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PDBsum entry 1qz2

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Top Page protein ligands Protein-protein interface(s) links
Isomerase/chaperone PDB id
1qz2
Jmol
Contents
Protein chain
285 a.a. *
Ligands
MET-GLU-GLU-VAL-
ASP
×2
Waters ×221
* Residue conservation analysis
HEADER    ISOMERASE/CHAPERONE                     15-SEP-03   1QZ2
TITLE     CRYSTAL STRUCTURE OF FKBP52 C-TERMINAL DOMAIN COMPLEX WITH
TITLE    2 THE C-TERMINAL PEPTIDE MEEVD OF HSP90
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: FK506-BINDING PROTEIN 4;
COMPND   3 CHAIN: A, B, C;
COMPND   4 FRAGMENT: FKBP52 C-TERMINAL DOMAIN;
COMPND   5 SYNONYM: FKBP52 PROTEIN, 52 KDA FK506 BINDING PROTEIN,
COMPND   6 FKBP59;
COMPND   7 EC: 5.2.1.8;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 2;
COMPND  10 MOLECULE: 5-MER PEPTIDE FROM HEAT SHOCK PROTEIN HSP 90;
COMPND  11 CHAIN: G, H;
COMPND  12 SYNONYM: HSP90;
COMPND  13 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 MOL_ID: 2;
SOURCE   8 SYNTHETIC: YES;
SOURCE   9 OTHER_DETAILS: THIS SEQUENCE IS OCCURS NATURALLY IN HUMAN
KEYWDS    ISOMERASE, ROTAMASE, CHAPERONE, HEAT SHOCK,
KEYWDS   2 ISOMERASE/CHAPERONE COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.WU,P.LI,Z.LOU,Y.LIU,Y.DING,C.SHU,B.SHEN,Z.RAO
REVDAT   2   24-FEB-09 1QZ2    1       VERSN
REVDAT   1   22-JUN-04 1QZ2    0
JRNL        AUTH   B.WU,P.LI,Y.LIU,Z.LOU,Y.DING,C.SHU,S.YE,M.BARTLAM,
JRNL        AUTH 2 B.SHEN,Z.RAO
JRNL        TITL   3D STRUCTURE OF HUMAN FK506-BINDING PROTEIN 52:
JRNL        TITL 2 IMPLICATIONS FOR THE ASSEMBLY OF THE
JRNL        TITL 3 GLUCOCORTICOID RECEPTOR/HSP90/IMMUNOPHILIN
JRNL        TITL 4 HETEROCOMPLEX.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 101  8348 2004
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   15159550
JRNL        DOI    10.1073/PNAS.0305969101
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
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) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 26054
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.230
REMARK   3   FREE R VALUE                     : 0.287
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1271
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7004
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 221
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.36
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1QZ2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-SEP-03.
REMARK 100 THE RCSB ID CODE IS RCSB020243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 26-AUG-03
REMARK 200  TEMPERATURE           (KELVIN) : 90
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 19-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66586
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
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) : 2.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 63.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, PH 8.0, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   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       85.40750
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       85.40750
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       55.80650
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       72.20850
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       55.80650
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       72.20850
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       85.40750
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       55.80650
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       72.20850
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       85.40750
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       55.80650
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       72.20850
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G, H
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A   -16
REMARK 465     GLY A   -15
REMARK 465     SER A   -14
REMARK 465     SER A   -13
REMARK 465     HIS A   -12
REMARK 465     HIS A   -11
REMARK 465     HIS A   -10
REMARK 465     HIS A    -9
REMARK 465     HIS A    -8
REMARK 465     HIS A    -7
REMARK 465     SER A    -6
REMARK 465     SER A    -5
REMARK 465     GLY A    -4
REMARK 465     LEU A    -3
REMARK 465     VAL A    -2
REMARK 465     PRO A    -1
REMARK 465     ARG A     0
REMARK 465     LYS A   426
REMARK 465     ALA A   427
REMARK 465     GLU A   428
REMARK 465     ALA A   429
REMARK 465     SER A   430
REMARK 465     SER A   431
REMARK 465     GLY A   432
REMARK 465     ASP A   433
REMARK 465     HIS A   434
REMARK 465     PRO A   435
REMARK 465     THR A   436
REMARK 465     ASP A   437
REMARK 465     THR A   438
REMARK 465     GLU A   439
REMARK 465     MET A   440
REMARK 465     LYS A   441
REMARK 465     GLU A   442
REMARK 465     GLU A   443
REMARK 465     GLN A   444
REMARK 465     LYS A   445
REMARK 465     SER A   446
REMARK 465     ASN A   447
REMARK 465     THR A   448
REMARK 465     ALA A   449
REMARK 465     GLY A   450
REMARK 465     SER A   451
REMARK 465     GLN A   452
REMARK 465     SER A   453
REMARK 465     GLN A   454
REMARK 465     VAL A   455
REMARK 465     GLU A   456
REMARK 465     THR A   457
REMARK 465     GLU A   458
REMARK 465     ALA A   459
REMARK 465     MET B   -16
REMARK 465     GLY B   -15
REMARK 465     SER B   -14
REMARK 465     SER B   -13
REMARK 465     HIS B   -12
REMARK 465     HIS B   -11
REMARK 465     HIS B   -10
REMARK 465     HIS B    -9
REMARK 465     HIS B    -8
REMARK 465     HIS B    -7
REMARK 465     SER B    -6
REMARK 465     SER B    -5
REMARK 465     GLY B    -4
REMARK 465     LEU B    -3
REMARK 465     VAL B    -2
REMARK 465     PRO B    -1
REMARK 465     ARG B     0
REMARK 465     LYS B   426
REMARK 465     ALA B   427
REMARK 465     GLU B   428
REMARK 465     ALA B   429
REMARK 465     SER B   430
REMARK 465     SER B   431
REMARK 465     GLY B   432
REMARK 465     ASP B   433
REMARK 465     HIS B   434
REMARK 465     PRO B   435
REMARK 465     THR B   436
REMARK 465     ASP B   437
REMARK 465     THR B   438
REMARK 465     GLU B   439
REMARK 465     MET B   440
REMARK 465     LYS B   441
REMARK 465     GLU B   442
REMARK 465     GLU B   443
REMARK 465     GLN B   444
REMARK 465     LYS B   445
REMARK 465     SER B   446
REMARK 465     ASN B   447
REMARK 465     THR B   448
REMARK 465     ALA B   449
REMARK 465     GLY B   450
REMARK 465     SER B   451
REMARK 465     GLN B   452
REMARK 465     SER B   453
REMARK 465     GLN B   454
REMARK 465     VAL B   455
REMARK 465     GLU B   456
REMARK 465     THR B   457
REMARK 465     GLU B   458
REMARK 465     ALA B   459
REMARK 465     MET C   -16
REMARK 465     GLY C   -15
REMARK 465     SER C   -14
REMARK 465     SER C   -13
REMARK 465     HIS C   -12
REMARK 465     HIS C   -11
REMARK 465     HIS C   -10
REMARK 465     HIS C    -9
REMARK 465     HIS C    -8
REMARK 465     HIS C    -7
REMARK 465     SER C    -6
REMARK 465     SER C    -5
REMARK 465     GLY C    -4
REMARK 465     LEU C    -3
REMARK 465     VAL C    -2
REMARK 465     PRO C    -1
REMARK 465     ARG C     0
REMARK 465     LYS C   426
REMARK 465     ALA C   427
REMARK 465     GLU C   428
REMARK 465     ALA C   429
REMARK 465     SER C   430
REMARK 465     SER C   431
REMARK 465     GLY C   432
REMARK 465     ASP C   433
REMARK 465     HIS C   434
REMARK 465     PRO C   435
REMARK 465     THR C   436
REMARK 465     ASP C   437
REMARK 465     THR C   438
REMARK 465     GLU C   439
REMARK 465     MET C   440
REMARK 465     LYS C   441
REMARK 465     GLU C   442
REMARK 465     GLU C   443
REMARK 465     GLN C   444
REMARK 465     LYS C   445
REMARK 465     SER C   446
REMARK 465     ASN C   447
REMARK 465     THR C   448
REMARK 465     ALA C   449
REMARK 465     GLY C   450
REMARK 465     SER C   451
REMARK 465     GLN C   452
REMARK 465     SER C   453
REMARK 465     GLN C   454
REMARK 465     VAL C   455
REMARK 465     GLU C   456
REMARK 465     THR C   457
REMARK 465     GLU C   458
REMARK 465     ALA C   459
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     GLU A 246    CB   CG   CD   OE1  OE2
REMARK 470     GLU A 275    CB   CG   CD   OE1  OE2
REMARK 470     GLU B 246    CB   CG   CD   OE1  OE2
REMARK 470     GLU B 275    CB   CG   CD   OE1  OE2
REMARK 470     GLU C 275    CB   CG   CD   OE1  OE2
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   O    HOH A   532     O    HOH A   534              0.00
REMARK 500   O    SER C   307     N    GLU C   309              2.17
REMARK 500   O    ASP A   349     N    ASN A   351              2.17
REMARK 500   O    GLU B   166     N    ALA B   168              2.19
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    HIS C   3   N   -  CA  -  C   ANGL. DEV. =  16.8 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    HIS A   3      -90.61    -20.43
REMARK 500    MET A   4       81.81      9.38
REMARK 500    GLU A 145       44.77   -145.37
REMARK 500    ILE A 154       74.31    -68.56
REMARK 500    ARG A 157     -160.62    -66.68
REMARK 500    GLU A 159     -111.12     24.48
REMARK 500    LYS A 179      -60.49     70.00
REMARK 500    ASP A 180        3.23    170.26
REMARK 500    ARG A 186      163.06    171.49
REMARK 500    GLN A 209        7.94    -66.63
REMARK 500    LYS A 213     -106.51    -71.00
REMARK 500    SER A 217     -168.11    176.38
REMARK 500    ALA A 226       93.14   -178.05
REMARK 500    PHE A 227      -19.03     64.03
REMARK 500    LYS A 232      107.51    179.04
REMARK 500    GLU A 233     -160.52    -75.13
REMARK 500    LYS A 234        9.46     44.71
REMARK 500    PHE A 235       -8.14   -159.99
REMARK 500    GLN A 236       72.74     31.41
REMARK 500    LYS A 250     -104.12    -78.20
REMARK 500    PHE A 252      134.61    160.06
REMARK 500    SER A 298      -82.23    -63.53
REMARK 500    TYR A 302      -82.72    -84.83
REMARK 500    GLU A 303      117.57    -13.38
REMARK 500    SER A 305       41.76    -79.16
REMARK 500    LEU A 332        7.84    -67.37
REMARK 500    GLN A 333       19.07     59.97
REMARK 500    SER A 350       10.62     32.43
REMARK 500    ASN A 352      126.18    -37.22
REMARK 500    ASN A 385       46.26    -79.80
REMARK 500    LYS A 387      -83.23    -39.22
REMARK 500    LYS A 424       97.46    -65.69
REMARK 500    SER B   2       20.07    132.84
REMARK 500    ASP B 147       89.19     44.44
REMARK 500    THR B 156       14.84     85.00
REMARK 500    ARG B 157       81.82    -20.61
REMARK 500    GLU B 159       91.97    -38.55
REMARK 500    TYR B 161      100.25     60.47
REMARK 500    ALA B 162     -124.94    178.98
REMARK 500    LYS B 163      116.72     86.55
REMARK 500    GLU B 166      -98.36    -63.07
REMARK 500    GLU B 175       84.52    166.40
REMARK 500    TYR B 178     -113.60    -70.62
REMARK 500    ASP B 180       48.87    148.85
REMARK 500    LEU B 182       99.57    -54.65
REMARK 500    GLU B 187       76.72   -116.23
REMARK 500    GLN B 209       -1.03    -59.56
REMARK 500    SER B 217     -178.93   -173.17
REMARK 500    ALA B 226     -123.42    -89.51
REMARK 500    VAL B 230      -27.41   -158.91
REMARK 500    GLU B 233      -46.50    -29.57
REMARK 500    ASN B 240       88.68     63.83
REMARK 500    LYS B 250      -71.09    -52.01
REMARK 500    LYS B 254      161.35    -42.40
REMARK 500    LYS B 256      151.34    -46.97
REMARK 500    SER B 258      -54.79    -17.13
REMARK 500    LEU B 300       33.84    -80.27
REMARK 500    GLU B 301      -86.17    -93.17
REMARK 500    GLU B 303       93.37    -69.25
REMARK 500    SER B 305       75.58    -64.54
REMARK 500    SER B 307       33.12    -88.91
REMARK 500    ASN B 308      -50.61     69.96
REMARK 500    ASP B 349       75.26   -158.19
REMARK 500    SER B 350      -15.45    -46.94
REMARK 500    ASP B 368       79.16   -118.97
REMARK 500    MET C   4       59.65     11.59
REMARK 500    GLU C 145       51.98   -100.52
REMARK 500    ASP C 147       68.77     62.88
REMARK 500    ILE C 154      100.53    -52.34
REMARK 500    GLU C 159      -97.05    -33.36
REMARK 500    TYR C 161     -100.93     92.19
REMARK 500    PRO C 164      139.47    -33.42
REMARK 500    GLU C 175      120.84   -178.21
REMARK 500    TYR C 178      -76.71    -68.27
REMARK 500    ASP C 180      -27.98    166.88
REMARK 500    LYS C 213     -100.34     -7.58
REMARK 500    PRO C 223       94.07    -59.57
REMARK 500    SER C 224      -26.41    161.98
REMARK 500    ALA C 226       80.28   -174.21
REMARK 500    SER C 229      -61.20     80.04
REMARK 500    VAL C 230      -73.21    -65.14
REMARK 500    LYS C 232       63.61   -163.14
REMARK 500    GLN C 236       77.67     68.93
REMARK 500    PRO C 239      -71.22    -32.46
REMARK 500    ALA C 241      141.70   -173.07
REMARK 500    SER C 305       27.87    -61.09
REMARK 500    PHE C 306     -148.60    -69.48
REMARK 500    SER C 307       95.54    177.19
REMARK 500    ASN C 308      -75.57     24.76
REMARK 500    ALA C 334       67.62   -100.25
REMARK 500    SER C 350      -32.72    -35.56
REMARK 500    ASN C 385       33.46    -81.01
REMARK 500    LYS C 387      -91.95    -29.01
REMARK 500    GLU G   3     -120.95   -132.40
REMARK 500    VAL G   4      -68.52     77.92
REMARK 500    GLU H   2     -154.76    -90.83
REMARK 500    VAL H   4      -78.86    -47.73
REMARK 500
REMARK 500 REMARK: NULL
DBREF  1QZ2 A  145   459  UNP    Q02790   FKBP4_HUMAN    144    458
DBREF  1QZ2 B  145   459  UNP    Q02790   FKBP4_HUMAN    144    458
DBREF  1QZ2 C  145   459  UNP    Q02790   FKBP4_HUMAN    144    458
DBREF  1QZ2 G    1     5  UNP    P08238   HS90B_HUMAN    719    723
DBREF  1QZ2 H    1     5  UNP    P08238   HS90B_HUMAN    719    723
SEQADV 1QZ2 MET A  -16  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 GLY A  -15  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER A  -14  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER A  -13  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS A  -12  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS A  -11  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS A  -10  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS A   -9  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS A   -8  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS A   -7  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER A   -6  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER A   -5  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 GLY A   -4  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 LEU A   -3  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 VAL A   -2  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 PRO A   -1  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 ARG A    0  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 GLY A    1  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER A    2  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS A    3  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 MET A    4  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 MET B  -16  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 GLY B  -15  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER B  -14  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER B  -13  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS B  -12  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS B  -11  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS B  -10  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS B   -9  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS B   -8  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS B   -7  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER B   -6  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER B   -5  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 GLY B   -4  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 LEU B   -3  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 VAL B   -2  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 PRO B   -1  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 ARG B    0  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 GLY B    1  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER B    2  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS B    3  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 MET B    4  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 MET C  -16  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 GLY C  -15  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER C  -14  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER C  -13  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS C  -12  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS C  -11  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS C  -10  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS C   -9  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS C   -8  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS C   -7  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER C   -6  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER C   -5  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 GLY C   -4  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 LEU C   -3  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 VAL C   -2  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 PRO C   -1  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 ARG C    0  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 GLY C    1  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 SER C    2  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 HIS C    3  UNP  Q02790              CLONING ARTIFACT
SEQADV 1QZ2 MET C    4  UNP  Q02790              CLONING ARTIFACT
SEQRES   1 A  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 A  336  LEU VAL PRO ARG GLY SER HIS MET GLU GLU ASP GLY GLY
SEQRES   3 A  336  ILE ILE ARG ARG ILE GLN THR ARG GLY GLU GLY TYR ALA
SEQRES   4 A  336  LYS PRO ASN GLU GLY ALA ILE VAL GLU VAL ALA LEU GLU
SEQRES   5 A  336  GLY TYR TYR LYS ASP LYS LEU PHE ASP GLN ARG GLU LEU
SEQRES   6 A  336  ARG PHE GLU ILE GLY GLU GLY GLU ASN LEU ASP LEU PRO
SEQRES   7 A  336  TYR GLY LEU GLU ARG ALA ILE GLN ARG MET GLU LYS GLY
SEQRES   8 A  336  GLU HIS SER ILE VAL TYR LEU LYS PRO SER TYR ALA PHE
SEQRES   9 A  336  GLY SER VAL GLY LYS GLU LYS PHE GLN ILE PRO PRO ASN
SEQRES  10 A  336  ALA GLU LEU LYS TYR GLU LEU HIS LEU LYS SER PHE GLU
SEQRES  11 A  336  LYS ALA LYS GLU SER TRP GLU MET ASN SER GLU GLU LYS
SEQRES  12 A  336  LEU GLU GLN SER THR ILE VAL LYS GLU ARG GLY THR VAL
SEQRES  13 A  336  TYR PHE LYS GLU GLY LYS TYR LYS GLN ALA LEU LEU GLN
SEQRES  14 A  336  TYR LYS LYS ILE VAL SER TRP LEU GLU TYR GLU SER SER
SEQRES  15 A  336  PHE SER ASN GLU GLU ALA GLN LYS ALA GLN ALA LEU ARG
SEQRES  16 A  336  LEU ALA SER HIS LEU ASN LEU ALA MET CYS HIS LEU LYS
SEQRES  17 A  336  LEU GLN ALA PHE SER ALA ALA ILE GLU SER CYS ASN LYS
SEQRES  18 A  336  ALA LEU GLU LEU ASP SER ASN ASN GLU LYS GLY LEU PHE
SEQRES  19 A  336  ARG ARG GLY GLU ALA HIS LEU ALA VAL ASN ASP PHE GLU
SEQRES  20 A  336  LEU ALA ARG ALA ASP PHE GLN LYS VAL LEU GLN LEU TYR
SEQRES  21 A  336  PRO ASN ASN LYS ALA ALA LYS THR GLN LEU ALA VAL CYS
SEQRES  22 A  336  GLN GLN ARG ILE ARG ARG GLN LEU ALA ARG GLU LYS LYS
SEQRES  23 A  336  LEU TYR ALA ASN MET PHE GLU ARG LEU ALA GLU GLU GLU
SEQRES  24 A  336  ASN LYS ALA LYS ALA GLU ALA SER SER GLY ASP HIS PRO
SEQRES  25 A  336  THR ASP THR GLU MET LYS GLU GLU GLN LYS SER ASN THR
SEQRES  26 A  336  ALA GLY SER GLN SER GLN VAL GLU THR GLU ALA
SEQRES   1 B  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 B  336  LEU VAL PRO ARG GLY SER HIS MET GLU GLU ASP GLY GLY
SEQRES   3 B  336  ILE ILE ARG ARG ILE GLN THR ARG GLY GLU GLY TYR ALA
SEQRES   4 B  336  LYS PRO ASN GLU GLY ALA ILE VAL GLU VAL ALA LEU GLU
SEQRES   5 B  336  GLY TYR TYR LYS ASP LYS LEU PHE ASP GLN ARG GLU LEU
SEQRES   6 B  336  ARG PHE GLU ILE GLY GLU GLY GLU ASN LEU ASP LEU PRO
SEQRES   7 B  336  TYR GLY LEU GLU ARG ALA ILE GLN ARG MET GLU LYS GLY
SEQRES   8 B  336  GLU HIS SER ILE VAL TYR LEU LYS PRO SER TYR ALA PHE
SEQRES   9 B  336  GLY SER VAL GLY LYS GLU LYS PHE GLN ILE PRO PRO ASN
SEQRES  10 B  336  ALA GLU LEU LYS TYR GLU LEU HIS LEU LYS SER PHE GLU
SEQRES  11 B  336  LYS ALA LYS GLU SER TRP GLU MET ASN SER GLU GLU LYS
SEQRES  12 B  336  LEU GLU GLN SER THR ILE VAL LYS GLU ARG GLY THR VAL
SEQRES  13 B  336  TYR PHE LYS GLU GLY LYS TYR LYS GLN ALA LEU LEU GLN
SEQRES  14 B  336  TYR LYS LYS ILE VAL SER TRP LEU GLU TYR GLU SER SER
SEQRES  15 B  336  PHE SER ASN GLU GLU ALA GLN LYS ALA GLN ALA LEU ARG
SEQRES  16 B  336  LEU ALA SER HIS LEU ASN LEU ALA MET CYS HIS LEU LYS
SEQRES  17 B  336  LEU GLN ALA PHE SER ALA ALA ILE GLU SER CYS ASN LYS
SEQRES  18 B  336  ALA LEU GLU LEU ASP SER ASN ASN GLU LYS GLY LEU PHE
SEQRES  19 B  336  ARG ARG GLY GLU ALA HIS LEU ALA VAL ASN ASP PHE GLU
SEQRES  20 B  336  LEU ALA ARG ALA ASP PHE GLN LYS VAL LEU GLN LEU TYR
SEQRES  21 B  336  PRO ASN ASN LYS ALA ALA LYS THR GLN LEU ALA VAL CYS
SEQRES  22 B  336  GLN GLN ARG ILE ARG ARG GLN LEU ALA ARG GLU LYS LYS
SEQRES  23 B  336  LEU TYR ALA ASN MET PHE GLU ARG LEU ALA GLU GLU GLU
SEQRES  24 B  336  ASN LYS ALA LYS ALA GLU ALA SER SER GLY ASP HIS PRO
SEQRES  25 B  336  THR ASP THR GLU MET LYS GLU GLU GLN LYS SER ASN THR
SEQRES  26 B  336  ALA GLY SER GLN SER GLN VAL GLU THR GLU ALA
SEQRES   1 C  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 C  336  LEU VAL PRO ARG GLY SER HIS MET GLU GLU ASP GLY GLY
SEQRES   3 C  336  ILE ILE ARG ARG ILE GLN THR ARG GLY GLU GLY TYR ALA
SEQRES   4 C  336  LYS PRO ASN GLU GLY ALA ILE VAL GLU VAL ALA LEU GLU
SEQRES   5 C  336  GLY TYR TYR LYS ASP LYS LEU PHE ASP GLN ARG GLU LEU
SEQRES   6 C  336  ARG PHE GLU ILE GLY GLU GLY GLU ASN LEU ASP LEU PRO
SEQRES   7 C  336  TYR GLY LEU GLU ARG ALA ILE GLN ARG MET GLU LYS GLY
SEQRES   8 C  336  GLU HIS SER ILE VAL TYR LEU LYS PRO SER TYR ALA PHE
SEQRES   9 C  336  GLY SER VAL GLY LYS GLU LYS PHE GLN ILE PRO PRO ASN
SEQRES  10 C  336  ALA GLU LEU LYS TYR GLU LEU HIS LEU LYS SER PHE GLU
SEQRES  11 C  336  LYS ALA LYS GLU SER TRP GLU MET ASN SER GLU GLU LYS
SEQRES  12 C  336  LEU GLU GLN SER THR ILE VAL LYS GLU ARG GLY THR VAL
SEQRES  13 C  336  TYR PHE LYS GLU GLY LYS TYR LYS GLN ALA LEU LEU GLN
SEQRES  14 C  336  TYR LYS LYS ILE VAL SER TRP LEU GLU TYR GLU SER SER
SEQRES  15 C  336  PHE SER ASN GLU GLU ALA GLN LYS ALA GLN ALA LEU ARG
SEQRES  16 C  336  LEU ALA SER HIS LEU ASN LEU ALA MET CYS HIS LEU LYS
SEQRES  17 C  336  LEU GLN ALA PHE SER ALA ALA ILE GLU SER CYS ASN LYS
SEQRES  18 C  336  ALA LEU GLU LEU ASP SER ASN ASN GLU LYS GLY LEU PHE
SEQRES  19 C  336  ARG ARG GLY GLU ALA HIS LEU ALA VAL ASN ASP PHE GLU
SEQRES  20 C  336  LEU ALA ARG ALA ASP PHE GLN LYS VAL LEU GLN LEU TYR
SEQRES  21 C  336  PRO ASN ASN LYS ALA ALA LYS THR GLN LEU ALA VAL CYS
SEQRES  22 C  336  GLN GLN ARG ILE ARG ARG GLN LEU ALA ARG GLU LYS LYS
SEQRES  23 C  336  LEU TYR ALA ASN MET PHE GLU ARG LEU ALA GLU GLU GLU
SEQRES  24 C  336  ASN LYS ALA LYS ALA GLU ALA SER SER GLY ASP HIS PRO
SEQRES  25 C  336  THR ASP THR GLU MET LYS GLU GLU GLN LYS SER ASN THR
SEQRES  26 C  336  ALA GLY SER GLN SER GLN VAL GLU THR GLU ALA
SEQRES   1 G    5  MET GLU GLU VAL ASP
SEQRES   1 H    5  MET GLU GLU VAL ASP
FORMUL   6  HOH   *221(H2 O)
HELIX    1   1 GLU A  194  ASP A  199  5                                   6
HELIX    2   2 PRO A  201  GLN A  209  1                                   9
HELIX    3   3 PRO A  223  ALA A  226  5                                   4
HELIX    4   4 GLU A  257  MET A  261  5                                   5
HELIX    5   5 ASN A  262  GLU A  283  1                                  22
HELIX    6   6 LYS A  285  GLU A  301  1                                  17
HELIX    7   7 SER A  307  LEU A  332  1                                  26
HELIX    8   8 ALA A  334  SER A  350  1                                  17
HELIX    9   9 ASN A  352  VAL A  366  1                                  15
HELIX   10  10 ASP A  368  TYR A  383  1                                  16
HELIX   11  11 ASN A  386  LYS A  424  1                                  39
HELIX   12  12 GLU B  194  ASP B  199  5                                   6
HELIX   13  13 PRO B  201  GLN B  209  1                                   9
HELIX   14  14 PRO B  223  ALA B  226  5                                   4
HELIX   15  15 LYS B  232  GLN B  236  5                                   5
HELIX   16  16 GLU B  257  MET B  261  5                                   5
HELIX   17  17 ASN B  262  GLU B  283  1                                  22
HELIX   18  18 LYS B  285  LEU B  300  1                                  16
HELIX   19  19 ASN B  308  LEU B  332  1                                  25
HELIX   20  20 ALA B  334  ASP B  349  1                                  16
HELIX   21  21 ASN B  352  VAL B  366  1                                  15
HELIX   22  22 ASP B  368  TYR B  383  1                                  16
HELIX   23  23 ASN B  386  LYS B  424  1                                  39
HELIX   24  24 GLU C  194  ASP C  199  5                                   6
HELIX   25  25 PRO C  201  ARG C  210  1                                  10
HELIX   26  26 GLU C  257  MET C  261  5                                   5
HELIX   27  27 ASN C  262  GLU C  283  1                                  22
HELIX   28  28 LYS C  285  LEU C  300  1                                  16
HELIX   29  29 ASN C  308  LEU C  332  1                                  25
HELIX   30  30 ALA C  334  GLU C  347  1                                  14
HELIX   31  31 ASN C  352  VAL C  366  1                                  15
HELIX   32  32 ASP C  368  TYR C  383  1                                  16
HELIX   33  33 ASN C  386  ASN C  423  1                                  38
SHEET    1   A 5 ILE A 150  THR A 156  0
SHEET    2   A 5 HIS A 216  LEU A 221 -1  O  TYR A 220   N  ILE A 151
SHEET    3   A 5 LEU A 243  GLU A 253 -1  O  TYR A 245   N  VAL A 219
SHEET    4   A 5 ILE A 169  TYR A 178 -1  N  TYR A 177   O  LYS A 244
SHEET    5   A 5 LYS A 181  ARG A 186 -1  O  ARG A 186   N  LEU A 174
SHEET    1   B 5 ILE A 150  THR A 156  0
SHEET    2   B 5 HIS A 216  LEU A 221 -1  O  TYR A 220   N  ILE A 151
SHEET    3   B 5 LEU A 243  GLU A 253 -1  O  TYR A 245   N  VAL A 219
SHEET    4   B 5 ILE A 169  TYR A 178 -1  N  TYR A 177   O  LYS A 244
SHEET    5   B 5 ARG A 189  GLU A 191 -1  O  PHE A 190   N  VAL A 170
SHEET    1   C 5 ILE B 150  ARG B 153  0
SHEET    2   C 5 HIS B 216  LEU B 221 -1  O  TYR B 220   N  ILE B 151
SHEET    3   C 5 LEU B 243  HIS B 248 -1  O  TYR B 245   N  VAL B 219
SHEET    4   C 5 GLY B 176  TYR B 177 -1  N  TYR B 177   O  LYS B 244
SHEET    5   C 5 LEU B 182  ASP B 184 -1  O  PHE B 183   N  GLY B 176
SHEET    1   D 3 ARG B 189  GLU B 191  0
SHEET    2   D 3 ILE B 169  GLU B 171 -1  N  VAL B 170   O  PHE B 190
SHEET    3   D 3 PHE B 252  GLU B 253 -1  O  GLU B 253   N  ILE B 169
SHEET    1   E 5 ILE C 150  ARG C 152  0
SHEET    2   E 5 VAL C 219  LEU C 221 -1  O  TYR C 220   N  ILE C 151
SHEET    3   E 5 LEU C 243  TYR C 245 -1  O  TYR C 245   N  VAL C 219
SHEET    4   E 5 ILE C 169  TYR C 177 -1  N  TYR C 177   O  LYS C 244
SHEET    5   E 5 LEU C 182  GLU C 191 -1  O  LEU C 188   N  VAL C 172
SHEET    1   F 5 ILE C 150  ARG C 152  0
SHEET    2   F 5 VAL C 219  LEU C 221 -1  O  TYR C 220   N  ILE C 151
SHEET    3   F 5 LEU C 243  TYR C 245 -1  O  TYR C 245   N  VAL C 219
SHEET    4   F 5 ILE C 169  TYR C 177 -1  N  TYR C 177   O  LYS C 244
SHEET    5   F 5 HIS C 248  GLU C 253 -1  O  SER C 251   N  GLU C 171
CRYST1  111.613  144.417  170.815  90.00  90.00  90.00 C 2 2 21     24
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      0.008960  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006924  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005854        0.00000
      
PROCHECK
Go to PROCHECK summary
 References