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PDBsum entry 1m5y

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Isomerase, cell cycle PDB id
1m5y
Jmol
Contents
Protein chains
388 a.a. *
* Residue conservation analysis
HEADER    ISOMERASE, CELL CYCLE                   10-JUL-02   1M5Y
TITLE     CRYSTALLOGRAPHIC STRUCTURE OF SURA, A MOLECULAR CHAPERONE
TITLE    2 THAT FACILITATES OUTER MEMBRANE PORIN FOLDING
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SURVIVAL PROTEIN SURA;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: SURVIVAL PROTEIN; PEPTIDYL-PROLYL CIS-TRANS
COMPND   5 ISOMERASE SURA; PPIASE; ROTAMASE C;
COMPND   6 EC: 5.2.1.8;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 GENE: SURA;
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: PTYB2
KEYWDS    SURVIVAL PROTEIN A, PERIPLASMIC MOLECULAR CHAPERONE,
KEYWDS   2 MEMBRANE PROTEIN FOLDING, GRAM NEGATIVE BACTERIA, CRYSTAL
KEYWDS   3 STRUCTURE, ISOMERASE, CELL CYCLE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.BITTO,D.B.MCKAY
REVDAT   2   24-FEB-09 1M5Y    1       VERSN
REVDAT   1   08-NOV-02 1M5Y    0
JRNL        AUTH   E.BITTO,D.B.MCKAY
JRNL        TITL   CRYSTALLOGRAPHIC STRUCTURE OF SURA, A MOLECULAR
JRNL        TITL 2 CHAPERONE THAT FACILITATES FOLDING OF OUTER
JRNL        TITL 3 MEMBRANE PORINS
JRNL        REF    STRUCTURE                     V.  10  1489 2002
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   12429090
JRNL        DOI    10.1016/S0969-2126(02)00877-8
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.80
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1008569.150
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 84.4
REMARK   3   NUMBER OF REFLECTIONS             : 41869
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 SET) : 0.228
REMARK   3   FREE R VALUE                     : 0.283
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3753
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.19
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 62.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4571
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3310
REMARK   3   BIN FREE R VALUE                    : 0.4080
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.10
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 511
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 11914
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 59.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.50
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -17.08000
REMARK   3    B22 (A**2) : 1.00000
REMARK   3    B33 (A**2) : 16.08000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.37
REMARK   3   ESD FROM SIGMAA              (A) : 0.48
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.49
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.62
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.70
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.31
REMARK   3   BSOL        : 27.42
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1M5Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-02.
REMARK 100 THE RCSB ID CODE IS RCSB016639.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-02; 11-MAR-01
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100
REMARK 200  PH                             : 5.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y
REMARK 200  RADIATION SOURCE               : SSRL; SSRL
REMARK 200  BEAMLINE                       : BL11-1; BL11-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.965; 0.965
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI(III) BENT
REMARK 200                                   MONOCHROMATOR (HORIZONTAL
REMARK 200                                   FOCUSING); SINGLE CRYSTAL
REMARK 200                                   SI(III) BENT MONOCHROMATOR
REMARK 200                                   (HORIZONTAL FOCUSING)
REMARK 200  OPTICS                         : FLAT MIRROR (VERTICAL
REMARK 200                                   FOCUSING); FLAT MIRROR
REMARK 200                                   (VERTICAL FOCUSING)
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD; CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC
REMARK 200                                   QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45004
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2
REMARK 200  DATA REDUNDANCY                : 4.600
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07700
REMARK 200   FOR THE DATA SET  : 1.6200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.34800
REMARK 200   FOR SHELL         : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 64.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.75M AMMONIUM SULPHATE, 100MM
REMARK 280  SODIUM CITRATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP AT 303K,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 303.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X,Y+1/2,Z+1/2
REMARK 290       6555   -X,-Y+1/2,Z+1/2
REMARK 290       7555   -X,Y+1/2,-Z+1/2
REMARK 290       8555   X,-Y+1/2,-Z+1/2
REMARK 290       9555   X+1/2,Y,Z+1/2
REMARK 290      10555   -X+1/2,-Y,Z+1/2
REMARK 290      11555   -X+1/2,Y,-Z+1/2
REMARK 290      12555   X+1/2,-Y,-Z+1/2
REMARK 290      13555   X+1/2,Y+1/2,Z
REMARK 290      14555   -X+1/2,-Y+1/2,Z
REMARK 290      15555   -X+1/2,Y+1/2,-Z
REMARK 290      16555   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        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      111.70300
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      139.86050
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      111.70300
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      139.86050
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      111.70300
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      139.86050
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      111.70300
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      139.86050
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       79.40850
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      139.86050
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       79.40850
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000      139.86050
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000       79.40850
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      139.86050
REMARK 290   SMTRY1  12  1.000000  0.000000  0.000000       79.40850
REMARK 290   SMTRY2  12  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      139.86050
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       79.40850
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      111.70300
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       79.40850
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000      111.70300
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       79.40850
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000      111.70300
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       79.40850
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000      111.70300
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: ASYMMETRIC UNIT CONTAINS 4 DIFFERENT CONFORMERS OF SURA,
REMARK 300 ALL OF WHICH ARE INCLUDED IN THE COORDINATE FILE CARBOXY
REMARK 300 TERMINAL GLYCINE RESIDUE REMAINS IN THE PRIMARY SEQUENCE AFTER
REMARK 300 CLEAVING THE AFFINITY TAG
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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     ALA A    21
REMARK 465     PRO A    22
REMARK 465     GLN A    23
REMARK 465     VAL A    24
REMARK 465     GLY A   165
REMARK 465     ASN A   166
REMARK 465     GLN A   167
REMARK 465     ASN A   168
REMARK 465     ASP A   169
REMARK 465     ALA A   170
REMARK 465     SER A   171
REMARK 465     ASP A   387
REMARK 465     LYS A   388
REMARK 465     THR A   389
REMARK 465     ASP A   390
REMARK 465     ALA A   391
REMARK 465     ALA A   392
REMARK 465     GLN A   393
REMARK 465     LYS A   394
REMARK 465     ASN A   428
REMARK 465     ALA B    21
REMARK 465     PRO B    22
REMARK 465     GLN B    23
REMARK 465     VAL B    24
REMARK 465     VAL B   164
REMARK 465     GLY B   165
REMARK 465     ASN B   166
REMARK 465     GLN B   167
REMARK 465     ASN B   168
REMARK 465     ASP B   169
REMARK 465     ALA B   170
REMARK 465     SER B   171
REMARK 465     GLY B   275
REMARK 465     GLU B   276
REMARK 465     SER B   277
REMARK 465     LYS B   278
REMARK 465     ASN B   279
REMARK 465     ILE B   280
REMARK 465     SER B   281
REMARK 465     VAL B   282
REMARK 465     VAL B   386
REMARK 465     ASP B   387
REMARK 465     LYS B   388
REMARK 465     THR B   389
REMARK 465     ASP B   390
REMARK 465     ALA B   391
REMARK 465     ALA B   392
REMARK 465     GLN B   393
REMARK 465     LYS B   394
REMARK 465     ASP B   395
REMARK 465     ASN B   428
REMARK 465     ALA C    21
REMARK 465     PRO C    22
REMARK 465     GLN C    23
REMARK 465     VAL C    24
REMARK 465     VAL C   164
REMARK 465     GLY C   165
REMARK 465     ASN C   166
REMARK 465     GLN C   167
REMARK 465     ASN C   168
REMARK 465     ASP C   169
REMARK 465     ALA C   170
REMARK 465     SER C   171
REMARK 465     ARG C   274
REMARK 465     GLY C   275
REMARK 465     GLU C   276
REMARK 465     SER C   277
REMARK 465     LYS C   278
REMARK 465     ASN C   279
REMARK 465     ILE C   280
REMARK 465     SER C   281
REMARK 465     VAL C   282
REMARK 465     VAL C   386
REMARK 465     ASP C   387
REMARK 465     LYS C   388
REMARK 465     THR C   389
REMARK 465     ASP C   390
REMARK 465     ALA C   391
REMARK 465     ALA C   392
REMARK 465     GLN C   393
REMARK 465     LYS C   394
REMARK 465     ASP C   395
REMARK 465     ASN C   428
REMARK 465     ALA D    21
REMARK 465     PRO D    22
REMARK 465     GLN D    23
REMARK 465     VAL D    24
REMARK 465     VAL D   164
REMARK 465     GLY D   165
REMARK 465     ASN D   166
REMARK 465     GLN D   167
REMARK 465     ASN D   168
REMARK 465     ASP D   169
REMARK 465     ALA D   170
REMARK 465     SER D   171
REMARK 465     THR D   389
REMARK 465     ASP D   390
REMARK 465     ALA D   391
REMARK 465     ALA D   392
REMARK 465     GLN D   393
REMARK 465     LYS D   394
REMARK 465     ASP D   395
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    ASN A  33     -118.09     51.33
REMARK 500    ASN A  34       59.04   -100.64
REMARK 500    GLN A  55        3.33    -54.76
REMARK 500    MET A  87       31.79    -75.60
REMARK 500    GLN A 155       -4.84     70.57
REMARK 500    GLN A 163      158.46    -43.31
REMARK 500    LEU A 226       -5.03    -56.65
REMARK 500    PRO A 258      102.60    -58.23
REMARK 500    ASN A 271      -73.57    -60.97
REMARK 500    LYS A 278      154.56    -45.00
REMARK 500    ASN A 279     -135.40    -69.22
REMARK 500    GLU A 308      -37.80    -36.24
REMARK 500    ILE A 310       -9.83    -57.36
REMARK 500    SER A 316       34.64    -93.58
REMARK 500    LYS A 326        2.16    -60.68
REMARK 500    GLN A 330       32.08    -98.84
REMARK 500    SER A 334      -58.84   -130.35
REMARK 500    ARG A 359       34.83    -88.43
REMARK 500    ASN B  33     -117.14     51.37
REMARK 500    GLN B  55       10.33    -59.08
REMARK 500    ASP B  63      -15.85    -49.18
REMARK 500    MET B  87       27.00    -71.56
REMARK 500    ARG B 148       20.62    -60.06
REMARK 500    ARG B 149      -30.05   -142.03
REMARK 500    ASN B 227       46.82   -104.16
REMARK 500    PRO B 258       98.78    -55.56
REMARK 500    PRO B 296      -73.75     17.57
REMARK 500    PHE B 328      -37.86   -138.21
REMARK 500    SER B 329      158.59    -39.22
REMARK 500    GLN B 330      -66.26   -105.00
REMARK 500    ASP B 331       98.40    -37.38
REMARK 500    SER B 334      -34.57    162.87
REMARK 500    GLN B 337       37.69    -92.86
REMARK 500    ILE B 348        0.03    -64.78
REMARK 500    LEU B 381      -85.44    -87.65
REMARK 500    ASN C  33     -118.16     43.15
REMARK 500    GLN C  55       10.51    -59.30
REMARK 500    MET C  87       32.21    -73.99
REMARK 500    ARG C 148       16.20    -62.21
REMARK 500    ARG C 149      -26.82   -140.17
REMARK 500    ASN C 227       46.65   -100.57
REMARK 500    PRO C 258      103.04    -57.09
REMARK 500    SER C 295      153.86    179.29
REMARK 500    PRO C 296      -70.06     19.61
REMARK 500    PHE C 328      -38.91   -138.63
REMARK 500    SER C 329      151.95    -38.87
REMARK 500    GLN C 330      -69.94   -100.73
REMARK 500    ASP C 331       96.85    -33.34
REMARK 500    SER C 334      -42.47    170.92
REMARK 500    GLN C 337       37.73    -93.05
REMARK 500    LEU C 381      -85.44    -92.91
REMARK 500    ASN D  33     -119.17     51.58
REMARK 500    ASN D  34       54.73    -98.70
REMARK 500    GLN D  55        6.01    -56.30
REMARK 500    MET D  87       35.30    -77.84
REMARK 500    GLN D 155       -5.52     73.23
REMARK 500    LYS D 278      154.11    -49.70
REMARK 500    ASN D 279     -136.12    -68.14
REMARK 500    GLU D 308      -34.56    -33.27
REMARK 500    SER D 316       38.92    -95.46
REMARK 500    LYS D 326        0.87    -60.34
REMARK 500    GLN D 330       32.28    -94.90
REMARK 500    SER D 334      -57.52   -132.65
REMARK 500    ARG D 359       38.87    -91.35
REMARK 500    SER D 371     -157.86   -126.41
REMARK 500    SER D 427     -140.39    -73.52
REMARK 500
REMARK 500 REMARK: NULL
DBREF  1M5Y A   21   428  UNP    P0ABZ6   SURA_ECOLI      21    428
DBREF  1M5Y B   21   428  UNP    P0ABZ6   SURA_ECOLI      21    428
DBREF  1M5Y C   21   428  UNP    P0ABZ6   SURA_ECOLI      21    428
DBREF  1M5Y D   21   428  UNP    P0ABZ6   SURA_ECOLI      21    428
SEQRES   1 A  408  ALA PRO GLN VAL VAL ASP LYS VAL ALA ALA VAL VAL ASN
SEQRES   2 A  408  ASN GLY VAL VAL LEU GLU SER ASP VAL ASP GLY LEU MET
SEQRES   3 A  408  GLN SER VAL LYS LEU ASN ALA ALA GLN ALA ARG GLN GLN
SEQRES   4 A  408  LEU PRO ASP ASP ALA THR LEU ARG HIS GLN ILE MET GLU
SEQRES   5 A  408  ARG LEU ILE MET ASP GLN ILE ILE LEU GLN MET GLY GLN
SEQRES   6 A  408  LYS MET GLY VAL LYS ILE SER ASP GLU GLN LEU ASP GLN
SEQRES   7 A  408  ALA ILE ALA ASN ILE ALA LYS GLN ASN ASN MET THR LEU
SEQRES   8 A  408  ASP GLN MET ARG SER ARG LEU ALA TYR ASP GLY LEU ASN
SEQRES   9 A  408  TYR ASN THR TYR ARG ASN GLN ILE ARG LYS GLU MET ILE
SEQRES  10 A  408  ILE SER GLU VAL ARG ASN ASN GLU VAL ARG ARG ARG ILE
SEQRES  11 A  408  THR ILE LEU PRO GLN GLU VAL GLU SER LEU ALA GLN GLN
SEQRES  12 A  408  VAL GLY ASN GLN ASN ASP ALA SER THR GLU LEU ASN LEU
SEQRES  13 A  408  SER HIS ILE LEU ILE PRO LEU PRO GLU ASN PRO THR SER
SEQRES  14 A  408  ASP GLN VAL ASN GLU ALA GLU SER GLN ALA ARG ALA ILE
SEQRES  15 A  408  VAL ASP GLN ALA ARG ASN GLY ALA ASP PHE GLY LYS LEU
SEQRES  16 A  408  ALA ILE ALA HIS SER ALA ASP GLN GLN ALA LEU ASN GLY
SEQRES  17 A  408  GLY GLN MET GLY TRP GLY ARG ILE GLN GLU LEU PRO GLY
SEQRES  18 A  408  ILE PHE ALA GLN ALA LEU SER THR ALA LYS LYS GLY ASP
SEQRES  19 A  408  ILE VAL GLY PRO ILE ARG SER GLY VAL GLY PHE HIS ILE
SEQRES  20 A  408  LEU LYS VAL ASN ASP LEU ARG GLY GLU SER LYS ASN ILE
SEQRES  21 A  408  SER VAL THR GLU VAL HIS ALA ARG HIS ILE LEU LEU LYS
SEQRES  22 A  408  PRO SER PRO ILE MET THR ASP GLU GLN ALA ARG VAL LYS
SEQRES  23 A  408  LEU GLU GLN ILE ALA ALA ASP ILE LYS SER GLY LYS THR
SEQRES  24 A  408  THR PHE ALA ALA ALA ALA LYS GLU PHE SER GLN ASP PRO
SEQRES  25 A  408  GLY SER ALA ASN GLN GLY GLY ASP LEU GLY TRP ALA THR
SEQRES  26 A  408  PRO ASP ILE PHE ASP PRO ALA PHE ARG ASP ALA LEU THR
SEQRES  27 A  408  ARG LEU ASN LYS GLY GLN MET SER ALA PRO VAL HIS SER
SEQRES  28 A  408  SER PHE GLY TRP HIS LEU ILE GLU LEU LEU ASP THR ARG
SEQRES  29 A  408  ASN VAL ASP LYS THR ASP ALA ALA GLN LYS ASP ARG ALA
SEQRES  30 A  408  TYR ARG MET LEU MET ASN ARG LYS PHE SER GLU GLU ALA
SEQRES  31 A  408  ALA SER TRP MET GLN GLU GLN ARG ALA SER ALA TYR VAL
SEQRES  32 A  408  LYS ILE LEU SER ASN
SEQRES   1 B  408  ALA PRO GLN VAL VAL ASP LYS VAL ALA ALA VAL VAL ASN
SEQRES   2 B  408  ASN GLY VAL VAL LEU GLU SER ASP VAL ASP GLY LEU MET
SEQRES   3 B  408  GLN SER VAL LYS LEU ASN ALA ALA GLN ALA ARG GLN GLN
SEQRES   4 B  408  LEU PRO ASP ASP ALA THR LEU ARG HIS GLN ILE MET GLU
SEQRES   5 B  408  ARG LEU ILE MET ASP GLN ILE ILE LEU GLN MET GLY GLN
SEQRES   6 B  408  LYS MET GLY VAL LYS ILE SER ASP GLU GLN LEU ASP GLN
SEQRES   7 B  408  ALA ILE ALA ASN ILE ALA LYS GLN ASN ASN MET THR LEU
SEQRES   8 B  408  ASP GLN MET ARG SER ARG LEU ALA TYR ASP GLY LEU ASN
SEQRES   9 B  408  TYR ASN THR TYR ARG ASN GLN ILE ARG LYS GLU MET ILE
SEQRES  10 B  408  ILE SER GLU VAL ARG ASN ASN GLU VAL ARG ARG ARG ILE
SEQRES  11 B  408  THR ILE LEU PRO GLN GLU VAL GLU SER LEU ALA GLN GLN
SEQRES  12 B  408  VAL GLY ASN GLN ASN ASP ALA SER THR GLU LEU ASN LEU
SEQRES  13 B  408  SER HIS ILE LEU ILE PRO LEU PRO GLU ASN PRO THR SER
SEQRES  14 B  408  ASP GLN VAL ASN GLU ALA GLU SER GLN ALA ARG ALA ILE
SEQRES  15 B  408  VAL ASP GLN ALA ARG ASN GLY ALA ASP PHE GLY LYS LEU
SEQRES  16 B  408  ALA ILE ALA HIS SER ALA ASP GLN GLN ALA LEU ASN GLY
SEQRES  17 B  408  GLY GLN MET GLY TRP GLY ARG ILE GLN GLU LEU PRO GLY
SEQRES  18 B  408  ILE PHE ALA GLN ALA LEU SER THR ALA LYS LYS GLY ASP
SEQRES  19 B  408  ILE VAL GLY PRO ILE ARG SER GLY VAL GLY PHE HIS ILE
SEQRES  20 B  408  LEU LYS VAL ASN ASP LEU ARG GLY GLU SER LYS ASN ILE
SEQRES  21 B  408  SER VAL THR GLU VAL HIS ALA ARG HIS ILE LEU LEU LYS
SEQRES  22 B  408  PRO SER PRO ILE MET THR ASP GLU GLN ALA ARG VAL LYS
SEQRES  23 B  408  LEU GLU GLN ILE ALA ALA ASP ILE LYS SER GLY LYS THR
SEQRES  24 B  408  THR PHE ALA ALA ALA ALA LYS GLU PHE SER GLN ASP PRO
SEQRES  25 B  408  GLY SER ALA ASN GLN GLY GLY ASP LEU GLY TRP ALA THR
SEQRES  26 B  408  PRO ASP ILE PHE ASP PRO ALA PHE ARG ASP ALA LEU THR
SEQRES  27 B  408  ARG LEU ASN LYS GLY GLN MET SER ALA PRO VAL HIS SER
SEQRES  28 B  408  SER PHE GLY TRP HIS LEU ILE GLU LEU LEU ASP THR ARG
SEQRES  29 B  408  ASN VAL ASP LYS THR ASP ALA ALA GLN LYS ASP ARG ALA
SEQRES  30 B  408  TYR ARG MET LEU MET ASN ARG LYS PHE SER GLU GLU ALA
SEQRES  31 B  408  ALA SER TRP MET GLN GLU GLN ARG ALA SER ALA TYR VAL
SEQRES  32 B  408  LYS ILE LEU SER ASN
SEQRES   1 C  408  ALA PRO GLN VAL VAL ASP LYS VAL ALA ALA VAL VAL ASN
SEQRES   2 C  408  ASN GLY VAL VAL LEU GLU SER ASP VAL ASP GLY LEU MET
SEQRES   3 C  408  GLN SER VAL LYS LEU ASN ALA ALA GLN ALA ARG GLN GLN
SEQRES   4 C  408  LEU PRO ASP ASP ALA THR LEU ARG HIS GLN ILE MET GLU
SEQRES   5 C  408  ARG LEU ILE MET ASP GLN ILE ILE LEU GLN MET GLY GLN
SEQRES   6 C  408  LYS MET GLY VAL LYS ILE SER ASP GLU GLN LEU ASP GLN
SEQRES   7 C  408  ALA ILE ALA ASN ILE ALA LYS GLN ASN ASN MET THR LEU
SEQRES   8 C  408  ASP GLN MET ARG SER ARG LEU ALA TYR ASP GLY LEU ASN
SEQRES   9 C  408  TYR ASN THR TYR ARG ASN GLN ILE ARG LYS GLU MET ILE
SEQRES  10 C  408  ILE SER GLU VAL ARG ASN ASN GLU VAL ARG ARG ARG ILE
SEQRES  11 C  408  THR ILE LEU PRO GLN GLU VAL GLU SER LEU ALA GLN GLN
SEQRES  12 C  408  VAL GLY ASN GLN ASN ASP ALA SER THR GLU LEU ASN LEU
SEQRES  13 C  408  SER HIS ILE LEU ILE PRO LEU PRO GLU ASN PRO THR SER
SEQRES  14 C  408  ASP GLN VAL ASN GLU ALA GLU SER GLN ALA ARG ALA ILE
SEQRES  15 C  408  VAL ASP GLN ALA ARG ASN GLY ALA ASP PHE GLY LYS LEU
SEQRES  16 C  408  ALA ILE ALA HIS SER ALA ASP GLN GLN ALA LEU ASN GLY
SEQRES  17 C  408  GLY GLN MET GLY TRP GLY ARG ILE GLN GLU LEU PRO GLY
SEQRES  18 C  408  ILE PHE ALA GLN ALA LEU SER THR ALA LYS LYS GLY ASP
SEQRES  19 C  408  ILE VAL GLY PRO ILE ARG SER GLY VAL GLY PHE HIS ILE
SEQRES  20 C  408  LEU LYS VAL ASN ASP LEU ARG GLY GLU SER LYS ASN ILE
SEQRES  21 C  408  SER VAL THR GLU VAL HIS ALA ARG HIS ILE LEU LEU LYS
SEQRES  22 C  408  PRO SER PRO ILE MET THR ASP GLU GLN ALA ARG VAL LYS
SEQRES  23 C  408  LEU GLU GLN ILE ALA ALA ASP ILE LYS SER GLY LYS THR
SEQRES  24 C  408  THR PHE ALA ALA ALA ALA LYS GLU PHE SER GLN ASP PRO
SEQRES  25 C  408  GLY SER ALA ASN GLN GLY GLY ASP LEU GLY TRP ALA THR
SEQRES  26 C  408  PRO ASP ILE PHE ASP PRO ALA PHE ARG ASP ALA LEU THR
SEQRES  27 C  408  ARG LEU ASN LYS GLY GLN MET SER ALA PRO VAL HIS SER
SEQRES  28 C  408  SER PHE GLY TRP HIS LEU ILE GLU LEU LEU ASP THR ARG
SEQRES  29 C  408  ASN VAL ASP LYS THR ASP ALA ALA GLN LYS ASP ARG ALA
SEQRES  30 C  408  TYR ARG MET LEU MET ASN ARG LYS PHE SER GLU GLU ALA
SEQRES  31 C  408  ALA SER TRP MET GLN GLU GLN ARG ALA SER ALA TYR VAL
SEQRES  32 C  408  LYS ILE LEU SER ASN
SEQRES   1 D  408  ALA PRO GLN VAL VAL ASP LYS VAL ALA ALA VAL VAL ASN
SEQRES   2 D  408  ASN GLY VAL VAL LEU GLU SER ASP VAL ASP GLY LEU MET
SEQRES   3 D  408  GLN SER VAL LYS LEU ASN ALA ALA GLN ALA ARG GLN GLN
SEQRES   4 D  408  LEU PRO ASP ASP ALA THR LEU ARG HIS GLN ILE MET GLU
SEQRES   5 D  408  ARG LEU ILE MET ASP GLN ILE ILE LEU GLN MET GLY GLN
SEQRES   6 D  408  LYS MET GLY VAL LYS ILE SER ASP GLU GLN LEU ASP GLN
SEQRES   7 D  408  ALA ILE ALA ASN ILE ALA LYS GLN ASN ASN MET THR LEU
SEQRES   8 D  408  ASP GLN MET ARG SER ARG LEU ALA TYR ASP GLY LEU ASN
SEQRES   9 D  408  TYR ASN THR TYR ARG ASN GLN ILE ARG LYS GLU MET ILE
SEQRES  10 D  408  ILE SER GLU VAL ARG ASN ASN GLU VAL ARG ARG ARG ILE
SEQRES  11 D  408  THR ILE LEU PRO GLN GLU VAL GLU SER LEU ALA GLN GLN
SEQRES  12 D  408  VAL GLY ASN GLN ASN ASP ALA SER THR GLU LEU ASN LEU
SEQRES  13 D  408  SER HIS ILE LEU ILE PRO LEU PRO GLU ASN PRO THR SER
SEQRES  14 D  408  ASP GLN VAL ASN GLU ALA GLU SER GLN ALA ARG ALA ILE
SEQRES  15 D  408  VAL ASP GLN ALA ARG ASN GLY ALA ASP PHE GLY LYS LEU
SEQRES  16 D  408  ALA ILE ALA HIS SER ALA ASP GLN GLN ALA LEU ASN GLY
SEQRES  17 D  408  GLY GLN MET GLY TRP GLY ARG ILE GLN GLU LEU PRO GLY
SEQRES  18 D  408  ILE PHE ALA GLN ALA LEU SER THR ALA LYS LYS GLY ASP
SEQRES  19 D  408  ILE VAL GLY PRO ILE ARG SER GLY VAL GLY PHE HIS ILE
SEQRES  20 D  408  LEU LYS VAL ASN ASP LEU ARG GLY GLU SER LYS ASN ILE
SEQRES  21 D  408  SER VAL THR GLU VAL HIS ALA ARG HIS ILE LEU LEU LYS
SEQRES  22 D  408  PRO SER PRO ILE MET THR ASP GLU GLN ALA ARG VAL LYS
SEQRES  23 D  408  LEU GLU GLN ILE ALA ALA ASP ILE LYS SER GLY LYS THR
SEQRES  24 D  408  THR PHE ALA ALA ALA ALA LYS GLU PHE SER GLN ASP PRO
SEQRES  25 D  408  GLY SER ALA ASN GLN GLY GLY ASP LEU GLY TRP ALA THR
SEQRES  26 D  408  PRO ASP ILE PHE ASP PRO ALA PHE ARG ASP ALA LEU THR
SEQRES  27 D  408  ARG LEU ASN LYS GLY GLN MET SER ALA PRO VAL HIS SER
SEQRES  28 D  408  SER PHE GLY TRP HIS LEU ILE GLU LEU LEU ASP THR ARG
SEQRES  29 D  408  ASN VAL ASP LYS THR ASP ALA ALA GLN LYS ASP ARG ALA
SEQRES  30 D  408  TYR ARG MET LEU MET ASN ARG LYS PHE SER GLU GLU ALA
SEQRES  31 D  408  ALA SER TRP MET GLN GLU GLN ARG ALA SER ALA TYR VAL
SEQRES  32 D  408  LYS ILE LEU SER ASN
HELIX    1   1 GLU A   39  GLN A   55  1                                  17
HELIX    2   2 ASP A   62  MET A   87  1                                  26
HELIX    3   3 SER A   92  ASN A  107  1                                  16
HELIX    4   4 THR A  110  GLY A  122  1                                  13
HELIX    5   5 ASN A  124  ARG A  149  1                                  26
HELIX    6   6 GLN A  155  GLN A  163  1                                   9
HELIX    7   7 THR A  188  ASN A  208  1                                  21
HELIX    8   8 ASP A  211  SER A  220  1                                  10
HELIX    9   9 GLN A  224  GLY A  228  5                                   5
HELIX   10  10 ARG A  235  LEU A  239  5                                   5
HELIX   11  11 PRO A  240  GLN A  245  1                                   6
HELIX   12  12 ALA A  246  THR A  249  5                                   4
HELIX   13  13 THR A  299  SER A  316  1                                  18
HELIX   14  14 THR A  320  SER A  329  1                                  10
HELIX   15  15 SER A  334  GLY A  338  5                                   5
HELIX   16  16 THR A  345  PHE A  349  5                                   5
HELIX   17  17 ASP A  350  ARG A  359  1                                  10
HELIX   18  18 ASP A  395  ALA A  421  1                                  27
HELIX   19  19 GLU B   39  GLN B   55  1                                  17
HELIX   20  20 ASP B   62  MET B   87  1                                  26
HELIX   21  21 SER B   92  ASN B  107  1                                  16
HELIX   22  22 THR B  110  GLY B  122  1                                  13
HELIX   23  23 ASN B  124  ARG B  148  1                                  25
HELIX   24  24 GLN B  155  GLN B  163  1                                   9
HELIX   25  25 THR B  188  ASN B  208  1                                  21
HELIX   26  26 ASP B  211  SER B  220  1                                  10
HELIX   27  27 GLN B  224  GLY B  228  5                                   5
HELIX   28  28 ARG B  235  LEU B  239  5                                   5
HELIX   29  29 PRO B  240  GLN B  245  1                                   6
HELIX   30  30 THR B  299  SER B  316  1                                  18
HELIX   31  31 THR B  320  SER B  329  1                                  10
HELIX   32  32 THR B  345  PHE B  349  5                                   5
HELIX   33  33 ASP B  350  LEU B  360  1                                  11
HELIX   34  34 ARG B  396  SER B  420  1                                  25
HELIX   35  35 GLU C   39  GLN C   55  1                                  17
HELIX   36  36 ASP C   62  MET C   87  1                                  26
HELIX   37  37 SER C   92  ASN C  107  1                                  16
HELIX   38  38 THR C  110  GLY C  122  1                                  13
HELIX   39  39 ASN C  124  ARG C  148  1                                  25
HELIX   40  40 GLN C  155  GLN C  163  1                                   9
HELIX   41  41 THR C  188  ASN C  208  1                                  21
HELIX   42  42 ASP C  211  SER C  220  1                                  10
HELIX   43  43 ASP C  222  GLY C  228  5                                   7
HELIX   44  44 ARG C  235  LEU C  239  5                                   5
HELIX   45  45 PRO C  240  GLN C  245  1                                   6
HELIX   46  46 THR C  299  SER C  316  1                                  18
HELIX   47  47 THR C  320  SER C  329  1                                  10
HELIX   48  48 THR C  345  PHE C  349  5                                   5
HELIX   49  49 ASP C  350  ARG C  359  1                                  10
HELIX   50  50 ARG C  396  SER C  420  1                                  25
HELIX   51  51 GLU D   39  GLN D   55  1                                  17
HELIX   52  52 ASP D   62  MET D   87  1                                  26
HELIX   53  53 SER D   92  ASN D  107  1                                  16
HELIX   54  54 THR D  110  GLY D  122  1                                  13
HELIX   55  55 ASN D  124  ILE D  150  1                                  27
HELIX   56  56 GLN D  155  GLN D  163  1                                   9
HELIX   57  57 THR D  188  ASN D  208  1                                  21
HELIX   58  58 ASP D  211  SER D  220  1                                  10
HELIX   59  59 GLN D  224  GLY D  228  5                                   5
HELIX   60  60 ARG D  235  LEU D  239  5                                   5
HELIX   61  61 PRO D  240  GLN D  245  1                                   6
HELIX   62  62 ALA D  246  THR D  249  5                                   4
HELIX   63  63 THR D  299  SER D  316  1                                  18
HELIX   64  64 THR D  320  SER D  329  1                                  10
HELIX   65  65 SER D  334  GLY D  338  5                                   5
HELIX   66  66 THR D  345  PHE D  349  5                                   5
HELIX   67  67 ASP D  350  ARG D  359  1                                  10
HELIX   68  68 ARG D  396  ALA D  421  1                                  26
SHEET    1   A 3 VAL A  36  LEU A  38  0
SHEET    2   A 3 VAL A  28  VAL A  32 -1  N  ALA A  30   O  VAL A  37
SHEET    3   A 3 VAL A 423  ILE A 425 -1  O  LYS A 424   N  VAL A  31
SHEET    1   B 4 GLN A 230  GLY A 234  0
SHEET    2   B 4 LEU A 174  PRO A 182 -1  N  LEU A 174   O  GLY A 234
SHEET    3   B 4 GLY A 264  LEU A 273 -1  O  PHE A 265   N  ILE A 181
SHEET    4   B 4 ILE A 255  SER A 261 -1  N  ILE A 259   O  HIS A 266
SHEET    1   C 4 ASP A 340  ALA A 344  0
SHEET    2   C 4 VAL A 282  LEU A 292 -1  N  VAL A 285   O  ALA A 344
SHEET    3   C 4 TRP A 375  VAL A 386 -1  O  TRP A 375   N  LEU A 292
SHEET    4   C 4 VAL A 369  HIS A 370 -1  N  VAL A 369   O  HIS A 376
SHEET    1   D 3 VAL B  36  LEU B  38  0
SHEET    2   D 3 VAL B  28  VAL B  32 -1  N  ALA B  30   O  VAL B  37
SHEET    3   D 3 VAL B 423  LYS B 424 -1  O  LYS B 424   N  VAL B  31
SHEET    1   E 4 GLN B 230  GLY B 234  0
SHEET    2   E 4 LEU B 174  PRO B 182 -1  N  LEU B 174   O  GLY B 234
SHEET    3   E 4 GLY B 264  LEU B 273 -1  O  PHE B 265   N  ILE B 181
SHEET    4   E 4 ILE B 255  SER B 261 -1  N  ILE B 259   O  HIS B 266
SHEET    1   F 4 ASP B 340  ALA B 344  0
SHEET    2   F 4 VAL B 285  LEU B 292 -1  N  VAL B 285   O  ALA B 344
SHEET    3   F 4 GLY B 374  ASP B 382 -1  O  TRP B 375   N  LEU B 292
SHEET    4   F 4 VAL B 369  SER B 371 -1  N  SER B 371   O  GLY B 374
SHEET    1   G 3 VAL C  36  LEU C  38  0
SHEET    2   G 3 VAL C  28  VAL C  32 -1  N  ALA C  30   O  VAL C  37
SHEET    3   G 3 VAL C 423  ILE C 425 -1  O  LYS C 424   N  VAL C  31
SHEET    1   H 4 GLN C 230  GLY C 234  0
SHEET    2   H 4 LEU C 174  PRO C 182 -1  N  LEU C 174   O  GLY C 234
SHEET    3   H 4 GLY C 264  ASP C 272 -1  O  ILE C 267   N  ILE C 179
SHEET    4   H 4 ILE C 255  ARG C 260 -1  N  ILE C 259   O  HIS C 266
SHEET    1   I 4 ASP C 340  ALA C 344  0
SHEET    2   I 4 VAL C 285  LEU C 292 -1  N  VAL C 285   O  ALA C 344
SHEET    3   I 4 TRP C 375  ASP C 382 -1  O  TRP C 375   N  LEU C 292
SHEET    4   I 4 VAL C 369  HIS C 370 -1  N  VAL C 369   O  HIS C 376
SHEET    1   J 3 VAL D  36  LEU D  38  0
SHEET    2   J 3 VAL D  28  VAL D  32 -1  N  ALA D  30   O  VAL D  37
SHEET    3   J 3 VAL D 423  ILE D 425 -1  O  LYS D 424   N  VAL D  31
SHEET    1   K 4 GLN D 230  GLY D 234  0
SHEET    2   K 4 LEU D 174  PRO D 182 -1  N  LEU D 174   O  GLY D 234
SHEET    3   K 4 GLY D 264  LEU D 273 -1  O  PHE D 265   N  ILE D 181
SHEET    4   K 4 ILE D 255  SER D 261 -1  N  ILE D 259   O  HIS D 266
SHEET    1   L 4 ASP D 340  ALA D 344  0
SHEET    2   L 4 VAL D 282  LEU D 292 -1  N  VAL D 285   O  ALA D 344
SHEET    3   L 4 TRP D 375  VAL D 386 -1  O  TRP D 375   N  LEU D 292
SHEET    4   L 4 VAL D 369  HIS D 370 -1  N  VAL D 369   O  HIS D 376
CRYST1  158.817  223.406  279.721  90.00  90.00  90.00 F 2 2 2      64
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      0.006297  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004476  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003575        0.00000
      
PROCHECK
Go to PROCHECK summary
 References