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PDBsum entry 2d69

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Lyase PDB id
2d69
Jmol
Contents
Protein chains
424 a.a.
Ligands
SO4 ×19
Waters ×750
HEADER    LYASE                                   10-NOV-05   2D69
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF SULFATE ION AND OCTAMERIC
TITLE    2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (RUBISCO) FROM
TITLE    3 PYROCOCCUS HORIKOSHII OT3 (FORM-2 CRYSTAL)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE;
COMPND   3 CHAIN: A, B, D, E;
COMPND   4 SYNONYM: RUBISCO, RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE;
COMPND   5 EC: 4.1.1.39;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE   3 ORGANISM_TAXID: 70601;
SOURCE   4 STRAIN: OT3;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS    ALPHA/BETA BARREL, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS   2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS   3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.MIZOHATA,C.MISHIMA,R.AKASAKA,H.UDA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,
AUTHOR   2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT   3   13-JUL-11 2D69    1       VERSN
REVDAT   2   24-FEB-09 2D69    1       VERSN
REVDAT   1   10-MAY-06 2D69    0
JRNL        AUTH   E.MIZOHATA,C.MISHIMA,R.AKASAKA,H.UDA,T.TERADA,M.SHIROUZU,
JRNL        AUTH 2 S.YOKOYAMA
JRNL        TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF SULFATE ION AND
JRNL        TITL 2 OCTAMERIC RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE
JRNL        TITL 3 (RUBISCO) FROM PYROCOCCUS HORIKOSHII OT3 (FORM-2 CRYSTAL)
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3
REMARK   3   NUMBER OF REFLECTIONS             : 154541
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) : 0.181
REMARK   3   R VALUE            (WORKING SET) : 0.180
REMARK   3   FREE R VALUE                     : 0.209
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 8084
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10454
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3120
REMARK   3   BIN FREE R VALUE SET COUNT          : 550
REMARK   3   BIN FREE R VALUE                    : 0.3230
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 13217
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 95
REMARK   3   SOLVENT ATOMS            : 750
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.43
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.91000
REMARK   3    B22 (A**2) : -1.49000
REMARK   3    B33 (A**2) : 2.57000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 1.67000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.134
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.124
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.102
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.747
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13609 ; 0.020 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A): 12486 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18393 ; 1.662 ; 1.966
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 28987 ; 0.896 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1667 ; 6.692 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1941 ; 0.109 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15055 ; 0.009 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  2835 ; 0.008 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2811 ; 0.212 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 14430 ; 0.243 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  7824 ; 0.088 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   597 ; 0.160 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    47 ; 0.182 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):   276 ; 0.293 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    26 ; 0.136 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8277 ; 0.910 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13260 ; 1.604 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5332 ; 2.578 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5133 ; 4.066 ; 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 : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 4
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     1        A   424
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3950  -0.4684  35.8628
REMARK   3    T TENSOR
REMARK   3      T11:   0.0853 T22:   0.1920
REMARK   3      T33:   0.1342 T12:   0.0615
REMARK   3      T13:  -0.0334 T23:  -0.0106
REMARK   3    L TENSOR
REMARK   3      L11:   0.5214 L22:   0.7802
REMARK   3      L33:   0.4238 L12:  -0.1016
REMARK   3      L13:  -0.1899 L23:   0.1735
REMARK   3    S TENSOR
REMARK   3      S11:   0.0073 S12:   0.0503 S13:  -0.0964
REMARK   3      S21:  -0.0331 S22:  -0.0261 S23:   0.2410
REMARK   3      S31:  -0.0912 S32:  -0.1161 S33:   0.0187
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     8        B   425
REMARK   3    ORIGIN FOR THE GROUP (A):  51.6478 -30.8985  56.9439
REMARK   3    T TENSOR
REMARK   3      T11:   0.1100 T22:   0.1039
REMARK   3      T33:   0.1731 T12:  -0.0246
REMARK   3      T13:  -0.0139 T23:   0.0297
REMARK   3    L TENSOR
REMARK   3      L11:   0.7973 L22:   0.3979
REMARK   3      L33:   0.6928 L12:   0.0908
REMARK   3      L13:  -0.0815 L23:   0.0177
REMARK   3    S TENSOR
REMARK   3      S11:   0.0502 S12:  -0.0675 S13:  -0.1938
REMARK   3      S21:   0.0521 S22:  -0.0580 S23:  -0.0099
REMARK   3      S31:   0.0863 S32:  -0.0233 S33:   0.0078
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D     1        D   419
REMARK   3    ORIGIN FOR THE GROUP (A):  43.6481  40.2282  50.9756
REMARK   3    T TENSOR
REMARK   3      T11:   0.2686 T22:   0.0853
REMARK   3      T33:   0.1064 T12:   0.0273
REMARK   3      T13:   0.0617 T23:  -0.0421
REMARK   3    L TENSOR
REMARK   3      L11:   0.6284 L22:   0.5070
REMARK   3      L33:   1.0769 L12:  -0.0023
REMARK   3      L13:   0.1854 L23:  -0.1046
REMARK   3    S TENSOR
REMARK   3      S11:   0.0351 S12:  -0.0938 S13:   0.2259
REMARK   3      S21:   0.0593 S22:  -0.0546 S23:   0.0595
REMARK   3      S31:  -0.2897 S32:  -0.0838 S33:   0.0195
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E     9        E   418
REMARK   3    ORIGIN FOR THE GROUP (A):  29.9269   9.5152  15.0650
REMARK   3    T TENSOR
REMARK   3      T11:   0.1783 T22:   0.2137
REMARK   3      T33:   0.0339 T12:   0.0736
REMARK   3      T13:  -0.0581 T23:  -0.0162
REMARK   3    L TENSOR
REMARK   3      L11:   0.8648 L22:   0.9957
REMARK   3      L33:   0.5092 L12:  -0.1732
REMARK   3      L13:  -0.2181 L23:   0.0966
REMARK   3    S TENSOR
REMARK   3      S11:   0.0564 S12:   0.2352 S13:  -0.0389
REMARK   3      S21:  -0.2152 S22:  -0.0495 S23:   0.1468
REMARK   3      S31:  -0.1137 S32:  -0.1208 S33:  -0.0069
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 2D69 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-NOV-05.
REMARK 100 THE RCSB ID CODE IS RCSB025038.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL26B1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS V
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 162742
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ID: 2CWX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM BICARBONATE,
REMARK 280  MAGNESIUM CHLORIDE, SODIUM ACETATE, 2CABP, TRIS-HCL , PH 5, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
REMARK 290       4555   -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       86.29550
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       74.38700
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       86.29550
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       74.38700
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE OCTAMER. BIOLOGICAL ASSEMBLY
REMARK 300 (SEGID A, B, C, D, E, F, G, H) IS GENERATED FROM THE ASYMMETRIC
REMARK 300 COMPONENT (A, B, D, E) BY OPERATOR -X+1, Y, -Z+1. (A, B, D, E) ->
REMARK 300 (G, F, H, C)
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: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      108.09650
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       87.19114
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 30660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 86150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -571.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      108.09650
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       87.19114
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      108.09650
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       87.19114
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH D3177  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B2186  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B2181  LIES ON A SPECIAL POSITION.
REMARK 375      HOH D3175  LIES ON A SPECIAL POSITION.
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     LYS A   425
REMARK 465     VAL A   426
REMARK 465     GLY A   427
REMARK 465     VAL A   428
REMARK 465     GLN A   429
REMARK 465     HIS A   430
REMARK 465     MET B     1
REMARK 465     MET B     2
REMARK 465     VAL B     3
REMARK 465     LEU B     4
REMARK 465     ARG B     5
REMARK 465     MET B     6
REMARK 465     LYS B     7
REMARK 465     VAL B   426
REMARK 465     GLY B   427
REMARK 465     VAL B   428
REMARK 465     GLN B   429
REMARK 465     HIS B   430
REMARK 465     GLY D   420
REMARK 465     LEU D   421
REMARK 465     SER D   422
REMARK 465     LYS D   423
REMARK 465     ALA D   424
REMARK 465     LYS D   425
REMARK 465     VAL D   426
REMARK 465     GLY D   427
REMARK 465     VAL D   428
REMARK 465     GLN D   429
REMARK 465     HIS D   430
REMARK 465     MET E     1
REMARK 465     MET E     2
REMARK 465     VAL E     3
REMARK 465     LEU E     4
REMARK 465     ARG E     5
REMARK 465     MET E     6
REMARK 465     LYS E     7
REMARK 465     VAL E     8
REMARK 465     VAL E   419
REMARK 465     GLY E   420
REMARK 465     LEU E   421
REMARK 465     SER E   422
REMARK 465     LYS E   423
REMARK 465     ALA E   424
REMARK 465     LYS E   425
REMARK 465     VAL E   426
REMARK 465     GLY E   427
REMARK 465     VAL E   428
REMARK 465     GLN E   429
REMARK 465     HIS E   430
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ALA A 424    O
REMARK 470     LYS B 425    O
REMARK 470     VAL D 419    O
REMARK 470     GLU E 418    O
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   OH   TYR B   323     O    HOH B  2101              2.00
REMARK 500   OD2  ASP E   391     OG   SER E   409              2.02
REMARK 500   OD1  ASP E   270     O    HOH E  4105              2.05
REMARK 500   O    GLY E   313     O    HOH E  4128              2.07
REMARK 500   OH   TYR E   248     NE2  GLN E   309              2.14
REMARK 500   O    GLU B    63     O    HOH B  2084              2.18
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    VAL E 231   CB    VAL E 231   CG2    -0.135
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A 331   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    LEU B 261   CB  -  CG  -  CD2 ANGL. DEV. =  12.4 DEGREES
REMARK 500    ASP B 331   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES
REMARK 500    ASP D  16   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP D 151   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ASP D 211   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    LEU D 261   CB  -  CG  -  CD2 ANGL. DEV. =  10.7 DEGREES
REMARK 500    ASP D 308   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP D 331   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP D 366   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP D 380   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES
REMARK 500    ASP D 391   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP E  16   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP E 211   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP E 308   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP E 380   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  51     -109.20   -131.63
REMARK 500    ALA A 106       33.62   -140.57
REMARK 500    ASP A 151      -47.41   -130.34
REMARK 500    THR A 192      -78.51   -110.32
REMARK 500    MET A 281      -14.86     90.24
REMARK 500    MET A 319      -11.32   -165.89
REMARK 500    ALA A 320      103.57    -19.65
REMARK 500    TRP A 337       78.83   -152.88
REMARK 500    GLU A 338     -131.01     49.11
REMARK 500    ASP B  16       82.73   -161.26
REMARK 500    SER B  51     -104.09   -132.42
REMARK 500    THR B 192      -83.13   -103.38
REMARK 500    ASN B 197       78.57   -151.80
REMARK 500    MET B 281      -18.13     88.20
REMARK 500    MET B 319     -112.33    -77.69
REMARK 500    ALA B 320      117.62     75.37
REMARK 500    TRP B 337       82.82   -151.47
REMARK 500    GLU B 338     -126.78     50.95
REMARK 500    ALA B 371       58.65   -141.95
REMARK 500    GLU D   9       45.35   -109.37
REMARK 500    SER D  51     -109.67   -130.11
REMARK 500    TRP D  55       30.45   -149.92
REMARK 500    ASP D 151      -55.65   -126.43
REMARK 500    THR D 192      -75.53   -102.39
REMARK 500    MET D 281      -18.15     90.60
REMARK 500    LYS D 318      -70.10   -104.45
REMARK 500    MET D 319     -131.75    -67.45
REMARK 500    ALA D 320      124.16     90.99
REMARK 500    GLU D 338     -130.16     45.63
REMARK 500    ALA D 371       44.51   -147.89
REMARK 500    ASP E  16       89.20   -155.54
REMARK 500    SER E  51     -107.65   -134.98
REMARK 500    TRP E  55     -166.54   -129.13
REMARK 500    THR E  56      117.41    108.05
REMARK 500    THR E  57      137.14    156.61
REMARK 500    LYS E  77      135.60    -37.58
REMARK 500    ASP E 151      -49.22   -139.90
REMARK 500    THR E 192      -77.04   -107.33
REMARK 500    ASN E 197       74.89   -152.92
REMARK 500    MET E 281      -22.19     88.38
REMARK 500    MET E 319     -129.54    -77.94
REMARK 500    ALA E 320      117.46     93.78
REMARK 500    TRP E 337       77.99   -153.62
REMARK 500    GLU E 338     -129.40     50.14
REMARK 500    ALA E 371       46.70   -146.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 THR E   56     THR E   57                 -145.87
REMARK 500 ALA E  315     VAL E  316                 -141.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A1182        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH A1186        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH A1211        DISTANCE =  5.77 ANGSTROMS
REMARK 525    HOH A1215        DISTANCE =  5.52 ANGSTROMS
REMARK 525    HOH A1225        DISTANCE =  6.65 ANGSTROMS
REMARK 525    HOH B2109        DISTANCE =  7.63 ANGSTROMS
REMARK 525    HOH B2128        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH B2173        DISTANCE =  5.80 ANGSTROMS
REMARK 525    HOH D3119        DISTANCE =  6.97 ANGSTROMS
REMARK 525    HOH E4139        DISTANCE =  6.83 ANGSTROMS
REMARK 525    HOH E4160        DISTANCE =  5.89 ANGSTROMS
REMARK 525    HOH E4168        DISTANCE =  6.98 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4004
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 4005
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CWX   RELATED DB: PDB
REMARK 900 RELATED ID: PHO001000939.3   RELATED DB: TARGETDB
DBREF  2D69 A    1   430  UNP    O58677   RBL_PYRHO        1    430
DBREF  2D69 B    1   430  UNP    O58677   RBL_PYRHO        1    430
DBREF  2D69 D    1   430  UNP    O58677   RBL_PYRHO        1    430
DBREF  2D69 E    1   430  UNP    O58677   RBL_PYRHO        1    430
SEQRES   1 A  430  MET MET VAL LEU ARG MET LYS VAL GLU TRP TYR LEU ASP
SEQRES   2 A  430  PHE VAL ASP LEU ASN TYR GLU PRO GLY ARG ASP GLU LEU
SEQRES   3 A  430  ILE VAL GLU TYR TYR PHE GLU PRO ASN GLY VAL SER PRO
SEQRES   4 A  430  GLU GLU ALA ALA GLY ARG ILE ALA SER GLU SER SER ILE
SEQRES   5 A  430  GLY THR TRP THR THR LEU TRP LYS LEU PRO GLU MET ALA
SEQRES   6 A  430  LYS ARG SER MET ALA LYS VAL PHE TYR LEU GLU LYS HIS
SEQRES   7 A  430  GLY GLU GLY TYR ILE ALA LYS ILE ALA TYR PRO LEU THR
SEQRES   8 A  430  LEU PHE GLU GLU GLY SER LEU VAL GLN LEU PHE SER ALA
SEQRES   9 A  430  VAL ALA GLY ASN VAL PHE GLY MET LYS ALA LEU LYS ASN
SEQRES  10 A  430  LEU ARG LEU LEU ASP PHE HIS PRO PRO TYR GLU TYR LEU
SEQRES  11 A  430  ARG HIS PHE LYS GLY PRO GLN PHE GLY VAL GLN GLY ILE
SEQRES  12 A  430  ARG GLU PHE MET GLY VAL LYS ASP ARG PRO LEU THR ALA
SEQRES  13 A  430  THR VAL PRO LYS PRO LYS MET GLY TRP SER VAL GLU GLU
SEQRES  14 A  430  TYR ALA GLU ILE ALA TYR GLU LEU TRP SER GLY GLY ILE
SEQRES  15 A  430  ASP LEU LEU LYS ASP ASP GLU ASN PHE THR SER PHE PRO
SEQRES  16 A  430  PHE ASN ARG PHE GLU GLU ARG VAL ARG LYS LEU TYR ARG
SEQRES  17 A  430  VAL ARG ASP ARG VAL GLU ALA GLU THR GLY GLU THR LYS
SEQRES  18 A  430  GLU TYR LEU ILE ASN ILE THR GLY PRO VAL ASN ILE MET
SEQRES  19 A  430  GLU LYS ARG ALA GLU MET VAL ALA ASN GLU GLY GLY GLN
SEQRES  20 A  430  TYR VAL MET ILE ASP ILE VAL VAL ALA GLY TRP SER ALA
SEQRES  21 A  430  LEU GLN TYR MET ARG GLU VAL THR GLU ASP LEU GLY LEU
SEQRES  22 A  430  ALA ILE HIS ALA HIS ARG ALA MET HIS ALA ALA PHE THR
SEQRES  23 A  430  ARG ASN PRO ARG HIS GLY ILE THR MET LEU ALA LEU ALA
SEQRES  24 A  430  LYS ALA ALA ARG MET ILE GLY VAL ASP GLN ILE HIS THR
SEQRES  25 A  430  GLY THR ALA VAL GLY LYS MET ALA GLY ASN TYR GLU GLU
SEQRES  26 A  430  ILE LYS ARG ILE ASN ASP PHE LEU LEU SER LYS TRP GLU
SEQRES  27 A  430  HIS ILE ARG PRO VAL PHE PRO VAL ALA SER GLY GLY LEU
SEQRES  28 A  430  HIS PRO GLY LEU MET PRO GLU LEU ILE ARG LEU PHE GLY
SEQRES  29 A  430  LYS ASP LEU VAL ILE GLN ALA GLY GLY GLY VAL MET GLY
SEQRES  30 A  430  HIS PRO ASP GLY PRO ARG ALA GLY ALA LYS ALA LEU ARG
SEQRES  31 A  430  ASP ALA ILE ASP ALA ALA ILE GLU GLY VAL ASP LEU ASP
SEQRES  32 A  430  GLU LYS ALA LYS SER SER PRO GLU LEU LYS LYS SER LEU
SEQRES  33 A  430  ARG GLU VAL GLY LEU SER LYS ALA LYS VAL GLY VAL GLN
SEQRES  34 A  430  HIS
SEQRES   1 B  430  MET MET VAL LEU ARG MET LYS VAL GLU TRP TYR LEU ASP
SEQRES   2 B  430  PHE VAL ASP LEU ASN TYR GLU PRO GLY ARG ASP GLU LEU
SEQRES   3 B  430  ILE VAL GLU TYR TYR PHE GLU PRO ASN GLY VAL SER PRO
SEQRES   4 B  430  GLU GLU ALA ALA GLY ARG ILE ALA SER GLU SER SER ILE
SEQRES   5 B  430  GLY THR TRP THR THR LEU TRP LYS LEU PRO GLU MET ALA
SEQRES   6 B  430  LYS ARG SER MET ALA LYS VAL PHE TYR LEU GLU LYS HIS
SEQRES   7 B  430  GLY GLU GLY TYR ILE ALA LYS ILE ALA TYR PRO LEU THR
SEQRES   8 B  430  LEU PHE GLU GLU GLY SER LEU VAL GLN LEU PHE SER ALA
SEQRES   9 B  430  VAL ALA GLY ASN VAL PHE GLY MET LYS ALA LEU LYS ASN
SEQRES  10 B  430  LEU ARG LEU LEU ASP PHE HIS PRO PRO TYR GLU TYR LEU
SEQRES  11 B  430  ARG HIS PHE LYS GLY PRO GLN PHE GLY VAL GLN GLY ILE
SEQRES  12 B  430  ARG GLU PHE MET GLY VAL LYS ASP ARG PRO LEU THR ALA
SEQRES  13 B  430  THR VAL PRO LYS PRO LYS MET GLY TRP SER VAL GLU GLU
SEQRES  14 B  430  TYR ALA GLU ILE ALA TYR GLU LEU TRP SER GLY GLY ILE
SEQRES  15 B  430  ASP LEU LEU LYS ASP ASP GLU ASN PHE THR SER PHE PRO
SEQRES  16 B  430  PHE ASN ARG PHE GLU GLU ARG VAL ARG LYS LEU TYR ARG
SEQRES  17 B  430  VAL ARG ASP ARG VAL GLU ALA GLU THR GLY GLU THR LYS
SEQRES  18 B  430  GLU TYR LEU ILE ASN ILE THR GLY PRO VAL ASN ILE MET
SEQRES  19 B  430  GLU LYS ARG ALA GLU MET VAL ALA ASN GLU GLY GLY GLN
SEQRES  20 B  430  TYR VAL MET ILE ASP ILE VAL VAL ALA GLY TRP SER ALA
SEQRES  21 B  430  LEU GLN TYR MET ARG GLU VAL THR GLU ASP LEU GLY LEU
SEQRES  22 B  430  ALA ILE HIS ALA HIS ARG ALA MET HIS ALA ALA PHE THR
SEQRES  23 B  430  ARG ASN PRO ARG HIS GLY ILE THR MET LEU ALA LEU ALA
SEQRES  24 B  430  LYS ALA ALA ARG MET ILE GLY VAL ASP GLN ILE HIS THR
SEQRES  25 B  430  GLY THR ALA VAL GLY LYS MET ALA GLY ASN TYR GLU GLU
SEQRES  26 B  430  ILE LYS ARG ILE ASN ASP PHE LEU LEU SER LYS TRP GLU
SEQRES  27 B  430  HIS ILE ARG PRO VAL PHE PRO VAL ALA SER GLY GLY LEU
SEQRES  28 B  430  HIS PRO GLY LEU MET PRO GLU LEU ILE ARG LEU PHE GLY
SEQRES  29 B  430  LYS ASP LEU VAL ILE GLN ALA GLY GLY GLY VAL MET GLY
SEQRES  30 B  430  HIS PRO ASP GLY PRO ARG ALA GLY ALA LYS ALA LEU ARG
SEQRES  31 B  430  ASP ALA ILE ASP ALA ALA ILE GLU GLY VAL ASP LEU ASP
SEQRES  32 B  430  GLU LYS ALA LYS SER SER PRO GLU LEU LYS LYS SER LEU
SEQRES  33 B  430  ARG GLU VAL GLY LEU SER LYS ALA LYS VAL GLY VAL GLN
SEQRES  34 B  430  HIS
SEQRES   1 D  430  MET MET VAL LEU ARG MET LYS VAL GLU TRP TYR LEU ASP
SEQRES   2 D  430  PHE VAL ASP LEU ASN TYR GLU PRO GLY ARG ASP GLU LEU
SEQRES   3 D  430  ILE VAL GLU TYR TYR PHE GLU PRO ASN GLY VAL SER PRO
SEQRES   4 D  430  GLU GLU ALA ALA GLY ARG ILE ALA SER GLU SER SER ILE
SEQRES   5 D  430  GLY THR TRP THR THR LEU TRP LYS LEU PRO GLU MET ALA
SEQRES   6 D  430  LYS ARG SER MET ALA LYS VAL PHE TYR LEU GLU LYS HIS
SEQRES   7 D  430  GLY GLU GLY TYR ILE ALA LYS ILE ALA TYR PRO LEU THR
SEQRES   8 D  430  LEU PHE GLU GLU GLY SER LEU VAL GLN LEU PHE SER ALA
SEQRES   9 D  430  VAL ALA GLY ASN VAL PHE GLY MET LYS ALA LEU LYS ASN
SEQRES  10 D  430  LEU ARG LEU LEU ASP PHE HIS PRO PRO TYR GLU TYR LEU
SEQRES  11 D  430  ARG HIS PHE LYS GLY PRO GLN PHE GLY VAL GLN GLY ILE
SEQRES  12 D  430  ARG GLU PHE MET GLY VAL LYS ASP ARG PRO LEU THR ALA
SEQRES  13 D  430  THR VAL PRO LYS PRO LYS MET GLY TRP SER VAL GLU GLU
SEQRES  14 D  430  TYR ALA GLU ILE ALA TYR GLU LEU TRP SER GLY GLY ILE
SEQRES  15 D  430  ASP LEU LEU LYS ASP ASP GLU ASN PHE THR SER PHE PRO
SEQRES  16 D  430  PHE ASN ARG PHE GLU GLU ARG VAL ARG LYS LEU TYR ARG
SEQRES  17 D  430  VAL ARG ASP ARG VAL GLU ALA GLU THR GLY GLU THR LYS
SEQRES  18 D  430  GLU TYR LEU ILE ASN ILE THR GLY PRO VAL ASN ILE MET
SEQRES  19 D  430  GLU LYS ARG ALA GLU MET VAL ALA ASN GLU GLY GLY GLN
SEQRES  20 D  430  TYR VAL MET ILE ASP ILE VAL VAL ALA GLY TRP SER ALA
SEQRES  21 D  430  LEU GLN TYR MET ARG GLU VAL THR GLU ASP LEU GLY LEU
SEQRES  22 D  430  ALA ILE HIS ALA HIS ARG ALA MET HIS ALA ALA PHE THR
SEQRES  23 D  430  ARG ASN PRO ARG HIS GLY ILE THR MET LEU ALA LEU ALA
SEQRES  24 D  430  LYS ALA ALA ARG MET ILE GLY VAL ASP GLN ILE HIS THR
SEQRES  25 D  430  GLY THR ALA VAL GLY LYS MET ALA GLY ASN TYR GLU GLU
SEQRES  26 D  430  ILE LYS ARG ILE ASN ASP PHE LEU LEU SER LYS TRP GLU
SEQRES  27 D  430  HIS ILE ARG PRO VAL PHE PRO VAL ALA SER GLY GLY LEU
SEQRES  28 D  430  HIS PRO GLY LEU MET PRO GLU LEU ILE ARG LEU PHE GLY
SEQRES  29 D  430  LYS ASP LEU VAL ILE GLN ALA GLY GLY GLY VAL MET GLY
SEQRES  30 D  430  HIS PRO ASP GLY PRO ARG ALA GLY ALA LYS ALA LEU ARG
SEQRES  31 D  430  ASP ALA ILE ASP ALA ALA ILE GLU GLY VAL ASP LEU ASP
SEQRES  32 D  430  GLU LYS ALA LYS SER SER PRO GLU LEU LYS LYS SER LEU
SEQRES  33 D  430  ARG GLU VAL GLY LEU SER LYS ALA LYS VAL GLY VAL GLN
SEQRES  34 D  430  HIS
SEQRES   1 E  430  MET MET VAL LEU ARG MET LYS VAL GLU TRP TYR LEU ASP
SEQRES   2 E  430  PHE VAL ASP LEU ASN TYR GLU PRO GLY ARG ASP GLU LEU
SEQRES   3 E  430  ILE VAL GLU TYR TYR PHE GLU PRO ASN GLY VAL SER PRO
SEQRES   4 E  430  GLU GLU ALA ALA GLY ARG ILE ALA SER GLU SER SER ILE
SEQRES   5 E  430  GLY THR TRP THR THR LEU TRP LYS LEU PRO GLU MET ALA
SEQRES   6 E  430  LYS ARG SER MET ALA LYS VAL PHE TYR LEU GLU LYS HIS
SEQRES   7 E  430  GLY GLU GLY TYR ILE ALA LYS ILE ALA TYR PRO LEU THR
SEQRES   8 E  430  LEU PHE GLU GLU GLY SER LEU VAL GLN LEU PHE SER ALA
SEQRES   9 E  430  VAL ALA GLY ASN VAL PHE GLY MET LYS ALA LEU LYS ASN
SEQRES  10 E  430  LEU ARG LEU LEU ASP PHE HIS PRO PRO TYR GLU TYR LEU
SEQRES  11 E  430  ARG HIS PHE LYS GLY PRO GLN PHE GLY VAL GLN GLY ILE
SEQRES  12 E  430  ARG GLU PHE MET GLY VAL LYS ASP ARG PRO LEU THR ALA
SEQRES  13 E  430  THR VAL PRO LYS PRO LYS MET GLY TRP SER VAL GLU GLU
SEQRES  14 E  430  TYR ALA GLU ILE ALA TYR GLU LEU TRP SER GLY GLY ILE
SEQRES  15 E  430  ASP LEU LEU LYS ASP ASP GLU ASN PHE THR SER PHE PRO
SEQRES  16 E  430  PHE ASN ARG PHE GLU GLU ARG VAL ARG LYS LEU TYR ARG
SEQRES  17 E  430  VAL ARG ASP ARG VAL GLU ALA GLU THR GLY GLU THR LYS
SEQRES  18 E  430  GLU TYR LEU ILE ASN ILE THR GLY PRO VAL ASN ILE MET
SEQRES  19 E  430  GLU LYS ARG ALA GLU MET VAL ALA ASN GLU GLY GLY GLN
SEQRES  20 E  430  TYR VAL MET ILE ASP ILE VAL VAL ALA GLY TRP SER ALA
SEQRES  21 E  430  LEU GLN TYR MET ARG GLU VAL THR GLU ASP LEU GLY LEU
SEQRES  22 E  430  ALA ILE HIS ALA HIS ARG ALA MET HIS ALA ALA PHE THR
SEQRES  23 E  430  ARG ASN PRO ARG HIS GLY ILE THR MET LEU ALA LEU ALA
SEQRES  24 E  430  LYS ALA ALA ARG MET ILE GLY VAL ASP GLN ILE HIS THR
SEQRES  25 E  430  GLY THR ALA VAL GLY LYS MET ALA GLY ASN TYR GLU GLU
SEQRES  26 E  430  ILE LYS ARG ILE ASN ASP PHE LEU LEU SER LYS TRP GLU
SEQRES  27 E  430  HIS ILE ARG PRO VAL PHE PRO VAL ALA SER GLY GLY LEU
SEQRES  28 E  430  HIS PRO GLY LEU MET PRO GLU LEU ILE ARG LEU PHE GLY
SEQRES  29 E  430  LYS ASP LEU VAL ILE GLN ALA GLY GLY GLY VAL MET GLY
SEQRES  30 E  430  HIS PRO ASP GLY PRO ARG ALA GLY ALA LYS ALA LEU ARG
SEQRES  31 E  430  ASP ALA ILE ASP ALA ALA ILE GLU GLY VAL ASP LEU ASP
SEQRES  32 E  430  GLU LYS ALA LYS SER SER PRO GLU LEU LYS LYS SER LEU
SEQRES  33 E  430  ARG GLU VAL GLY LEU SER LYS ALA LYS VAL GLY VAL GLN
SEQRES  34 E  430  HIS
HET    SO4  A1001       5
HET    SO4  A1002       5
HET    SO4  A1003       5
HET    SO4  A1004       5
HET    SO4  A1005       5
HET    SO4  B2001       5
HET    SO4  B2002       5
HET    SO4  B2003       5
HET    SO4  B2004       5
HET    SO4  B2005       5
HET    SO4  D3001       5
HET    SO4  D3002       5
HET    SO4  D3003       5
HET    SO4  D3004       5
HET    SO4  E4001       5
HET    SO4  E4002       5
HET    SO4  E4003       5
HET    SO4  E4004       5
HET    SO4  E4005       5
HETNAM     SO4 SULFATE ION
FORMUL   5  SO4    19(O4 S 2-)
FORMUL  24  HOH   *750(H2 O)
HELIX    1   1 TRP A   10  VAL A   15  5                                   6
HELIX    2   2 SER A   38  SER A   50  1                                  13
HELIX    3   3 ALA A   65  MET A   69  5                                   5
HELIX    4   4 PRO A   89  PHE A   93  5                                   5
HELIX    5   5 SER A   97  ALA A  106  1                                  10
HELIX    6   6 GLY A  107  MET A  112  5                                   6
HELIX    7   7 PRO A  126  ARG A  131  1                                   6
HELIX    8   8 PHE A  138  GLY A  148  1                                  11
HELIX    9   9 SER A  166  GLY A  180  1                                  15
HELIX   10  10 ARG A  198  GLY A  218  1                                  21
HELIX   11  11 PRO A  230  GLU A  244  1                                  15
HELIX   12  12 ILE A  253  GLY A  257  1                                   5
HELIX   13  13 GLY A  257  GLY A  272  1                                  16
HELIX   14  14 HIS A  282  ARG A  287  1                                   6
HELIX   15  15 THR A  294  GLY A  306  1                                  13
HELIX   16  16 ASN A  322  SER A  335  1                                  14
HELIX   17  17 HIS A  352  GLY A  354  5                                   3
HELIX   18  18 LEU A  355  GLY A  364  1                                  10
HELIX   19  19 ALA A  371  GLY A  377  1                                   7
HELIX   20  20 GLY A  381  GLY A  399  1                                  19
HELIX   21  21 ASP A  401  ALA A  406  1                                   6
HELIX   22  22 SER A  409  LYS A  423  1                                  15
HELIX   23  23 TRP B   10  VAL B   15  5                                   6
HELIX   24  24 SER B   38  SER B   50  1                                  13
HELIX   25  25 ALA B   65  MET B   69  5                                   5
HELIX   26  26 PRO B   89  PHE B   93  5                                   5
HELIX   27  27 SER B   97  ALA B  106  1                                  10
HELIX   28  28 GLY B  107  MET B  112  5                                   6
HELIX   29  29 PRO B  126  ARG B  131  1                                   6
HELIX   30  30 PHE B  138  GLY B  148  1                                  11
HELIX   31  31 SER B  166  GLY B  181  1                                  16
HELIX   32  32 ARG B  198  GLY B  218  1                                  21
HELIX   33  33 PRO B  230  GLU B  244  1                                  15
HELIX   34  34 ILE B  253  GLY B  257  1                                   5
HELIX   35  35 GLY B  257  GLY B  272  1                                  16
HELIX   36  36 HIS B  282  ARG B  287  1                                   6
HELIX   37  37 THR B  294  GLY B  306  1                                  13
HELIX   38  38 ASN B  322  SER B  335  1                                  14
HELIX   39  39 HIS B  352  GLY B  354  5                                   3
HELIX   40  40 LEU B  355  GLY B  364  1                                  10
HELIX   41  41 ALA B  371  GLY B  377  1                                   7
HELIX   42  42 GLY B  381  GLY B  399  1                                  19
HELIX   43  43 ASP B  401  LYS B  407  1                                   7
HELIX   44  44 SER B  409  LYS B  423  1                                  15
HELIX   45  45 GLU D    9  VAL D   15  5                                   7
HELIX   46  46 SER D   38  SER D   50  1                                  13
HELIX   47  47 ALA D   65  MET D   69  5                                   5
HELIX   48  48 THR D   91  PHE D   93  5                                   3
HELIX   49  49 SER D   97  ALA D  106  1                                  10
HELIX   50  50 GLY D  107  MET D  112  5                                   6
HELIX   51  51 PRO D  126  ARG D  131  1                                   6
HELIX   52  52 PHE D  138  GLY D  148  1                                  11
HELIX   53  53 SER D  166  GLY D  181  1                                  16
HELIX   54  54 ARG D  198  GLY D  218  1                                  21
HELIX   55  55 PRO D  230  GLU D  244  1                                  15
HELIX   56  56 ILE D  253  GLY D  257  1                                   5
HELIX   57  57 GLY D  257  GLY D  272  1                                  16
HELIX   58  58 HIS D  282  ARG D  287  1                                   6
HELIX   59  59 THR D  294  GLY D  306  1                                  13
HELIX   60  60 ASN D  322  SER D  335  1                                  14
HELIX   61  61 HIS D  352  GLY D  354  5                                   3
HELIX   62  62 LEU D  355  GLY D  364  1                                  10
HELIX   63  63 ALA D  371  HIS D  378  1                                   8
HELIX   64  64 GLY D  381  GLU D  398  1                                  18
HELIX   65  65 ASP D  401  LYS D  407  1                                   7
HELIX   66  66 SER D  409  VAL D  419  1                                  11
HELIX   67  67 TRP E   10  VAL E   15  5                                   6
HELIX   68  68 SER E   38  SER E   50  1                                  13
HELIX   69  69 ALA E   65  MET E   69  5                                   5
HELIX   70  70 THR E   91  PHE E   93  5                                   3
HELIX   71  71 SER E   97  ALA E  106  1                                  10
HELIX   72  72 GLY E  107  MET E  112  5                                   6
HELIX   73  73 PRO E  126  ARG E  131  1                                   6
HELIX   74  74 PHE E  138  GLY E  148  1                                  11
HELIX   75  75 SER E  166  GLY E  181  1                                  16
HELIX   76  76 ARG E  198  GLY E  218  1                                  21
HELIX   77  77 PRO E  230  GLU E  244  1                                  15
HELIX   78  78 ILE E  253  GLY E  257  1                                   5
HELIX   79  79 GLY E  257  GLY E  272  1                                  16
HELIX   80  80 HIS E  282  ARG E  287  1                                   6
HELIX   81  81 THR E  294  GLY E  306  1                                  13
HELIX   82  82 ASN E  322  SER E  335  1                                  14
HELIX   83  83 HIS E  352  GLY E  354  5                                   3
HELIX   84  84 LEU E  355  GLY E  364  1                                  10
HELIX   85  85 ALA E  371  HIS E  378  1                                   8
HELIX   86  86 GLY E  381  GLY E  399  1                                  19
HELIX   87  87 ASP E  401  ALA E  406  1                                   6
HELIX   88  88 SER E  409  GLU E  418  1                                  10
SHEET    1   A 2 LYS A   7  GLU A   9  0
SHEET    2   A 2 TRP A  55  THR A  57 -1  O  THR A  57   N  LYS A   7
SHEET    1   B 5 LYS A  71  HIS A  78  0
SHEET    2   B 5 GLY A  81  TYR A  88 -1  O  ILE A  83   N  GLU A  76
SHEET    3   B 5 LEU A  26  PRO A  34 -1  N  LEU A  26   O  TYR A  88
SHEET    4   B 5 LEU A 115  HIS A 124 -1  O  LYS A 116   N  GLU A  33
SHEET    5   B 5 GLY A 292  ILE A 293  1  O  GLY A 292   N  LEU A 120
SHEET    1   C 8 GLU A 222  LEU A 224  0
SHEET    2   C 8 LEU A 184  LYS A 186  1  N  LEU A 185   O  LEU A 224
SHEET    3   C 8 LEU A 154  THR A 157  1  N  THR A 155   O  LEU A 184
SHEET    4   C 8 VAL A 368  GLN A 370  1  O  ILE A 369   N  LEU A 154
SHEET    5   C 8 PHE A 344  SER A 348  1  N  ALA A 347   O  GLN A 370
SHEET    6   C 8 GLN A 309  HIS A 311  1  N  ILE A 310   O  PHE A 344
SHEET    7   C 8 ALA A 274  HIS A 278  1  N  ALA A 277   O  GLN A 309
SHEET    8   C 8 TYR A 248  ASP A 252  1  N  VAL A 249   O  HIS A 276
SHEET    1   D 5 LYS B  71  HIS B  78  0
SHEET    2   D 5 GLY B  81  TYR B  88 -1  O  GLY B  81   N  HIS B  78
SHEET    3   D 5 LEU B  26  PRO B  34 -1  N  TYR B  30   O  ALA B  84
SHEET    4   D 5 LEU B 115  HIS B 124 -1  O  ARG B 119   N  TYR B  31
SHEET    5   D 5 GLY B 292  ILE B 293  1  O  GLY B 292   N  LEU B 120
SHEET    1   E 8 GLU B 222  LEU B 224  0
SHEET    2   E 8 LEU B 184  LYS B 186  1  N  LEU B 185   O  LEU B 224
SHEET    3   E 8 LEU B 154  THR B 157  1  N  THR B 155   O  LEU B 184
SHEET    4   E 8 VAL B 368  GLN B 370  1  O  ILE B 369   N  LEU B 154
SHEET    5   E 8 PHE B 344  SER B 348  1  N  ALA B 347   O  GLN B 370
SHEET    6   E 8 GLN B 309  HIS B 311  1  N  ILE B 310   O  VAL B 346
SHEET    7   E 8 ALA B 274  HIS B 278  1  N  ALA B 277   O  GLN B 309
SHEET    8   E 8 TYR B 248  ASP B 252  1  N  VAL B 249   O  HIS B 276
SHEET    1   F 5 LYS D  71  HIS D  78  0
SHEET    2   F 5 GLY D  81  PRO D  89 -1  O  ILE D  83   N  GLU D  76
SHEET    3   F 5 GLU D  25  PRO D  34 -1  N  TYR D  30   O  ALA D  84
SHEET    4   F 5 LEU D 115  HIS D 124 -1  O  LEU D 121   N  GLU D  29
SHEET    5   F 5 GLY D 292  ILE D 293  1  O  GLY D 292   N  LEU D 118
SHEET    1   G 8 GLU D 222  LEU D 224  0
SHEET    2   G 8 LEU D 184  LYS D 186  1  N  LEU D 185   O  LEU D 224
SHEET    3   G 8 LEU D 154  THR D 157  1  N  THR D 155   O  LEU D 184
SHEET    4   G 8 VAL D 368  GLN D 370  1  O  ILE D 369   N  LEU D 154
SHEET    5   G 8 PHE D 344  ALA D 347  1  N  ALA D 347   O  GLN D 370
SHEET    6   G 8 GLN D 309  HIS D 311  1  N  ILE D 310   O  VAL D 346
SHEET    7   G 8 ALA D 274  HIS D 278  1  N  ALA D 277   O  GLN D 309
SHEET    8   G 8 TYR D 248  ASP D 252  1  N  VAL D 249   O  HIS D 276
SHEET    1   H 5 LYS E  71  HIS E  78  0
SHEET    2   H 5 GLY E  81  PRO E  89 -1  O  GLY E  81   N  HIS E  78
SHEET    3   H 5 GLU E  25  PRO E  34 -1  N  LEU E  26   O  TYR E  88
SHEET    4   H 5 LEU E 115  HIS E 124 -1  O  ARG E 119   N  TYR E  31
SHEET    5   H 5 GLY E 292  ILE E 293  1  O  GLY E 292   N  LEU E 120
SHEET    1   I 8 GLU E 222  LEU E 224  0
SHEET    2   I 8 LEU E 184  LYS E 186  1  N  LEU E 185   O  LEU E 224
SHEET    3   I 8 LEU E 154  THR E 157  1  N  THR E 155   O  LEU E 184
SHEET    4   I 8 VAL E 368  GLN E 370  1  O  ILE E 369   N  LEU E 154
SHEET    5   I 8 PHE E 344  ALA E 347  1  N  ALA E 347   O  GLN E 370
SHEET    6   I 8 GLN E 309  HIS E 311  1  N  ILE E 310   O  VAL E 346
SHEET    7   I 8 ALA E 274  HIS E 278  1  N  ALA E 277   O  GLN E 309
SHEET    8   I 8 TYR E 248  ASP E 252  1  N  VAL E 249   O  HIS E 276
CISPEP   1 LYS A  160    PRO A  161          0        -3.45
CISPEP   2 LYS B  160    PRO B  161          0        -1.36
CISPEP   3 LYS D  160    PRO D  161          0        -0.21
CISPEP   4 LYS E  160    PRO E  161          0         2.35
SITE     1 AC1  8 LYS A 160  GLY A 349  GLY A 350  GLN A 370
SITE     2 AC1  8 GLY A 372  GLY A 373  HOH A1094  HOH A1135
SITE     1 AC2  5 ARG A 279  HIS A 311  HOH A1141  HOH A1200
SITE     2 AC2  5 HOH A1217
SITE     1 AC3  4 TYR A  31  HIS A  78  ARG A 119  PRO A 289
SITE     1 AC4  5 GLY A 148  VAL A 149  LYS A 150  ASP A 151
SITE     2 AC4  5 ARG A 152
SITE     1 AC5  4 LYS A 205  ARG A 208  VAL A 209  ARG A 212
SITE     1 AC6  7 GLY B 349  GLY B 350  GLN B 370  GLY B 372
SITE     2 AC6  7 GLY B 373  HOH B2076  HOH B2077
SITE     1 AC7  6 ARG B 279  HIS B 311  SER B 348  HOH B2149
SITE     2 AC7  6 HOH B2150  HOH B2155
SITE     1 AC8  6 TYR B  31  HIS B  78  ARG B 119  LEU B 121
SITE     2 AC8  6 PRO B 289  HOH B2082
SITE     1 AC9  3 GLY B 148  VAL B 149  ARG B 152
SITE     1 BC1  4 LYS B 205  ARG B 208  VAL B 209  ARG B 212
SITE     1 BC2  8 LYS D 160  GLY D 349  GLY D 350  GLN D 370
SITE     2 BC2  8 GLY D 372  GLY D 373  HOH D3025  HOH D3108
SITE     1 BC3  3 ARG D 279  HIS D 311  HOH D3147
SITE     1 BC4  5 TYR D  31  HIS D  78  ARG D 119  PRO D 289
SITE     2 BC4  5 HOH D3129
SITE     1 BC5  3 GLY D 148  VAL D 149  ARG D 152
SITE     1 BC6  7 LYS E 160  GLY E 350  GLN E 370  GLY E 372
SITE     2 BC6  7 GLY E 373  HOH E4157  HOH E4175
SITE     1 BC7  5 ARG E 279  HIS E 311  SER E 348  HOH E4146
SITE     2 BC7  5 HOH E4147
SITE     1 BC8  3 TYR E  31  HIS E  78  PRO E 289
SITE     1 BC9  5 GLY E 148  VAL E 149  LYS E 150  ASP E 151
SITE     2 BC9  5 ARG E 152
SITE     1 CC1  3 LYS E 205  ARG E 208  VAL E 209
CRYST1  172.591  148.774  108.452  90.00 126.49  90.00 C 1 2 1      16
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      0.005794  0.000000  0.004285        0.00000
SCALE2      0.000000  0.006722  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011468        0.00000
      
PROCHECK
Go to PROCHECK summary
 References