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PDBsum entry 2c3b

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Top Page protein ligands Protein-protein interface(s) links
Isomerase PDB id
2c3b
Jmol
Contents
Protein chains
141 a.a.
Ligands
SO4 ×2
Waters ×123
HEADER    ISOMERASE                               05-OCT-05   2C3B
TITLE     THE CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS CYCLOPHILIN
TITLE    2 REVEALS 3D DOMAIN SWAPPING OF A CENTRAL ELEMENT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PPIASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CYCLOPHILIN;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS;
SOURCE   3 ORGANISM_TAXID: 5085;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PQE32
KEYWDS    ISOMERASE, 3D DOMAIN SWAPPING, MISFOLDING, PPIASE, ASP F 11,
KEYWDS   2 ALLERGEN, ROTAMASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.LIMACHER,D.P.KLOER,S.FLUCKIGER,G.FOLKERS,R.CRAMERI, L.SCAPOZZA
REVDAT   4   13-JUL-11 2C3B    1       VERSN
REVDAT   3   24-FEB-09 2C3B    1       VERSN
REVDAT   2   15-FEB-06 2C3B    1       JRNL
REVDAT   1   30-JAN-06 2C3B    0
JRNL        AUTH   A.LIMACHER,D.P.KLOER,S.FLUCKIGER,G.FOLKERS,R.CRAMERI,
JRNL        AUTH 2 L.SCAPOZZA
JRNL        TITL   THE CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS CYCLOPHILIN
JRNL        TITL 2 REVEALS 3D DOMAIN SWAPPING OF A CENTRAL ELEMENT
JRNL        REF    STRUCTURE                     V.  14   185 2006
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   16472738
JRNL        DOI    10.1016/J.STR.2005.10.015
REMARK   2
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0003
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) : 1.85
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.90
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1
REMARK   3   NUMBER OF REFLECTIONS             : 31360
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) : 0.191
REMARK   3   R VALUE            (WORKING SET) : 0.189
REMARK   3   FREE R VALUE                     : 0.214
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1675
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) : 1.85
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2264
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400
REMARK   3   BIN FREE R VALUE SET COUNT          : 136
REMARK   3   BIN FREE R VALUE                    : 0.2880
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2175
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 123
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) : 39.81
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.26000
REMARK   3    B22 (A**2) : -0.26000
REMARK   3    B33 (A**2) : 0.38000
REMARK   3    B12 (A**2) : -0.13000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.115
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.110
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.077
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.037
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960
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):  2224 ; 0.014 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  2018 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2989 ; 1.947 ; 1.944
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4704 ; 0.932 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   271 ; 4.090 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    98 ;36.843 ;23.367
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   398 ;10.602 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;13.020 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   329 ; 0.119 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2429 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   469 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   382 ; 0.198 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1928 ; 0.178 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1070 ; 0.179 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1326 ; 0.085 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    91 ; 0.173 ; 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):    15 ; 0.199 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    35 ; 0.245 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.102 ; 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):  1766 ; 2.940 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2216 ; 3.330 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   998 ; 5.529 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   773 ; 7.187 ; 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 : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     0        A    69
REMARK   3    RESIDUE RANGE :   A   128        A   171
REMARK   3    ORIGIN FOR THE GROUP (A):  24.2957  -3.9885  74.4592
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0108 T22:  -0.1472
REMARK   3      T33:  -0.1707 T12:  -0.0511
REMARK   3      T13:   0.0008 T23:   0.0205
REMARK   3    L TENSOR
REMARK   3      L11:   4.0014 L22:   3.9954
REMARK   3      L33:   2.4284 L12:   1.7292
REMARK   3      L13:   0.3143 L23:   1.4301
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2246 S12:   0.4885 S13:   0.2039
REMARK   3      S21:  -0.6900 S22:   0.1588 S23:   0.2555
REMARK   3      S31:  -0.2537 S32:  -0.1262 S33:   0.0658
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 :   A    92        A   127
REMARK   3    ORIGIN FOR THE GROUP (A):  20.8109   6.2146  95.1479
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1277 T22:  -0.2162
REMARK   3      T33:  -0.0895 T12:   0.0814
REMARK   3      T13:   0.0171 T23:  -0.0357
REMARK   3    L TENSOR
REMARK   3      L11:   6.4429 L22:   5.9844
REMARK   3      L33:   7.2573 L12:   0.2441
REMARK   3      L13:   0.0819 L23:   1.5913
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0937 S12:   0.4342 S13:   0.0639
REMARK   3      S21:  -0.3603 S22:   0.1032 S23:   0.5598
REMARK   3      S31:  -0.1177 S32:  -0.4380 S33:  -0.0094
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     1        B    68
REMARK   3    RESIDUE RANGE :   B   128        B   171
REMARK   3    ORIGIN FOR THE GROUP (A):  25.1891   2.1288 107.0887
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0380 T22:  -0.1833
REMARK   3      T33:  -0.1405 T12:   0.0941
REMARK   3      T13:   0.0591 T23:   0.0131
REMARK   3    L TENSOR
REMARK   3      L11:   4.0487 L22:   3.9811
REMARK   3      L33:   2.7609 L12:  -2.0089
REMARK   3      L13:  -0.1396 L23:   0.3600
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2021 S12:  -0.4112 S13:  -0.1790
REMARK   3      S21:   0.5247 S22:   0.1749 S23:   0.3394
REMARK   3      S31:   0.2408 S32:  -0.0882 S33:   0.0273
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 :   B    96        B   127
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7833  -4.4926  84.2331
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1361 T22:  -0.2265
REMARK   3      T33:  -0.0844 T12:  -0.0246
REMARK   3      T13:   0.0240 T23:  -0.0346
REMARK   3    L TENSOR
REMARK   3      L11:   9.0448 L22:   5.7169
REMARK   3      L33:  13.0616 L12:   2.8201
REMARK   3      L13:  -0.9560 L23:   4.2558
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0677 S12:  -0.1329 S13:   0.0506
REMARK   3      S21:   0.1294 S22:  -0.0127 S23:   0.7459
REMARK   3      S31:   0.0744 S32:  -0.4482 S33:   0.0804
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 2C3B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-OCT-05.
REMARK 100 THE PDBE ID CODE IS EBI-23307.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 6.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X06SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99990
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33079
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.600
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1
REMARK 200  DATA REDUNDANCY                : 5.900
REMARK 200  R MERGE                    (I) : 0.09000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 19.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 57.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: DROP SOLUTION: 13% AMMONIUM
REMARK 280  SULFATE, 0.1 M MES PH 6. RESERVOIR SOLUTION: 50% AMMONIUM
REMARK 280  SULFATE, 0.1 M SODIUM CITRATE PH 5.5.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.09600
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      104.19200
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      104.19200
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       52.09600
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     PHE A    70
REMARK 465     THR A    71
REMARK 465     ARG A    72
REMARK 465     GLY A    73
REMARK 465     ASN A    74
REMARK 465     GLY A    75
REMARK 465     THR A    76
REMARK 465     GLY A    77
REMARK 465     GLY A    78
REMARK 465     ARG A    79
REMARK 465     SER A    80
REMARK 465     ILE A    81
REMARK 465     TYR A    82
REMARK 465     GLY A    83
REMARK 465     ASP A    84
REMARK 465     LYS A    85
REMARK 465     PHE A    86
REMARK 465     ALA A    87
REMARK 465     ASP A    88
REMARK 465     GLU A    89
REMARK 465     ASN A    90
REMARK 465     PHE A    91
REMARK 465     ASN A   105
REMARK 465     ALA A   106
REMARK 465     GLY A   107
REMARK 465     PRO A   108
REMARK 465     ASN A   109
REMARK 465     THR A   110
REMARK 465     ASN A   111
REMARK 465     GLY A   112
REMARK 465     SER A   113
REMARK 465     SER B     0
REMARK 465     ASP B    69
REMARK 465     PHE B    70
REMARK 465     THR B    71
REMARK 465     ARG B    72
REMARK 465     GLY B    73
REMARK 465     ASN B    74
REMARK 465     GLY B    75
REMARK 465     THR B    76
REMARK 465     GLY B    77
REMARK 465     GLY B    78
REMARK 465     ARG B    79
REMARK 465     SER B    80
REMARK 465     ILE B    81
REMARK 465     TYR B    82
REMARK 465     GLY B    83
REMARK 465     ASP B    84
REMARK 465     LYS B    85
REMARK 465     PHE B    86
REMARK 465     ALA B    87
REMARK 465     ASP B    88
REMARK 465     GLU B    89
REMARK 465     ASN B    90
REMARK 465     PHE B    91
REMARK 465     SER B    92
REMARK 465     ARG B    93
REMARK 465     LYS B    94
REMARK 465     HIS B    95
REMARK 465     ASN B   105
REMARK 465     ALA B   106
REMARK 465     GLY B   107
REMARK 465     PRO B   108
REMARK 465     ASN B   109
REMARK 465     THR B   110
REMARK 465     ASN B   111
REMARK 465     GLY B   112
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 B  2039     O    HOH B  2040              2.17
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 B  29   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
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    PHE A  28       59.87   -103.08
REMARK 500    GLU A  53        0.21     82.88
REMARK 500    PHE A  63      -61.59   -141.57
REMARK 500    PHE B  28       59.62    -96.40
REMARK 500    PHE B  63      -58.56   -139.97
REMARK 500    VAL B 121       47.71     37.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1172
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1172
DBREF  2C3B A    0     0  PDB    2C3B     2C3B             0      0
DBREF  2C3B A    1   171  UNP    Q9Y7F6   Q9Y7F6_ASPFU     8    178
DBREF  2C3B B    0     0  PDB    2C3B     2C3B             0      0
DBREF  2C3B B    1   171  UNP    Q9Y7F6   Q9Y7F6_ASPFU     8    178
SEQRES   1 A  172  SER MET SER GLN VAL PHE PHE ASP VAL GLU TYR ALA PRO
SEQRES   2 A  172  VAL GLY THR ALA GLU THR LYS VAL GLY ARG ILE VAL PHE
SEQRES   3 A  172  ASN LEU PHE ASP LYS ASP VAL PRO LYS THR ALA LYS ASN
SEQRES   4 A  172  PHE ARG GLU LEU CYS LYS ARG PRO ALA GLY GLU GLY TYR
SEQRES   5 A  172  ARG GLU SER THR PHE HIS ARG ILE ILE PRO ASN PHE MET
SEQRES   6 A  172  ILE GLN GLY GLY ASP PHE THR ARG GLY ASN GLY THR GLY
SEQRES   7 A  172  GLY ARG SER ILE TYR GLY ASP LYS PHE ALA ASP GLU ASN
SEQRES   8 A  172  PHE SER ARG LYS HIS ASP LYS LYS GLY ILE LEU SER MET
SEQRES   9 A  172  ALA ASN ALA GLY PRO ASN THR ASN GLY SER GLN PHE PHE
SEQRES  10 A  172  ILE THR THR ALA VAL THR SER TRP LEU ASP GLY LYS HIS
SEQRES  11 A  172  VAL VAL PHE GLY GLU VAL ALA ASP GLU LYS SER TYR SER
SEQRES  12 A  172  VAL VAL LYS GLU ILE GLU ALA LEU GLY SER SER SER GLY
SEQRES  13 A  172  SER VAL ARG SER ASN THR ARG PRO LYS ILE VAL ASN CYS
SEQRES  14 A  172  GLY GLU LEU
SEQRES   1 B  172  SER MET SER GLN VAL PHE PHE ASP VAL GLU TYR ALA PRO
SEQRES   2 B  172  VAL GLY THR ALA GLU THR LYS VAL GLY ARG ILE VAL PHE
SEQRES   3 B  172  ASN LEU PHE ASP LYS ASP VAL PRO LYS THR ALA LYS ASN
SEQRES   4 B  172  PHE ARG GLU LEU CYS LYS ARG PRO ALA GLY GLU GLY TYR
SEQRES   5 B  172  ARG GLU SER THR PHE HIS ARG ILE ILE PRO ASN PHE MET
SEQRES   6 B  172  ILE GLN GLY GLY ASP PHE THR ARG GLY ASN GLY THR GLY
SEQRES   7 B  172  GLY ARG SER ILE TYR GLY ASP LYS PHE ALA ASP GLU ASN
SEQRES   8 B  172  PHE SER ARG LYS HIS ASP LYS LYS GLY ILE LEU SER MET
SEQRES   9 B  172  ALA ASN ALA GLY PRO ASN THR ASN GLY SER GLN PHE PHE
SEQRES  10 B  172  ILE THR THR ALA VAL THR SER TRP LEU ASP GLY LYS HIS
SEQRES  11 B  172  VAL VAL PHE GLY GLU VAL ALA ASP GLU LYS SER TYR SER
SEQRES  12 B  172  VAL VAL LYS GLU ILE GLU ALA LEU GLY SER SER SER GLY
SEQRES  13 B  172  SER VAL ARG SER ASN THR ARG PRO LYS ILE VAL ASN CYS
SEQRES  14 B  172  GLY GLU LEU
HET    SO4  A1172       5
HET    SO4  B1172       5
HETNAM     SO4 SULFATE ION
FORMUL   3  SO4    2(O4 S 2-)
FORMUL   5  HOH   *123(H2 O)
HELIX    1   1 PRO A   33  LYS A   44  1                                  12
HELIX    2   2 ARG A   93  LYS A   97  1                                   5
HELIX    3   3 GLU A  138  GLU A  148  1                                  11
HELIX    4   4 PRO B   33  LYS B   44  1                                  12
HELIX    5   5 THR B  122  TRP B  124  1                                   3
HELIX    6   6 GLU B  138  GLU B  148  1                                  11
SHEET    1  AA 8 ARG A  58  ILE A  60  0
SHEET    2  AA 8 MET A  64  GLY A  67 -1  O  MET A  64   N  ILE A  60
SHEET    3  AA 8 PHE B 115  THR B 118 -1  O  PHE B 115   N  GLY A  67
SHEET    4  AA 8 ILE B 100  MET B 103 -1  O  ILE B 100   N  THR B 118
SHEET    5  AA 8 VAL A 130  VAL A 135 -1  O  VAL A 130   N  MET B 103
SHEET    6  AA 8 LYS A  19  LEU A  27 -1  O  ASN A  26   N  GLU A 134
SHEET    7  AA 8 VAL A   4  TYR A  10 -1  O  VAL A   4   N  PHE A  25
SHEET    8  AA 8 LYS A 164  GLU A 170 -1  O  LYS A 164   N  GLU A   9
SHEET    1  BA 8 ARG B  58  ILE B  60  0
SHEET    2  BA 8 MET B  64  GLY B  67 -1  O  MET B  64   N  ILE B  60
SHEET    3  BA 8 PHE A 115  THR A 118 -1  O  PHE A 115   N  GLY B  67
SHEET    4  BA 8 ILE A 100  MET A 103 -1  O  ILE A 100   N  THR A 118
SHEET    5  BA 8 VAL B 130  VAL B 135 -1  O  VAL B 130   N  MET A 103
SHEET    6  BA 8 LYS B  19  LEU B  27 -1  O  ASN B  26   N  GLU B 134
SHEET    7  BA 8 GLN B   3  TYR B  10 -1  O  VAL B   4   N  PHE B  25
SHEET    8  BA 8 LYS B 164  LEU B 171 -1  O  LYS B 164   N  GLU B   9
SSBOND   1 CYS A   43    CYS A  168                          1555   1555  2.04
SSBOND   2 CYS B   43    CYS B  168                          1555   1555  2.04
SITE     1 AC1  4 VAL A  32  PRO A  33  LYS A  34  THR A  35
SITE     1 AC2  4 VAL B  32  PRO B  33  LYS B  34  THR B  35
CRYST1   64.829   64.829  156.288  90.00  90.00 120.00 P 31 2 1     12
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      0.015425  0.008906  0.000000        0.00000
SCALE2      0.000000  0.017811  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006398        0.00000
      
PROCHECK
Go to PROCHECK summary
 References