES  10 J  118  TYR
SEQRES   1 K  475  MET ALA TYR THR GLN SER LYS SER GLN LYS VAL GLY TYR
SEQRES   2 K  475  GLN ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 K  475  PRO ASP TYR THR PRO LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 K  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PHE GLU GLU
SEQRES   5 K  475  ALA ALA ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 K  475  TRP THR THR VAL TRP THR ASP LEU LEU THR ASP LEU ASP
SEQRES   7 K  475  ARG TYR LYS GLY CYS CYS TYR ASP ILE GLU PRO LEU PRO
SEQRES   8 K  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR ILE ALA TYR PRO
SEQRES   9 K  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET LEU
SEQRES  10 K  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 K  475  LYS ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 K  475  TYR LEU LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 K  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO 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 LYS ASP ASP GLU ASN ILE ASN SER
SEQRES  17 K  475  GLN PRO PHE GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 K  475  ALA ASP ALA ILE HIS LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 K  475  ILE LYS GLY HIS TYR LEU ASN VAL THR ALA PRO THR CYS
SEQRES  20 K  475  GLU GLU MET LEU LYS ARG ALA GLU PHE ALA LYS GLU LEU
SEQRES  21 K  475  GLU MET PRO ILE ILE MET HIS ASP PHE LEU THR ALA GLY
SEQRES  22 K  475  PHE THR ALA ASN THR THR LEU SER LYS TRP CYS ARG ASP
SEQRES  23 K  475  ASN GLY MET LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 K  475  VAL MET ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 K  475  VAL LEU ALA LYS CYS LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 K  475  ILE HIS THR GLY THR VAL VAL GLY LYS LEU GLU GLY ASP
SEQRES  27 K  475  LYS ALA VAL THR LEU GLY PHE VAL ASP LEU LEU ARG GLU
SEQRES  28 K  475  ASN TYR ILE GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 K  475  THR GLN ASP TRP ALA SER MET PRO GLY VAL MET ALA VAL
SEQRES  30 K  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 K  475  VAL ASP ILE PHE GLY ASP ASP ALA VAL 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 THR ALA ASN ARG VAL ALA LEU GLU ALA CYS ILE GLN
SEQRES  34 K  475  ALA ARG ASN GLU GLY ARG ASP LEU MET ARG GLU GLY GLY
SEQRES  35 K  475  ASP ILE ILE ARG GLU ALA ALA ARG TRP SER PRO GLU LEU
SEQRES  36 K  475  ALA ALA ALA CYS GLU LEU TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 K  475  PHE GLU ALA GLN ASP THR ILE
SEQRES   1 L  118  MET LYS THR LEU PRO LYS GLU ARG ARG TYR GLU THR PHE
SEQRES   2 L  118  SER TYR LEU PRO PRO LEU SER ASP ALA GLN ILE ALA ARG
SEQRES   3 L  118  GLN ILE GLN TYR ALA ILE ASP GLN GLY TYR HIS PRO CYS
SEQRES   4 L  118  VAL GLU PHE ASN GLU THR SER ASN ALA GLU ILE ARG TYR
SEQRES   5 L  118  TRP THR MET TRP LYS LEU PRO LEU PHE ASN CYS THR ASN
SEQRES   6 L  118  ALA GLN ASP VAL LEU ASN GLU VAL GLN GLN CYS ARG SER
SEQRES   7 L  118  GLU TYR PRO ASN CYS PHE ILE ARG VAL VAL ALA PHE ASP
SEQRES   8 L  118  ASN ILE LYS GLN CYS GLN VAL MET SER PHE ILE VAL TYR
SEQRES   9 L  118  LYS PRO ASN GLN ALA ASN SER GLY TYR SER GLY TYR ARG
SEQRES  10 L  118  TYR
SEQRES   1 M  475  MET ALA TYR THR GLN SER LYS SER GLN LYS VAL GLY TYR
SEQRES   2 M  475  GLN ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 M  475  PRO ASP TYR THR PRO LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 M  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PHE GLU GLU
SEQRES   5 M  475  ALA ALA ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 M  475  TRP THR THR VAL TRP THR ASP LEU LEU THR ASP LEU ASP
SEQRES   7 M  475  ARG TYR LYS GLY CYS CYS TYR ASP ILE GLU PRO LEU PRO
SEQRES   8 M  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR ILE ALA TYR PRO
SEQRES   9 M  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET LEU
SEQRES  10 M  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 M  475  LYS ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 M  475  TYR LEU LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 M  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 M  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 M  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 M  475  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN ILE ASN SER
SEQRES  17 M  475  GLN PRO PHE GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 M  475  ALA ASP ALA ILE HIS LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 M  475  ILE LYS GLY HIS TYR LEU ASN VAL THR ALA PRO THR CYS
SEQRES  20 M  475  GLU GLU MET LEU LYS ARG ALA GLU PHE ALA LYS GLU LEU
SEQRES  21 M  475  GLU MET PRO ILE ILE MET HIS ASP PHE LEU THR ALA GLY
SEQRES  22 M  475  PHE THR ALA ASN THR THR LEU SER LYS TRP CYS ARG ASP
SEQRES  23 M  475  ASN GLY MET LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 M  475  VAL MET ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 M  475  VAL LEU ALA LYS CYS LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 M  475  ILE HIS THR GLY THR VAL VAL GLY LYS LEU GLU GLY ASP
SEQRES  27 M  475  LYS ALA VAL THR LEU GLY PHE VAL ASP LEU LEU ARG GLU
SEQRES  28 M  475  ASN TYR ILE GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 M  475  THR GLN ASP TRP ALA SER MET PRO GLY VAL MET ALA VAL
SEQRES  30 M  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 M  475  VAL ASP ILE PHE GLY ASP ASP ALA VAL LEU GLN PHE GLY
SEQRES  32 M  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 M  475  ALA THR ALA ASN ARG VAL ALA LEU GLU ALA CYS ILE GLN
SEQRES  34 M  475  ALA ARG ASN GLU GLY ARG ASP LEU MET ARG GLU GLY GLY
SEQRES  35 M  475  ASP ILE ILE ARG GLU ALA ALA ARG TRP SER PRO GLU LEU
SEQRES  36 M  475  ALA ALA ALA CYS GLU LEU TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 M  475  PHE GLU ALA GLN ASP THR ILE
SEQRES   1 N  118  MET LYS THR LEU PRO LYS GLU ARG ARG TYR GLU THR PHE
SEQRES   2 N  118  SER TYR LEU PRO PRO LEU SER ASP ALA GLN ILE ALA ARG
SEQRES   3 N  118  GLN ILE GLN TYR ALA ILE ASP GLN GLY TYR HIS PRO CYS
SEQRES   4 N  118  VAL GLU PHE ASN GLU THR SER ASN ALA GLU ILE ARG TYR
SEQRES   5 N  118  TRP THR MET TRP LYS LEU PRO LEU PHE ASN CYS THR ASN
SEQRES   6 N  118  ALA GLN ASP VAL LEU ASN GLU VAL GLN GLN CYS ARG SER
SEQRES   7 N  118  GLU TYR PRO ASN CYS PHE ILE ARG VAL VAL ALA PHE ASP
SEQRES   8 N  118  ASN ILE LYS GLN CYS GLN VAL MET SER PHE ILE VAL TYR
SEQRES   9 N  118  LYS PRO ASN GLN ALA ASN SER GLY TYR SER GLY TYR ARG
SEQRES  10 N  118  TYR
SEQRES   1 O  475  MET ALA TYR THR GLN SER LYS SER GLN LYS VAL GLY TYR
SEQRES   2 O  475  GLN ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 O  475  PRO ASP TYR THR PRO LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 O  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PHE GLU GLU
SEQRES   5 O  475  ALA ALA ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 O  475  TRP THR THR VAL TRP THR ASP LEU LEU THR ASP LEU ASP
SEQRES   7 O  475  ARG TYR LYS GLY CYS CYS TYR ASP ILE GLU PRO LEU PRO
SEQRES   8 O  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR ILE ALA TYR PRO
SEQRES   9 O  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET LEU
SEQRES  10 O  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 O  475  LYS ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 O  475  TYR LEU LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 O  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO 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 LYS ASP ASP GLU ASN ILE ASN SER
SEQRES  17 O  475  GLN PRO PHE GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 O  475  ALA ASP ALA ILE HIS LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 O  475  ILE LYS GLY HIS TYR LEU ASN VAL THR ALA PRO THR CYS
SEQRES  20 O  475  GLU GLU MET LEU LYS ARG ALA GLU PHE ALA LYS GLU LEU
SEQRES  21 O  475  GLU MET PRO ILE ILE MET HIS ASP PHE LEU THR ALA GLY
SEQRES  22 O  475  PHE THR ALA ASN THR THR LEU SER LYS TRP CYS ARG ASP
SEQRES  23 O  475  ASN GLY MET LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 O  475  VAL MET ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 O  475  VAL LEU ALA LYS CYS LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 O  475  ILE HIS THR GLY THR VAL VAL GLY LYS LEU GLU GLY ASP
SEQRES  27 O  475  LYS ALA VAL THR LEU GLY PHE VAL ASP LEU LEU ARG GLU
SEQRES  28 O  475  ASN TYR ILE GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 O  475  THR GLN ASP TRP ALA SER MET PRO GLY VAL MET ALA VAL
SEQRES  30 O  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 O  475  VAL ASP ILE PHE GLY ASP ASP ALA VAL 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 THR ALA ASN ARG VAL ALA LEU GLU ALA CYS ILE GLN
SEQRES  34 O  475  ALA ARG ASN GLU GLY ARG ASP LEU MET ARG GLU GLY GLY
SEQRES  35 O  475  ASP ILE ILE ARG GLU ALA ALA ARG TRP SER PRO GLU LEU
SEQRES  36 O  475  ALA ALA ALA CYS GLU LEU TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 O  475  PHE GLU ALA GLN ASP THR ILE
SEQRES   1 P  118  MET LYS THR LEU PRO LYS GLU ARG ARG TYR GLU THR PHE
SEQRES   2 P  118  SER TYR LEU PRO PRO LEU SER ASP ALA GLN ILE ALA ARG
SEQRES   3 P  118  GLN ILE GLN TYR ALA ILE ASP GLN GLY TYR HIS PRO CYS
SEQRES   4 P  118  VAL GLU PHE ASN GLU THR SER ASN ALA GLU ILE ARG TYR
SEQRES   5 P  118  TRP THR MET TRP LYS LEU PRO LEU PHE ASN CYS THR ASN
SEQRES   6 P  118  ALA GLN ASP VAL LEU ASN GLU VAL GLN GLN CYS ARG SER
SEQRES   7 P  118  GLU TYR PRO ASN CYS PHE ILE ARG VAL VAL ALA PHE ASP
SEQRES   8 P  118  ASN ILE LYS GLN CYS GLN VAL MET SER PHE ILE VAL TYR
SEQRES   9 P  118  LYS PRO ASN GLN ALA ASN SER GLY TYR SER GLY TYR ARG
SEQRES  10 P  118  TYR
HET     CL  A1460       1
HET     CL  A1461       1
HET     CL  C1460       1
HET     CL  C1461       1
HET     CL  E1460       1
HET     CL  G1460       1
HET     CL  G1461       1
HET     CL  I1460       1
HET     CL  I1461       1
HET     CL  K1460       1
HET     CL  K1461       1
HET     CL  M1460       1
HET     CL  M1461       1
HET     CL  O1460       1
HET     CL  O1461       1
HETNAM      CL CHLORIDE ION
FORMUL  17   CL    15(CL 1-)
FORMUL  18  HOH   *832(H2 O)
HELIX    1   1 PRO A   49  SER A   61  1                                  13
HELIX    2   2 TRP A   70  LEU A   74  5                                   5
HELIX    3   3 ASP A   76  LYS A   81  5                                   6
HELIX    4   4 PRO A  104  PHE A  108  5                                   5
HELIX    5   5 SER A  112  GLY A  122  1                                  11
HELIX    6   6 ASN A  123  PHE A  127  5                                   5
HELIX    7   7 PRO A  141  LYS A  146  1                                   6
HELIX    8   8 GLY A  154  ASN A  163  1                                  10
HELIX    9   9 SER A  181  GLY A  195  1                                  15
HELIX   10  10 ARG A  213  GLY A  233  1                                  21
HELIX   11  11 THR A  246  LEU A  260  1                                  15
HELIX   12  12 PHE A  269  GLY A  288  1                                  20
HELIX   13  13 MET A  297  ARG A  303  1                                   7
HELIX   14  14 HIS A  310  GLY A  322  1                                  13
HELIX   15  15 LEU A  335  GLU A  351  1                                  17
HELIX   16  16 ARG A  358  GLY A  361  5                                   4
HELIX   17  17 HIS A  383  TRP A  385  5                                   3
HELIX   18  18 HIS A  386  GLY A  395  1                                  10
HELIX   19  19 GLY A  412  GLU A  433  1                                  22
HELIX   20  20 ASP A  436  ALA A  458  1                                  23
HELIX   21  21 SER B   20  GLY B   35  1                                  16
HELIX   22  22 ASN B   65  TYR B   80  1                                  16
HELIX   23  23 PRO C   49  SER C   61  1                                  13
HELIX   24  24 TRP C   70  LEU C   74  5                                   5
HELIX   25  25 ASP C   76  LYS C   81  5                                   6
HELIX   26  26 PRO C  104  PHE C  108  5                                   5
HELIX   27  27 SER C  112  GLY C  122  1                                  11
HELIX   28  28 ASN C  123  PHE C  127  5                                   5
HELIX   29  29 PRO C  141  LYS C  146  1                                   6
HELIX   30  30 GLY C  154  ASN C  163  1                                  10
HELIX   31  31 SER C  181  GLY C  195  1                                  15
HELIX   32  32 ARG C  213  GLY C  233  1                                  21
HELIX   33  33 THR C  246  LEU C  260  1                                  15
HELIX   34  34 PHE C  269  GLY C  288  1                                  20
HELIX   35  35 MET C  297  ARG C  303  1                                   7
HELIX   36  36 HIS C  310  GLY C  322  1                                  13
HELIX   37  37 LEU C  335  GLU C  351  1                                  17
HELIX   38  38 ARG C  358  GLY C  361  5                                   4
HELIX   39  39 HIS C  383  TRP C  385  5                                   3
HELIX   40  40 HIS C  386  GLY C  395  1                                  10
HELIX   41  41 GLY C  412  GLU C  433  1                                  22
HELIX   42  42 ASP C  436  ALA C  458  1                                  23
HELIX   43  43 SER D   20  GLN D   34  1                                  15
HELIX   44  44 ASN D   65  TYR D   80  1                                  16
HELIX   45  45 PRO E   49  SER E   61  1                                  13
HELIX   46  46 TRP E   70  LEU E   74  5                                   5
HELIX   47  47 ASP E   76  LYS E   81  5                                   6
HELIX   48  48 PRO E  104  PHE E  108  5                                   5
HELIX   49  49 SER E  112  GLY E  122  1                                  11
HELIX   50  50 ASN E  123  PHE E  127  5                                   5
HELIX   51  51 PRO E  141  LYS E  146  1                                   6
HELIX   52  52 GLY E  154  ASN E  163  1                                  10
HELIX   53  53 SER E  181  GLY E  195  1                                  15
HELIX   54  54 ARG E  213  GLY E  233  1                                  21
HELIX   55  55 THR E  246  LEU E  260  1                                  15
HELIX   56  56 PHE E  269  GLY E  288  1                                  20
HELIX   57  57 MET E  297  ARG E  303  1                                   7
HELIX   58  58 HIS E  310  GLY E  322  1                                  13
HELIX   59  59 LEU E  335  GLU E  351  1                                  17
HELIX   60  60 ARG E  358  GLY E  361  5                                   4
HELIX   61  61 HIS E  383  TRP E  385  5                                   3
HELIX   62  62 HIS E  386  GLY E  395  1                                  10
HELIX   63  63 GLY E  412  GLU E  433  1                                  22
HELIX   64  64 ASP E  436  ALA E  458  1                                  23
HELIX   65  65 SER F   20  GLN F   34  1                                  15
HELIX   66  66 ALA F   66  TYR F   80  1                                  15
HELIX   67  67 PRO G   49  SER G   61  1                                  13
HELIX   68  68 TRP G   70  LEU G   74  5                                   5
HELIX   69  69 ASP G   76  LYS G   81  5                                   6
HELIX   70  70 PRO G  104  PHE G  108  5                                   5
HELIX   71  71 SER G  112  GLY G  122  1                                  11
HELIX   72  72 ASN G  123  PHE G  127  5                                   5
HELIX   73  73 PRO G  141  LYS G  146  1                                   6
HELIX   74  74 GLY G  154  ASN G  163  1                                  10
HELIX   75  75 SER G  181  GLY G  195  1                                  15
HELIX   76  76 ARG G  213  GLY G  233  1                                  21
HELIX   77  77 THR G  246  LEU G  260  1                                  15
HELIX   78  78 PHE G  269  GLY G  288  1                                  20
HELIX   79  79 MET G  297  ARG G  303  1                                   7
HELIX   80  80 HIS G  310  GLY G  322  1                                  13
HELIX   81  81 LEU G  335  GLU G  351  1                                  17
HELIX   82  82 ARG G  358  GLY G  361  5                                   4
HELIX   83  83 HIS G  383  TRP G  385  5                                   3
HELIX   84  84 HIS G  386  GLY G  395  1                                  10
HELIX   85  85 GLY G  412  GLU G  433  1                                  22
HELIX   86  86 ASP G  436  ALA G  458  1                                  23
HELIX   87  87 SER H   20  GLN H   34  1                                  15
HELIX   88  88 ASN H   65  TYR H   80  1                                  16
HELIX   89  89 PRO I   49  SER I   61  1                                  13
HELIX   90  90 TRP I   70  LEU I   74  5                                   5
HELIX   91  91 ASP I   76  LYS I   81  5                                   6
HELIX   92  92 PRO I  104  PHE I  108  5                                   5
HELIX   93  93 SER I  112  GLY I  122  1                                  11
HELIX   94  94 ASN I  123  PHE I  127  5                                   5
HELIX   95  95 PRO I  141  LYS I  146  1                                   6
HELIX   96  96 GLY I  154  ASN I  163  1                                  10
HELIX   97  97 SER I  181  GLY I  195  1                                  15
HELIX   98  98 ARG I  213  GLY I  233  1                                  21
HELIX   99  99 THR I  246  LEU I  260  1                                  15
HELIX  100 100 PHE I  269  GLY I  288  1                                  20
HELIX  101 101 MET I  297  ARG I  303  1                                   7
HELIX  102 102 HIS I  310  GLY I  322  1                                  13
HELIX  103 103 LEU I  335  GLU I  351  1                                  17
HELIX  104 104 ARG I  358  GLY I  361  5                                   4
HELIX  105 105 HIS I  383  TRP I  385  5                                   3
HELIX  106 106 HIS I  386  GLY I  395  1                                  10
HELIX  107 107 GLY I  412  GLU I  433  1                                  22
HELIX  108 108 ASP I  436  ALA I  458  1                                  23
HELIX  109 109 SER J   20  GLN J   34  1                                  15
HELIX  110 110 ASN J   65  TYR J   80  1                                  16
HELIX  111 111 PRO K   49  SER K   61  1                                  13
HELIX  112 112 TRP K   70  LEU K   74  5                                   5
HELIX  113 113 ASP K   76  LYS K   81  5                                   6
HELIX  114 114 PRO K  104  PHE K  108  5                                   5
HELIX  115 115 SER K  112  GLY K  122  1                                  11
HELIX  116 116 ASN K  123  PHE K  127  5                                   5
HELIX  117 117 PRO K  141  LYS K  146  1                                   6
HELIX  118 118 GLY K  154  ASN K  163  1                                  10
HELIX  119 119 SER K  181  GLY K  195  1                                  15
HELIX  120 120 ARG K  213  GLY K  233  1                                  21
HELIX  121 121 THR K  246  LEU K  260  1                                  15
HELIX  122 122 PHE K  269  GLY K  288  1                                  20
HELIX  123 123 MET K  297  ARG K  303  1                                   7
HELIX  124 124 HIS K  310  GLY K  322  1                                  13
HELIX  125 125 LEU K  335  GLU K  351  1                                  17
HELIX  126 126 ARG K  358  GLY K  361  5                                   4
HELIX  127 127 HIS K  383  TRP K  385  5                                   3
HELIX  128 128 HIS K  386  GLY K  395  1                                  10
HELIX  129 129 GLY K  412  GLU K  433  1                                  22
HELIX  130 130 ASP K  436  ALA K  458  1                                  23
HELIX  131 131 SER L   20  GLN L   34  1                                  15
HELIX  132 132 ASN L   65  TYR L   80  1                                  16
HELIX  133 133 PRO M   49  SER M   61  1                                  13
HELIX  134 134 TRP M   70  LEU M   74  5                                   5
HELIX  135 135 ASP M   76  LYS M   81  5                                   6
HELIX  136 136 PRO M  104  PHE M  108  5                                   5
HELIX  137 137 SER M  112  GLY M  122  1                                  11
HELIX  138 138 ASN M  123  PHE M  127  5                                   5
HELIX  139 139 PRO M  141  LYS M  146  1                                   6
HELIX  140 140 GLY M  154  ASN M  163  1                                  10
HELIX  141 141 SER M  181  GLY M  195  1                                  15
HELIX  142 142 ARG M  213  GLY M  233  1                                  21
HELIX  143 143 THR M  246  LEU M  260  1                                  15
HELIX  144 144 PHE M  269  GLY M  288  1                                  20
HELIX  145 145 MET M  297  ARG M  303  1                                   7
HELIX  146 146 HIS M  310  GLY M  322  1                                  13
HELIX  147 147 LEU M  335  GLU M  351  1                                  17
HELIX  148 148 ARG M  358  GLY M  361  5                                   4
HELIX  149 149 HIS M  383  TRP M  385  5                                   3
HELIX  150 150 HIS M  386  GLY M  395  1                                  10
HELIX  151 151 GLY M  412  GLU M  433  1                                  22
HELIX  152 152 ASP M  436  ALA M  458  1                                  23
HELIX  153 153 SER N   20  GLN N   34  1                                  15
HELIX  154 154 ALA N   66  TYR N   80  1                                  15
HELIX  155 155 PRO O   49  SER O   61  1                                  13
HELIX  156 156 TRP O   70  LEU O   74  5                                   5
HELIX  157 157 ASP O   76  LYS O   81  5                                   6
HELIX  158 158 PRO O  104  PHE O  108  5                                   5
HELIX  159 159 SER O  112  GLY O  122  1                                  11
HELIX  160 160 ASN O  123  PHE O  127  5                                   5
HELIX  161 161 PRO O  141  LYS O  146  1                                   6
HELIX  162 162 GLY O  154  ASN O  163  1                                  10
HELIX  163 163 SER O  181  GLY O  195  1                                  15
HELIX  164 164 ARG O  213  GLY O  233  1                                  21
HELIX  165 165 THR O  246  LEU O  260  1                                  15
HELIX  166 166 PHE O  269  GLY O  288  1                                  20
HELIX  167 167 MET O  297  ARG O  303  1                                   7
HELIX  168 168 HIS O  310  GLY O  322  1                                  13
HELIX  169 169 LEU O  335  GLU O  351  1                                  17
HELIX  170 170 ARG O  358  GLY O  361  5                                   4
HELIX  171 171 HIS O  383  TRP O  385  5                                   3
HELIX  172 172 HIS O  386  GLY O  395  1                                  10
HELIX  173 173 GLY O  412  GLU O  433  1                                  22
HELIX  174 174 ASP O  436  ALA O  458  1                                  23
HELIX  175 175 SER P   20  GLN P   34  1                                  15
HELIX  176 176 ASN P   65  TYR P   80  1                                  16
SHEET    1  AA 5 CYS A  83  PRO A  89  0
SHEET    2  AA 5 PHE 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  LYS 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 9 LEU A 169  THR A 173  0
SHEET    2  AB 9 ALA A 398  PHE A 402  1  O  ALA A 398   N  LEU A 169
SHEET    3  AB 9 MET A 375  SER A 379  1  O  ALA A 376   N  VAL A 399
SHEET    4  AB 9 HIS A 325  HIS A 327  1  O  ILE A 326   N  VAL A 377
SHEET    5  AB 9 LEU A 290  HIS A 294  1  O  ILE A 293   N  HIS A 327
SHEET    6  AB 9 ILE A 264  ASP A 268  1  O  ILE A 265   N  HIS A 292
SHEET    7  AB 9 GLY A 237  ASN A 241  1  O  LEU A 240   N  MET A 266
SHEET    8  AB 9 PHE A 199  LYS A 201  1  O  THR A 200   N  TYR A 239
SHEET    9  AB 9 LEU A 169  THR A 173  1  O  LEU A 170   N  PHE A 199
SHEET    1  AC 2 TYR A 353  ILE A 354  0
SHEET    2  AC 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  ILE A 354
SHEET    1  BA 4 THR B  54  MET B  55  0
SHEET    2  BA 4 HIS B  37  ASN B  43 -1  O  PHE B  42   N  THR B  54
SHEET    3  BA 4 PHE B  84  ASP B  91 -1  O  PHE B  84   N  ASN B  43
SHEET    4  BA 4 CYS B  96  TYR B 104 -1  O  CYS B  96   N  ASP B  91
SHEET    1  CA 5 CYS C  83  PRO C  89  0
SHEET    2  CA 5 PHE C  97  TYR C 103 -1  O  ILE C  98   N  GLU C  88
SHEET    3  CA 5 ILE C  36  PRO C  44 -1  O  ILE C  36   N  TYR C 103
SHEET    4  CA 5 LEU C 130  ARG C 139 -1  N  LYS C 131   O  THR C  43
SHEET    5  CA 5 GLY C 308  ILE C 309  1  O  GLY C 308   N  LEU C 135
SHEET    1  CB 9 LEU C 169  THR C 173  0
SHEET    2  CB 9 ALA C 398  PHE C 402  1  O  ALA C 398   N  LEU C 169
SHEET    3  CB 9 MET C 375  SER C 379  1  O  ALA C 376   N  VAL C 399
SHEET    4  CB 9 HIS C 325  HIS C 327  1  O  ILE C 326   N  VAL C 377
SHEET    5  CB 9 LEU C 290  HIS C 294  1  O  ILE C 293   N  HIS C 327
SHEET    6  CB 9 ILE C 264  ASP C 268  1  O  ILE C 265   N  HIS C 292
SHEET    7  CB 9 GLY C 237  ASN C 241  1  O  LEU C 240   N  MET C 266
SHEET    8  CB 9 PHE C 199  LYS C 201  1  O  THR C 200   N  TYR C 239
SHEET    9  CB 9 LEU C 169  THR C 173  1  O  CYS C 172   N  LYS C 201
SHEET    1  CC 2 TYR C 353  ILE C 354  0
SHEET    2  CC 2 GLN C 366  ASP C 367 -1  O  GLN C 366   N  ILE C 354
SHEET    1  DA 4 THR D  54  MET D  55  0
SHEET    2  DA 4 HIS D  37  ASN D  43 -1  O  PHE D  42   N  THR D  54
SHEET    3  DA 4 PHE D  84  ASP D  91 -1  O  PHE D  84   N  ASN D  43
SHEET    4  DA 4 CYS D  96  TYR D 104 -1  O  CYS D  96   N  ASP D  91
SHEET    1  EA 5 CYS E  83  PRO E  89  0
SHEET    2  EA 5 PHE 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  LYS 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 9 LEU E 169  THR E 173  0
SHEET    2  EB 9 ALA E 398  PHE E 402  1  O  ALA E 398   N  LEU E 169
SHEET    3  EB 9 MET E 375  SER E 379  1  O  ALA E 376   N  VAL E 399
SHEET    4  EB 9 HIS E 325  HIS E 327  1  O  ILE E 326   N  VAL E 377
SHEET    5  EB 9 LEU E 290  HIS E 294  1  O  ILE E 293   N  HIS E 327
SHEET    6  EB 9 ILE E 264  ASP E 268  1  O  ILE E 265   N  HIS E 292
SHEET    7  EB 9 GLY E 237  ASN E 241  1  O  LEU E 240   N  MET E 266
SHEET    8  EB 9 PHE E 199  LYS E 201  1  O  THR E 200   N  TYR E 239
SHEET    9  EB 9 LEU E 169  THR E 173  1  O  LEU E 170   N  PHE E 199
SHEET    1  EC 2 TYR E 353  ILE E 354  0
SHEET    2  EC 2 GLN E 366  ASP E 367 -1  O  GLN E 366   N  ILE E 354
SHEET    1  FA 4 THR F  54  MET F  55  0
SHEET    2  FA 4 HIS F  37  ASN F  43 -1  O  PHE F  42   N  THR F  54
SHEET    3  FA 4 PHE F  84  ASP F  91 -1  O  PHE F  84   N  ASN F  43
SHEET    4  FA 4 CYS F  96  TYR F 104 -1  O  CYS F  96   N  ASP F  91
SHEET    1  GA 5 CYS G  83  PRO G  89  0
SHEET    2  GA 5 PHE G  97  TYR G 103 -1  O  ILE G  98   N  GLU G  88
SHEET    3  GA 5 ILE G  36  PRO G  44 -1  O  ILE G  36   N  TYR G 103
SHEET    4  GA 5 LEU G 130  ARG G 139 -1  N  LYS G 131   O  THR G  43
SHEET    5  GA 5 GLY G 308  ILE G 309  1  O  GLY G 308   N  LEU G 135
SHEET    1  GB 9 LEU G 169  THR G 173  0
SHEET    2  GB 9 ALA G 398  PHE G 402  1  O  ALA G 398   N  LEU G 169
SHEET    3  GB 9 MET G 375  SER G 379  1  O  ALA G 376   N  VAL G 399
SHEET    4  GB 9 HIS G 325  HIS G 327  1  O  ILE G 326   N  VAL G 377
SHEET    5  GB 9 LEU G 290  HIS G 294  1  O  ILE G 293   N  HIS G 327
SHEET    6  GB 9 ILE G 264  ASP G 268  1  O  ILE G 265   N  HIS G 292
SHEET    7  GB 9 GLY G 237  ASN G 241  1  O  LEU G 240   N  MET G 266
SHEET    8  GB 9 PHE G 199  LYS G 201  1  O  THR G 200   N  TYR G 239
SHEET    9  GB 9 LEU G 169  THR G 173  1  O  LEU G 170   N  PHE G 199
SHEET    1  GC 2 TYR G 353  ILE G 354  0
SHEET    2  GC 2 GLN G 366  ASP G 367 -1  O  GLN G 366   N  ILE G 354
SHEET    1  HA 4 THR H  54  MET H  55  0
SHEET    2  HA 4 HIS H  37  ASN H  43 -1  O  PHE H  42   N  THR H  54
SHEET    3  HA 4 PHE H  84  ASP H  91 -1  O  PHE H  84   N  ASN H  43
SHEET    4  HA 4 CYS H  96  TYR H 104 -1  O  CYS H  96   N  ASP H  91
SHEET    1  IA 5 CYS I  83  PRO I  89  0
SHEET    2  IA 5 PHE I  97  TYR I 103 -1  O  ILE I  98   N  GLU I  88
SHEET    3  IA 5 ILE I  36  PRO I  44 -1  O  ILE I  36   N  TYR I 103
SHEET    4  IA 5 LEU I 130  ARG I 139 -1  N  LYS I 131   O  THR I  43
SHEET    5  IA 5 GLY I 308  ILE I 309  1  O  GLY I 308   N  LEU I 135
SHEET    1  IB 9 LEU I 169  THR I 173  0
SHEET    2  IB 9 ALA I 398  PHE I 402  1  O  ALA I 398   N  LEU I 169
SHEET    3  IB 9 MET I 375  SER I 379  1  O  ALA I 376   N  VAL I 399
SHEET    4  IB 9 HIS I 325  HIS I 327  1  O  ILE I 326   N  VAL I 377
SHEET    5  IB 9 LEU I 290  HIS I 294  1  O  ILE I 293   N  HIS I 327
SHEET    6  IB 9 ILE I 264  ASP I 268  1  O  ILE I 265   N  HIS I 292
SHEET    7  IB 9 GLY I 237  ASN I 241  1  O  LEU I 240   N  MET I 266
SHEET    8  IB 9 PHE I 199  LYS I 201  1  O  THR I 200   N  TYR I 239
SHEET    9  IB 9 LEU I 169  THR I 173  1  O  LEU I 170   N  PHE I 199
SHEET    1  IC 2 TYR I 353  ILE I 354  0
SHEET    2  IC 2 GLN I 366  ASP I 367 -1  O  GLN I 366   N  ILE I 354
SHEET    1  JA 4 THR J  54  MET J  55  0
SHEET    2  JA 4 HIS J  37  ASN J  43 -1  O  PHE J  42   N  THR J  54
SHEET    3  JA 4 PHE J  84  ASP J  91 -1  O  PHE J  84   N  ASN J  43
SHEET    4  JA 4 CYS J  96  TYR J 104 -1  O  CYS J  96   N  ASP J  91
SHEET    1  KA 5 CYS K  83  PRO K  89  0
SHEET    2  KA 5 PHE 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  LYS 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 9 LEU K 169  THR K 173  0
SHEET    2  KB 9 ALA K 398  PHE K 402  1  O  ALA K 398   N  LEU K 169
SHEET    3  KB 9 MET K 375  SER K 379  1  O  ALA K 376   N  VAL K 399
SHEET    4  KB 9 HIS K 325  HIS K 327  1  O  ILE K 326   N  VAL K 377
SHEET    5  KB 9 LEU K 290  HIS K 294  1  O  ILE K 293   N  HIS K 327
SHEET    6  KB 9 ILE K 264  ASP K 268  1  O  ILE K 265   N  HIS K 292
SHEET    7  KB 9 GLY K 237  ASN K 241  1  O  LEU K 240   N  MET K 266
SHEET    8  KB 9 PHE K 199  LYS K 201  1  O  THR K 200   N  TYR K 239
SHEET    9  KB 9 LEU K 169  THR K 173  1  O  CYS K 172   N  LYS K 201
SHEET    1  KC 2 TYR K 353  ILE K 354  0
SHEET    2  KC 2 GLN K 366  ASP K 367 -1  O  GLN K 366   N  ILE K 354
SHEET    1  LA 4 THR L  54  TRP L  56  0
SHEET    2  LA 4 HIS L  37  ASN L  43 -1  O  VAL L  40   N  TRP L  56
SHEET    3  LA 4 PHE L  84  ASP L  91 -1  O  PHE L  84   N  ASN L  43
SHEET    4  LA 4 CYS L  96  TYR L 104 -1  O  CYS L  96   N  ASP L  91
SHEET    1  MA 5 CYS M  83  PRO M  89  0
SHEET    2  MA 5 PHE M  97  TYR M 103 -1  O  ILE M  98   N  GLU M  88
SHEET    3  MA 5 ILE M  36  PRO M  44 -1  O  ILE M  36   N  TYR M 103
SHEET    4  MA 5 LEU M 130  ARG M 139 -1  N  LYS M 131   O  THR M  43
SHEET    5  MA 5 GLY M 308  ILE M 309  1  O  GLY M 308   N  LEU M 135
SHEET    1  MB 9 LEU M 169  THR M 173  0
SHEET    2  MB 9 ALA M 398  PHE M 402  1  O  ALA M 398   N  LEU M 169
SHEET    3  MB 9 MET M 375  SER M 379  1  O  ALA M 376   N  VAL M 399
SHEET    4  MB 9 HIS M 325  HIS M 327  1  O  ILE M 326   N  VAL M 377
SHEET    5  MB 9 LEU M 290  HIS M 294  1  O  ILE M 293   N  HIS M 327
SHEET    6  MB 9 ILE M 264  ASP M 268  1  O  ILE M 265   N  HIS M 292
SHEET    7  MB 9 GLY M 237  ASN M 241  1  O  LEU M 240   N  MET M 266
SHEET    8  MB 9 PHE M 199  LYS M 201  1  O  THR M 200   N  TYR M 239
SHEET    9  MB 9 LEU M 169  THR M 173  1  O  LEU M 170   N  PHE M 199
SHEET    1  MC 2 TYR M 353  ILE M 354  0
SHEET    2  MC 2 GLN M 366  ASP M 367 -1  O  GLN M 366   N  ILE M 354
SHEET    1  NA 4 THR N  54  MET N  55  0
SHEET    2  NA 4 HIS N  37  ASN N  43 -1  O  PHE N  42   N  THR N  54
SHEET    3  NA 4 PHE N  84  ASP N  91 -1  O  PHE N  84   N  ASN N  43
SHEET    4  NA 4 CYS N  96  TYR N 104 -1  O  CYS N  96   N  ASP N  91
SHEET    1  OA 5 CYS O  83  PRO O  89  0
SHEET    2  OA 5 PHE 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  LYS 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 9 LEU O 169  THR O 173  0
SHEET    2  OB 9 ALA O 398  PHE O 402  1  O  ALA O 398   N  LEU O 169
SHEET    3  OB 9 MET O 375  SER O 379  1  O  ALA O 376   N  VAL O 399
SHEET    4  OB 9 HIS O 325  HIS O 327  1  O  ILE O 326   N  VAL O 377
SHEET    5  OB 9 LEU O 290  HIS O 294  1  O  ILE O 293   N  HIS O 327
SHEET    6  OB 9 ILE O 264  ASP O 268  1  O  ILE O 265   N  HIS O 292
SHEET    7  OB 9 GLY O 237  ASN O 241  1  O  LEU O 240   N  MET O 266
SHEET    8  OB 9 PHE O 199  LYS O 201  1  O  THR O 200   N  TYR O 239
SHEET    9  OB 9 LEU O 169  THR O 173  1  O  LEU O 170   N  PHE O 199
SHEET    1  OC 2 TYR O 353  ILE O 354  0
SHEET    2  OC 2 GLN O 366  ASP O 367 -1  O  GLN O 366   N  ILE O 354
SHEET    1  PA 4 THR P  54  TRP P  56  0
SHEET    2  PA 4 HIS P  37  ASN P  43 -1  O  VAL P  40   N  TRP P  56
SHEET    3  PA 4 PHE P  84  ASP P  91 -1  O  PHE P  84   N  ASN P  43
SHEET    4  PA 4 CYS P  96  TYR P 104 -1  O  CYS P  96   N  ASP P  91
SSBOND   1 CYS A  172    CYS A  192                          1555   1555  2.19
SSBOND   2 CYS A  247    CYS I  247                          1555   1555  2.09
SSBOND   3 CYS C  172    CYS C  192                          1555   1555  2.15
SSBOND   4 CYS C  247    CYS K  247                          1555   1555  2.10
SSBOND   5 CYS E  172    CYS E  192                          1555   1555  2.17
SSBOND   6 CYS E  247    CYS M  247                          1555   1555  2.09
SSBOND   7 CYS G  172    CYS G  192                          1555   1555  2.21
SSBOND   8 CYS G  247    CYS O  247                          1555   1555  2.08
SSBOND   9 CYS I  172    CYS I  192                          1555   1555  2.12
SSBOND  10 CYS K  172    CYS K  192                          1555   1555  2.16
SSBOND  11 CYS M  172    CYS M  192                          1555   1555  2.16
SSBOND  12 CYS O  172    CYS O  192                          1555   1555  2.17
CISPEP   1 LYS A  175    PRO A  176          0         2.15
CISPEP   2 LYS C  175    PRO C  176          0        -0.44
CISPEP   3 LYS E  175    PRO E  176          0         3.34
CISPEP   4 LYS G  175    PRO G  176          0         3.35
CISPEP   5 LYS I  175    PRO I  176          0         3.86
CISPEP   6 LYS K  175    PRO K  176          0         3.91
CISPEP   7 LYS M  175    PRO M  176          0         3.61
CISPEP   8 LYS O  175    PRO O  176          0         1.72
SITE     1 AC1  2 LYS A 305  HIS A 310
SITE     1 AC2  1 ARG A 295
SITE     1 AC3  3 LYS C 305  HIS C 310  HOH C2099
SITE     1 AC4  1 ARG C 295
SITE     1 AC5  1 ARG E 295
SITE     1 AC6  2 LYS G 305  HIS G 310
SITE     1 AC7  1 ARG G 295
SITE     1 AC8  4 ARG I 134  LYS I 305  HIS I 310  HOH I2022
SITE     1 AC9  1 ARG I 295
SITE     1 BC1  2 LYS K 305  HIS K 310
SITE     1 BC2  1 ARG K 295
SITE     1 BC3  1 ARG M 295
SITE     1 BC4  2 LYS M 305  HIS M 310
SITE     1 BC5  3 ARG O 134  LYS O 305  HIS O 310
SITE     1 BC6  1 ARG O 295
CRYST1  115.480  163.470  163.540  90.00 108.96  90.00 P 1 21 1      8
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      0.008660  0.000000  0.002975        0.00000
SCALE2      0.000000  0.006117  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006465        0.00000
      
PROCHECK
Go to PROCHECK summary
 References