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PDBsum entry 2x25

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Isomerase PDB id
2x25
Jmol
Contents
Protein chain
168 a.a.
Waters ×443
HEADER    ISOMERASE                               11-JAN-10   2X25
TITLE     FREE ACETYL-CYPA ORTHORHOMBIC FORM
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A;
COMPND   3 CHAIN: B;
COMPND   4 SYNONYM: PPIASE A, ROTAMASE A, CYCLOPHILIN A, CYCLOSPORIN
COMPND   5  A-BINDING PROTEIN, CYPA;
COMPND   6 EC: 5.2.1.8
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606
KEYWDS    HIV-1, ISOMERASE, HOST-VIRUS INTERACTION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.LAMMERS,H.NEUMANN,J.W.CHIN,L.C.JAMES
REVDAT   2   15-JUN-11 2X25    1       JRNL   REMARK DBREF  SEQADV
REVDAT   1   23-MAR-10 2X25    0
JRNL        AUTH   M.LAMMERS,H.NEUMANN,J.W.CHIN,L.C.JAMES
JRNL        TITL   ACETYLATION REGULATES CYCLOPHILIN A CATALYSIS,
JRNL        TITL 2 IMMUNOSUPPRESSION AND HIV ISOMERIZATION.
JRNL        REF    NAT.CHEM.BIOL.                V.   6   331 2010
JRNL        REFN                   ISSN 1552-4450
JRNL        PMID   20364129
JRNL        DOI    10.1038/NCHEMBIO.342
REMARK   2
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0088
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.19
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.30
REMARK   3   NUMBER OF REFLECTIONS             : 58489
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) : 0.12756
REMARK   3   R VALUE            (WORKING SET) : 0.12607
REMARK   3   FREE R VALUE                     : 0.15568
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1
REMARK   3   FREE R VALUE TEST SET COUNT      : 3128
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) : 1.200
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.231
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4242
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.86
REMARK   3   BIN R VALUE           (WORKING SET) : 0.156
REMARK   3   BIN FREE R VALUE SET COUNT          : 236
REMARK   3   BIN FREE R VALUE                    : 0.184
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1289
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 12
REMARK   3   SOLVENT ATOMS            : 443
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 17.3
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.4
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.43
REMARK   3    B22 (A**2) : 0.63
REMARK   3    B33 (A**2) : -0.20
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.00
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.031
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.033
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.018
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.856
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1332 ; 0.033 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):   932 ; 0.009 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1783 ; 2.408 ; 1.927
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2243 ; 1.227 ; 3.002
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   165 ; 6.110 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    62 ;32.007 ;23.710
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   221 ;12.424 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;16.831 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   182 ; 0.159 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1497 ; 0.014 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   291 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   820 ; 2.397 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   352 ; 1.017 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1305 ; 3.247 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   512 ; 4.432 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   478 ; 5.753 ; 4.500
REMARK   3
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2264 ; 2.366 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   443 ;11.205 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2233 ; 4.679 ; 3.000
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  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3   RIDING POSITIONS.
REMARK   4
REMARK   4 2X25 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-10.
REMARK 100 THE PDBE ID CODE IS EBI-42416.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 287
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62683
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.20
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5
REMARK 200  DATA REDUNDANCY                : 3
REMARK 200  R MERGE                    (I) : 0.09
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 5.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       21.11100
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.61800
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.20200
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.61800
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.11100
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.20200
REMARK 290   SMTRY3   4  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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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     GLU B   165
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   CD   LYS B   120     O    HOH B  2348              1.59
REMARK 500   OE2  GLU B   134     O    HOH B  2375              2.12
REMARK 500   O    HOH B  2002     O    HOH B  2020              1.24
REMARK 500   O    HOH B  2014     O    HOH B  2040              1.43
REMARK 500   O    HOH B  2014     O    HOH B  2055              2.14
REMARK 500   O    HOH B  2015     O    HOH B  2124              1.73
REMARK 500   O    HOH B  2016     O    HOH B  2167              1.20
REMARK 500   O    HOH B  2023     O    HOH B  2085              1.64
REMARK 500   O    HOH B  2024     O    HOH B  2084              1.46
REMARK 500   O    HOH B  2043     O    HOH B  2044              1.75
REMARK 500   O    HOH B  2044     O    HOH B  2056              1.78
REMARK 500   O    HOH B  2055     O    HOH B  2443              0.90
REMARK 500   O    HOH B  2056     O    HOH B  2146              2.00
REMARK 500   O    HOH B  2065     O    HOH B  2279              2.14
REMARK 500   O    HOH B  2066     O    HOH B  2161              2.18
REMARK 500   O    HOH B  2069     O    HOH B  2202              0.71
REMARK 500   O    HOH B  2072     O    HOH B  2073              0.56
REMARK 500   O    HOH B  2076     O    HOH B  2211              1.66
REMARK 500   O    HOH B  2077     O    HOH B  2416              1.45
REMARK 500   O    HOH B  2083     O    HOH B  2425              2.03
REMARK 500   O    HOH B  2084     O    HOH B  2085              2.00
REMARK 500   O    HOH B  2092     O    HOH B  2239              1.88
REMARK 500   O    HOH B  2093     O    HOH B  2240              2.18
REMARK 500   O    HOH B  2096     O    HOH B  2097              1.70
REMARK 500   O    HOH B  2113     O    HOH B  2319              2.04
REMARK 500   O    HOH B  2120     O    HOH B  2277              1.85
REMARK 500   O    HOH B  2122     O    HOH B  2123              1.08
REMARK 500   O    HOH B  2130     O    HOH B  2131              2.13
REMARK 500   O    HOH B  2140     O    HOH B  2141              0.85
REMARK 500   O    HOH B  2140     O    HOH B  2308              1.96
REMARK 500   O    HOH B  2146     O    HOH B  2148              1.07
REMARK 500   O    HOH B  2149     O    HOH B  2152              1.74
REMARK 500   O    HOH B  2152     O    HOH B  2284              2.12
REMARK 500   O    HOH B  2153     O    HOH B  2156              0.79
REMARK 500   O    HOH B  2154     O    HOH B  2155              0.47
REMARK 500   O    HOH B  2159     O    HOH B  2166              2.19
REMARK 500   O    HOH B  2160     O    HOH B  2162              0.68
REMARK 500   O    HOH B  2161     O    HOH B  2163              0.93
REMARK 500   O    HOH B  2168     O    HOH B  2345              2.08
REMARK 500   O    HOH B  2171     O    HOH B  2172              0.60
REMARK 500   O    HOH B  2173     O    HOH B  2350              2.07
REMARK 500   O    HOH B  2173     O    HOH B  2176              2.07
REMARK 500   O    HOH B  2177     O    HOH B  2186              0.71
REMARK 500   O    HOH B  2179     O    HOH B  2180              1.64
REMARK 500   O    HOH B  2184     O    HOH B  2434              1.46
REMARK 500   O    HOH B  2188     O    HOH B  2191              1.28
REMARK 500   O    HOH B  2201     O    HOH B  2212              1.07
REMARK 500   O    HOH B  2208     O    HOH B  2209              1.64
REMARK 500   O    HOH B  2211     O    HOH B  2213              1.91
REMARK 500   O    HOH B  2216     O    HOH B  2218              1.86
REMARK 500
REMARK 500 THIS ENTRY HAS     103 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH B  2007     O    HOH B  2097     1655     1.29
REMARK 500   O    HOH B  2009     O    HOH B  2081     1655     1.49
REMARK 500   O    HOH B  2012     O    HOH B  2389     1655     0.54
REMARK 500   O    HOH B  2020     O    HOH B  2420     1655     1.65
REMARK 500   O    HOH B  2025     O    HOH B  2114     3554     1.66
REMARK 500   O    HOH B  2029     O    HOH B  2392     1655     2.16
REMARK 500   O    HOH B  2029     O    HOH B  2206     1655     2.10
REMARK 500   O    HOH B  2051     O    HOH B  2326     4545     2.15
REMARK 500   O    HOH B  2095     O    HOH B  2114     3554     2.10
REMARK 500   O    HOH B  2125     O    HOH B  2243     4545     1.80
REMARK 500   O    HOH B  2129     O    HOH B  2158     4545     1.38
REMARK 500   O    HOH B  2131     O    HOH B  2240     4545     1.39
REMARK 500   O    HOH B  2138     O    HOH B  2242     4545     1.31
REMARK 500   O    HOH B  2151     O    HOH B  2361     4545     1.95
REMARK 500   O    HOH B  2158     O    HOH B  2297     4445     2.17
REMARK 500   O    HOH B  2203     O    HOH B  2380     3544     0.74
REMARK 500   O    HOH B  2213     O    HOH B  2384     3544     1.69
REMARK 500   O    HOH B  2217     O    HOH B  2375     3544     1.78
REMARK 500   O    HOH B  2243     O    HOH B  2288     4445     1.89
REMARK 500   O    HOH B  2284     O    HOH B  2351     4545     2.20
REMARK 500   O    HOH B  2360     O    HOH B  2401     4545     2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    HIS B   1   CB    HIS B   1   CG     -0.117
REMARK 500    LYS B  82   CB    LYS B  82   CG     -0.592
REMARK 500    GLU B 134   CB    GLU B 134   CG     -0.134
REMARK 500    MET B 142   CG    MET B 142   SD      0.256
REMARK 500    GLU B 143   CB    GLU B 143   CG     -0.120
REMARK 500    LYS B 154   CD    LYS B 154   CE      0.343
REMARK 500    LYS B 154   CE    LYS B 154   NZ     -0.199
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  27   CB  -  CG  -  OD1 ANGL. DEV. =   7.8 DEGREES
REMARK 500    ARG B  55   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.9 DEGREES
REMARK 500    ARG B  55   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 DEGREES
REMARK 500    HIS B 126   CB  -  CG  -  ND1 ANGL. DEV. =  10.1 DEGREES
REMARK 500    LYS B 131   CD  -  CE  -  NZ  ANGL. DEV. = -16.7 DEGREES
REMARK 500    LYS B 154   CD  -  CE  -  NZ  ANGL. DEV. = -45.0 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 B  60      -72.35   -127.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    HIS B   1         0.12    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VBS   RELATED DB: PDB
REMARK 900  STRUCTURE OF CYCLOPHILIN COMPLEXED WITH (D)
REMARK 900  ALA CONTAINING TETRAPEPTIDE
REMARK 900 RELATED ID: 1OCA   RELATED DB: PDB
REMARK 900  HUMAN CYCLOPHILIN A, UNLIGATED, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1MF8   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CALCINEURIN
REMARK 900  COMPLEXED WITHCYCLOSPORIN A AND HUMAN CYCLOPHILIN
REMARK 900 RELATED ID: 2CYH   RELATED DB: PDB
REMARK 900  CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO
REMARK 900 RELATED ID: 1CWB   RELATED DB: PDB
REMARK 900 RELATED ID: 1VBT   RELATED DB: PDB
REMARK 900  STRUCTURE OF CYCLOPHILIN COMPLEXED WITH SULFUR
REMARK 900  -SUBSTITUTED TETRAPEPTIDE AAPF
REMARK 900 RELATED ID: 1M9E   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/
REMARK 900  HIV-1 CA N-TERMINAL DOMAIN (1-146) M-
REMARK 900  TYPE H87A COMPLEX.
REMARK 900 RELATED ID: 1CWL   RELATED DB: PDB
REMARK 900  HUMAN CYCLOPHILIN A COMPLEXED WITH 4 4-
REMARK 900  HYDROXY-MELEU CYCLOSPORIN
REMARK 900 RELATED ID: 1CWC   RELATED DB: PDB
REMARK 900 RELATED ID: 1CWI   RELATED DB: PDB
REMARK 900  HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3
REMARK 900  -(N-METHYL)-D-ALANINE CYCLOSPORIN
REMARK 900 RELATED ID: 1CWO   RELATED DB: PDB
REMARK 900  HUMAN CYCLOPHILIN A COMPLEXED WITH THR2,
REMARK 900  LEU5, D-HIV8, LEU10 CYCLOSPORIN
REMARK 900 RELATED ID: 1RMH   RELATED DB: PDB
REMARK 900  RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL
REMARK 900 RELATED ID: 1CWJ   RELATED DB: PDB
REMARK 900  HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3
REMARK 900  -S-METHYL-SARCOSINE CYCLOSPORIN
REMARK 900 RELATED ID: 2RMB   RELATED DB: PDB
REMARK 900  CYCLOPHILIN A COMPLEXED WITH DIMETHYL-
REMARK 900  CYCLOSPORIN A
REMARK 900 RELATED ID: 1M9C   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/
REMARK 900  HIV-1 CA N-TERMINAL DOMAIN (1-146) M-
REMARK 900  TYPE COMPLEX.
REMARK 900 RELATED ID: 1CWA   RELATED DB: PDB
REMARK 900 RELATED ID: 1CWF   RELATED DB: PDB
REMARK 900  HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL
REMARK 900  CYCLOSPORIN
REMARK 900 RELATED ID: 1M9Y   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/
REMARK 900  HIV-1 CA N-TERMINAL DOMAIN (1-146) M-
REMARK 900  TYPE H87A,G89A COMPLEX.
REMARK 900 RELATED ID: 3CYH   RELATED DB: PDB
REMARK 900  CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE SER-PRO
REMARK 900 RELATED ID: 1M9F   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/
REMARK 900  HIV-1 CA N-TERMINAL DOMAIN (1-146) M-
REMARK 900  TYPE H87A,A88M COMPLEX.
REMARK 900 RELATED ID: 4CYH   RELATED DB: PDB
REMARK 900  CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE HIS-PRO
REMARK 900 RELATED ID: 1CWH   RELATED DB: PDB
REMARK 900  HUMAN CYCLOPHILIN A COMPLEXED WITH 3-D-SER
REMARK 900   CYCLOSPORIN
REMARK 900 RELATED ID: 1BCK   RELATED DB: PDB
REMARK 900  HUMAN CYCLOPHILIN A COMPLEXED WITH 2-THR
REMARK 900  CYCLOSPORIN
REMARK 900 RELATED ID: 1W8V   RELATED DB: PDB
REMARK 900  ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF
REMARK 900  NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES
REMARK 900 RELATED ID: 1AWR   RELATED DB: PDB
REMARK 900  CYPA COMPLEXED WITH HAGPIA
REMARK 900 RELATED ID: 1NMK   RELATED DB: PDB
REMARK 900  THE SANGLIFEHRIN-CYCLOPHILIN INTERACTION:
REMARK 900  DEGRADATION WORK,SYNTHETIC MACROCYCLIC ANALOGUES
REMARK 900  , X-RAY CRYSTAL STRUCTUREAND BINDING DATA
REMARK 900 RELATED ID: 1MIK   RELATED DB: PDB
REMARK 900 RELATED ID: 1AWV   RELATED DB: PDB
REMARK 900  CYPA COMPLEXED WITH HVGPIA
REMARK 900 RELATED ID: 1M9D   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/
REMARK 900  HIV-1 CA N-TERMINAL DOMAIN (1-146) O-
REMARK 900  TYPE CHIMERA COMPLEX.
REMARK 900 RELATED ID: 1AWT   RELATED DB: PDB
REMARK 900  SECYPA COMPLEXED WITH HAGPIA
REMARK 900 RELATED ID: 2CPL   RELATED DB: PDB
REMARK 900  CYCLOPHILIN A
REMARK 900 RELATED ID: 1FGL   RELATED DB: PDB
REMARK 900  CYCLOPHILIN A COMPLEXED WITH A FRAGMENT OF
REMARK 900  HIV-1 GAGPROTEIN
REMARK 900 RELATED ID: 1M9X   RELATED DB: PDB
REMARK 900  X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/
REMARK 900  HIV-1 CA N-TERMINAL DOMAIN (1-146) M-
REMARK 900  TYPE H87A,A88M,G89A COMPLEX.
REMARK 900 RELATED ID: 1M63   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF CALCINEURIN-CYCLOPHILIN-
REMARK 900  CYCLOSPORINSHOWS COMMON BUT DISTINCT RECOGNITION
REMARK 900   OF IMMUNOPHILIN-DRUGCOMPLEXES
REMARK 900 RELATED ID: 1CWK   RELATED DB: PDB
REMARK 900  HUMAN CYCLOPHILIN A COMPLEXED WITH 1-(6,7
REMARK 900  -DIHYDRO)MEBMT 2-VAL 3-D-(2-S-METHYL)
REMARK 900  SARCOSINE CYCLOSPORIN
REMARK 900 RELATED ID: 5CYH   RELATED DB: PDB
REMARK 900  CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-PRO
REMARK 900 RELATED ID: 1AK4   RELATED DB: PDB
REMARK 900  HUMAN CYCLOPHILIN A BOUND TO THE AMINO-
REMARK 900  TERMINAL DOMAIN OF HIV-1 CAPSID
REMARK 900 RELATED ID: 3CYS   RELATED DB: PDB
REMARK 900  CYCLOPHILIN A COMPLEXED WITH CYCLOSPORIN A
REMARK 900  (NMR, 22 STRUCTURES)
REMARK 900 RELATED ID: 2ALF   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN CYPA MUTANT K131A
REMARK 900 RELATED ID: 1AWS   RELATED DB: PDB
REMARK 900  SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC
REMARK 900   MONOMER)
REMARK 900 RELATED ID: 1W8L   RELATED DB: PDB
REMARK 900  ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF
REMARK 900  NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES
REMARK 900 RELATED ID: 1AWU   RELATED DB: PDB
REMARK 900  CYPA COMPLEXED WITH HVGPIA (PSEUDO-SYMMETRIC
REMARK 900  MONOMER)
REMARK 900 RELATED ID: 1W8M   RELATED DB: PDB
REMARK 900  ENZYMATIC AND STRUCTURAL CHARACTERISATION OF
REMARK 900  NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES
REMARK 900 RELATED ID: 2RMA   RELATED DB: PDB
REMARK 900  CYCLOPHILIN A COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 1CWM   RELATED DB: PDB
REMARK 900  HUMAN CYCLOPHILIN A COMPLEXED WITH 4 MEILE
REMARK 900  CYCLOSPORIN
REMARK 900 RELATED ID: 1AWQ   RELATED DB: PDB
REMARK 900  CYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC
REMARK 900  MONOMER)
REMARK 900 RELATED ID: 2X2D   RELATED DB: PDB
REMARK 900  ACETYL-CYPA:HIV-1 N-TERM CAPSID DOMAIN COMPLEX
REMARK 900 RELATED ID: 2X2A   RELATED DB: PDB
REMARK 900  FREE ACETYL-CYPA TRIGONAL FORM
REMARK 900 RELATED ID: 2X2C   RELATED DB: PDB
REMARK 900  ACETYL-CYPA:CYCLOSPORINE COMPLEX
DBREF  2X25 B    2   165  UNP    P62937   PPIA_HUMAN       2    165
SEQADV 2X25 HIS B   -3  UNP  P62937              EXPRESSION TAG
SEQADV 2X25 HIS B   -2  UNP  P62937              EXPRESSION TAG
SEQADV 2X25 HIS B   -1  UNP  P62937              EXPRESSION TAG
SEQADV 2X25 HIS B    0  UNP  P62937              EXPRESSION TAG
SEQADV 2X25 HIS B    1  UNP  P62937              EXPRESSION TAG
SEQADV 2X25 LYS B  120  UNP  P62937    GLU   120 CONFLICT
SEQRES   1 B  169  HIS HIS HIS HIS HIS VAL ASN PRO THR VAL PHE PHE ASP
SEQRES   2 B  169  ILE ALA VAL ASP GLY GLU PRO LEU GLY ARG VAL SER PHE
SEQRES   3 B  169  GLU LEU PHE ALA ASP LYS VAL PRO LYS THR ALA GLU ASN
SEQRES   4 B  169  PHE ARG ALA LEU SER THR GLY GLU LYS GLY PHE GLY TYR
SEQRES   5 B  169  LYS GLY SER CYS PHE HIS ARG ILE ILE PRO GLY PHE MET
SEQRES   6 B  169  CYS GLN GLY GLY ASP PHE THR ARG HIS ASN GLY THR GLY
SEQRES   7 B  169  GLY LYS SER ILE TYR GLY GLU LYS PHE GLU ASP GLU ASN
SEQRES   8 B  169  PHE ILE LEU LYS HIS THR GLY PRO GLY ILE LEU SER MET
SEQRES   9 B  169  ALA ASN ALA GLY PRO ASN THR ASN GLY SER GLN PHE PHE
SEQRES  10 B  169  ILE CYS THR ALA LYS THR LYS TRP LEU ASP GLY ALY HIS
SEQRES  11 B  169  VAL VAL PHE GLY LYS VAL LYS GLU GLY MET ASN ILE VAL
SEQRES  12 B  169  GLU ALA MET GLU ARG PHE GLY SER ARG ASN GLY LYS THR
SEQRES  13 B  169  SER LYS LYS ILE THR ILE ALA ASP CYS GLY GLN LEU GLU
MODRES 2X25 ALY B  125  LYS  N(6)-ACETYLLYSINE
HET    ALY  B 125      12
HETNAM     ALY N(6)-ACETYLLYSINE
FORMUL   2  ALY    C8 H16 N2 O3
FORMUL   3  HOH   *443(H2 O)
HELIX    1   1 VAL B   29  GLY B   42  1                                  14
HELIX    2   2 THR B  119  ASP B  123  5                                   5
HELIX    3   3 GLY B  135  ARG B  144  1                                  10
SHEET    1  BA 8 PHE B  53  ILE B  57  0
SHEET    2  BA 8 MET B  61  GLY B  64 -1  O  MET B  61   N  ILE B  57
SHEET    3  BA 8 PHE B 112  CYS B 115 -1  O  PHE B 112   N  GLY B  64
SHEET    4  BA 8 ILE B  97  MET B 100 -1  O  ILE B  97   N  CYS B 115
SHEET    5  BA 8 VAL B 128  GLU B 134 -1  N  PHE B 129   O  LEU B  98
SHEET    6  BA 8 GLU B  15  LEU B  24 -1  O  SER B  21   N  LYS B 133
SHEET    7  BA 8 THR B   5  VAL B  12 -1  O  VAL B   6   N  PHE B  22
SHEET    8  BA 8 ILE B 156  LEU B 164 -1  O  THR B 157   N  ALA B  11
LINK         C   GLY B 124                 N   ALY B 125     1555   1555  1.33
LINK         C   ALY B 125                 N   HIS B 126     1555   1555  1.32
CRYST1   42.222   52.404   89.236  90.00  90.00  90.00 P 21 21 21    4
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      0.023684  0.000000  0.000000        0.00000
SCALE2      0.000000  0.019083  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011206        0.00000
      
PROCHECK
Go to PROCHECK summary
 References