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PDBsum entry 1oca

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Isomerase PDB id
1oca
Jmol
Contents
Protein chain
165 a.a.
HEADER    ISOMERASE                               07-JUL-97   1OCA
TITLE     HUMAN CYCLOPHILIN A, UNLIGATED, NMR, 20 STRUCTURES
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CYCLOPHILIN A;
COMPND   3 CHAIN: A;
COMPND   4 EC: 5.2.1.8;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 CELL: T-CELL (JURKAT);
SOURCE   6 GENE: CYCLOPHILIN;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: W3110CI;
SOURCE  10 EXPRESSION_SYSTEM_GENE: CYCLOPHILIN
KEYWDS    ISOMERASE, PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
EXPDTA    SOLUTION NMR
NUMMDL    20
AUTHOR    M.OTTIGER,O.ZERBE,P.GUNTERT,K.WUTHRICH
REVDAT   2   24-FEB-09 1OCA    1       VERSN
REVDAT   1   19-NOV-97 1OCA    0
JRNL        AUTH   M.OTTIGER,O.ZERBE,P.GUNTERT,K.WUTHRICH
JRNL        TITL   THE NMR SOLUTION CONFORMATION OF UNLIGATED HUMAN
JRNL        TITL 2 CYCLOPHILIN A.
JRNL        REF    J.MOL.BIOL.                   V. 272    64 1997
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   9299338
JRNL        DOI    10.1006/JMBI.1997.1220
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : OPAL
REMARK   3   AUTHORS     : WUTHRICH
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK   3  THE JRNL CITATION ABOVE.
REMARK   4
REMARK   4 1OCA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210  EXPERIMENT TYPE                : NMR
REMARK 210  TEMPERATURE           (KELVIN) : 299
REMARK 210  PH                             : 6.5
REMARK 210  IONIC STRENGTH                 : NULL
REMARK 210  PRESSURE                       : NULL
REMARK 210  SAMPLE CONTENTS                : NULL
REMARK 210
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NOESY, HNHB, HSQC, CBCA (CO)
REMARK 210                                   NH, CT-HNCA, HCCH-TOCSY, CT-
REMARK 210                                   HCCH-COSY, CLEAN-TOCSY, HMBC,
REMARK 210                                   (HB)CB(CGCD)HD, HB(CBCGCD)HD,
REMARK 210                                   TOCSY-RELAYED-CT-HMQC
REMARK 210  SPECTROMETER FIELD STRENGTH    : 750 MHZ, 600 MHZ
REMARK 210  SPECTROMETER MODEL             : UNITYPLUS 750, AMX600
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN, BRUKER
REMARK 210
REMARK 210  STRUCTURE DETERMINATION.
REMARK 210   SOFTWARE USED                 : DIANA
REMARK 210   METHOD USED                   : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA  : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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  6 TYR A  48   CB  -  CG  -  CD2 ANGL. DEV. =  -5.3 DEGREES
REMARK 500  8 ASP A  13   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500 12 TYR A  48   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500 13 TYR A  48   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500 14 TYR A  48   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500 15 TYR A  48   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 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  1 ASP A  13       13.76     55.43
REMARK 500  1 CYS A  52      174.59     62.94
REMARK 500  1 PHE A  60      -79.89   -135.84
REMARK 500  1 HIS A  70       34.32   -152.27
REMARK 500  1 ASN A  71       12.18   -150.72
REMARK 500  1 LYS A  82      161.41     48.38
REMARK 500  1 ASN A 106       48.17     39.14
REMARK 500  1 SER A 110       -5.59   -156.22
REMARK 500  1 LYS A 118       91.96    -64.64
REMARK 500  1 PHE A 129       -0.70   -140.76
REMARK 500  1 SER A 147      -61.51   -146.47
REMARK 500  1 ARG A 148      -38.60    141.75
REMARK 500  2 PHE A  25       52.71    -69.61
REMARK 500  2 PHE A  60      -62.96   -142.03
REMARK 500  2 ARG A  69     -165.90   -117.11
REMARK 500  2 HIS A  70       46.83   -174.22
REMARK 500  2 ASN A  71       20.82   -166.85
REMARK 500  2 GLU A  81     -133.63     62.17
REMARK 500  2 ALA A 101       50.92    -95.00
REMARK 500  2 SER A 110      -47.13   -142.21
REMARK 500  2 THR A 119       72.77   -117.67
REMARK 500  2 LYS A 125      -40.31   -135.53
REMARK 500  2 PHE A 129       -3.83   -145.30
REMARK 500  3 VAL A   2     -172.95     48.15
REMARK 500  3 ASP A  13       14.03     56.07
REMARK 500  3 CYS A  52      161.91    113.90
REMARK 500  3 PHE A  60      -80.36   -140.64
REMARK 500  3 PHE A  67       40.10    -58.52
REMARK 500  3 THR A  68      -12.96   -148.39
REMARK 500  3 HIS A  70       45.21   -169.94
REMARK 500  3 ASN A  71       -7.33   -155.45
REMARK 500  3 THR A  73      -96.01    -91.52
REMARK 500  3 GLU A  81     -139.32    -91.58
REMARK 500  3 ALA A 103       36.49   -146.00
REMARK 500  3 THR A 119       42.22    -81.03
REMARK 500  4 ASP A  13       13.37     53.68
REMARK 500  4 PHE A  60      -78.72   -137.37
REMARK 500  4 THR A  68      -58.39   -125.65
REMARK 500  4 ARG A  69     -158.37   -103.94
REMARK 500  4 HIS A  70       41.04   -168.34
REMARK 500  4 ASN A  71      -51.59   -122.94
REMARK 500  4 GLU A  81     -133.82     34.48
REMARK 500  4 ASN A 102     -169.88    -76.59
REMARK 500  4 ASN A 106       53.02     34.16
REMARK 500  4 THR A 107       23.29   -140.63
REMARK 500  4 SER A 110      -39.87   -147.06
REMARK 500  4 THR A 119       43.40    -74.10
REMARK 500  4 SER A 147      -70.36   -137.80
REMARK 500  4 ARG A 148      -29.28    143.44
REMARK 500  5 ASP A  13       12.94     50.88
REMARK 500  5 LYS A  49      101.71    -59.28
REMARK 500  5 CYS A  52      161.32    105.39
REMARK 500  5 PHE A  60      -78.29   -138.90
REMARK 500  5 THR A  68      -50.72   -121.83
REMARK 500  5 ARG A  69     -149.23   -106.29
REMARK 500  5 HIS A  70       69.36   -171.19
REMARK 500  5 ASN A  71      -77.12   -165.60
REMARK 500  5 THR A  73      -73.47    -83.60
REMARK 500  5 ASP A  85       89.27    -67.67
REMARK 500  5 ASN A 102     -179.25    -68.34
REMARK 500  5 THR A 107       39.58    -92.14
REMARK 500  5 LYS A 118       96.22    -66.92
REMARK 500  5 SER A 147     -103.30   -143.63
REMARK 500  5 ARG A 148      -27.03   -153.70
REMARK 500  6 VAL A   2     -173.40     50.66
REMARK 500  6 ASP A  13       14.04     54.72
REMARK 500  6 PHE A  60      -75.98   -122.90
REMARK 500  6 ASP A  66       46.21    -84.45
REMARK 500  6 ARG A  69     -139.12   -125.06
REMARK 500  6 HIS A  70       23.49   -170.06
REMARK 500  6 GLU A  81     -142.10     33.79
REMARK 500  6 ASN A 108     -154.29    -66.29
REMARK 500  6 THR A 119       58.45    -92.98
REMARK 500  7 ASN A   3      112.40    -36.34
REMARK 500  7 PRO A  16       99.20    -66.95
REMARK 500  7 PHE A  60      -81.26   -140.67
REMARK 500  7 PHE A  67       35.70    -96.29
REMARK 500  7 THR A  68      -67.07   -155.00
REMARK 500  7 ASN A  71        4.70   -167.00
REMARK 500  7 LYS A  82      158.25     63.40
REMARK 500  7 ASN A 102     -179.05    -69.26
REMARK 500  7 SER A 110      -21.68   -155.74
REMARK 500  7 PHE A 129       -0.22   -140.74
REMARK 500  8 VAL A   2     -173.11     50.12
REMARK 500  8 PHE A  25       49.54    -81.13
REMARK 500  8 CYS A  52      167.73    122.85
REMARK 500  8 PHE A  60      -75.57   -129.11
REMARK 500  8 THR A  68      -35.41   -139.15
REMARK 500  8 ASN A  71      -54.05   -164.51
REMARK 500  8 LYS A  82      149.88     52.31
REMARK 500  8 ASN A 102     -169.10   -165.38
REMARK 500  8 ASN A 106       51.04     34.18
REMARK 500  8 THR A 107       13.92   -140.63
REMARK 500  8 ASN A 108       96.61    -57.79
REMARK 500  8 SER A 110      -17.43   -156.29
REMARK 500  8 THR A 119       56.88   -114.21
REMARK 500  8 LYS A 125      -45.11   -138.91
REMARK 500  9 ASP A  13       17.96     58.71
REMARK 500  9 PHE A  25       61.37    -68.97
REMARK 500  9 CYS A  52      164.93     86.00
REMARK 500  9 PHE A  60      -81.89   -146.93
REMARK 500  9 PHE A  67        1.25    -63.34
REMARK 500  9 THR A  68      -69.08   -139.21
REMARK 500  9 HIS A  70       33.77   -148.25
REMARK 500  9 ASN A  71       16.27   -144.96
REMARK 500  9 LYS A  76     -177.34    170.69
REMARK 500  9 GLU A  81     -133.51    -76.24
REMARK 500  9 ASN A 106       14.70     44.93
REMARK 500  9 SER A 110      -11.25   -144.34
REMARK 500  9 CYS A 115       94.42    -66.68
REMARK 500  9 LYS A 125      -34.33   -144.25
REMARK 500 10 VAL A   2     -174.26    -65.86
REMARK 500 10 ASN A   3       99.98    -27.94
REMARK 500 10 ASP A  13       13.69     54.24
REMARK 500 10 PHE A  60      -79.23   -153.55
REMARK 500 10 PHE A  67      -18.02    -33.37
REMARK 500 10 HIS A  70       44.03   -156.17
REMARK 500 10 ASN A  71       -8.36   -140.34
REMARK 500 10 SER A  77       35.20    -89.63
REMARK 500 10 ILE A  78       -3.14     42.10
REMARK 500 10 GLU A  81     -132.91    -68.50
REMARK 500 10 PHE A 129        1.18   -150.24
REMARK 500 10 SER A 147      -81.86   -146.14
REMARK 500 10 ARG A 148      -21.41    169.06
REMARK 500 11 CYS A  52      132.81     67.11
REMARK 500 11 PHE A  60      -81.36   -143.13
REMARK 500 11 ASN A  71       10.14   -140.78
REMARK 500 11 GLU A  81     -156.22    -68.82
REMARK 500 11 ASN A  87      157.58    159.07
REMARK 500 11 LYS A 118       84.87    -64.69
REMARK 500 11 LYS A 125      -56.97   -132.22
REMARK 500 12 ASP A  13       13.95     56.62
REMARK 500 12 LYS A  49      108.91    -52.49
REMARK 500 12 CYS A  52      176.58     60.18
REMARK 500 12 PHE A  60      -76.44   -150.32
REMARK 500 12 HIS A  70       54.00   -164.53
REMARK 500 12 ASN A  71       -1.29   -159.08
REMARK 500 12 GLU A  81     -133.50     37.25
REMARK 500 12 ASN A 106       54.77     33.61
REMARK 500 12 SER A 110      -30.97   -155.92
REMARK 500 12 LYS A 118       89.17    -67.51
REMARK 500 12 LYS A 125      -35.00   -140.11
REMARK 500 13 ASP A  13       13.92     57.04
REMARK 500 13 LYS A  28      -47.89   -130.45
REMARK 500 13 PHE A  60      -79.93   -142.40
REMARK 500 13 HIS A  70       72.01   -159.80
REMARK 500 13 ASN A  71      -10.26   -168.79
REMARK 500 13 GLU A  81     -139.26   -147.72
REMARK 500 13 ALA A 101       57.12    -97.08
REMARK 500 13 ASN A 106       47.27     34.56
REMARK 500 13 LYS A 118       89.82    -67.86
REMARK 500 13 SER A 147      -86.51   -141.62
REMARK 500 13 ARG A 148      -17.40    178.14
REMARK 500 14 VAL A   2      175.46     63.89
REMARK 500 14 ASP A  13       13.94     57.32
REMARK 500 14 PHE A  60      -74.02   -150.89
REMARK 500 14 PHE A  67       -2.36    -41.16
REMARK 500 14 ASN A  71      -22.94   -173.45
REMARK 500 14 GLU A  81     -157.61   -135.13
REMARK 500 14 ASN A 102     -178.18    -65.98
REMARK 500 14 ASN A 106       57.27     34.21
REMARK 500 14 SER A 110      -13.12   -151.01
REMARK 500 14 LYS A 118       88.45    -65.52
REMARK 500 15 VAL A   2     -173.65     48.16
REMARK 500 15 ASP A  13       13.82     58.35
REMARK 500 15 PHE A  25       59.11    -69.04
REMARK 500 15 PHE A  60      -72.89   -133.11
REMARK 500 15 THR A  68      -51.68   -140.03
REMARK 500 15 ASN A  71        2.95   -154.07
REMARK 500 15 SER A  77       23.16    -71.45
REMARK 500 15 ILE A  78      -19.13     46.29
REMARK 500 15 GLU A  81     -132.80     41.23
REMARK 500 15 ALA A 101       59.22   -102.09
REMARK 500 15 ALA A 103       19.84   -147.82
REMARK 500 15 LYS A 118       92.10    -67.83
REMARK 500 16 ASN A   3      109.19    -44.97
REMARK 500 16 LYS A  44        2.49    -67.59
REMARK 500 16 CYS A  52      144.28    130.14
REMARK 500 16 PHE A  60      -79.61   -133.94
REMARK 500 16 THR A  68      -45.95   -137.16
REMARK 500 16 HIS A  70       12.96     54.25
REMARK 500 16 LYS A  76     -178.84   -170.58
REMARK 500 16 LYS A  82      148.42     67.38
REMARK 500 16 THR A 107       41.74   -142.25
REMARK 500 16 SER A 147      -72.06   -142.18
REMARK 500 16 ARG A 148      -27.39    140.67
REMARK 500 17 VAL A   2     -172.70     46.65
REMARK 500 17 PHE A  60      -75.64   -136.57
REMARK 500 17 HIS A  70       53.81   -145.11
REMARK 500 17 ASN A  71      -67.37   -152.91
REMARK 500 17 GLU A  81     -133.80     34.06
REMARK 500 17 SER A 110      -13.76   -144.54
REMARK 500 17 LYS A 118       89.85    -68.59
REMARK 500 17 LYS A 125      -52.01   -127.22
REMARK 500 17 SER A 147      -96.05   -142.59
REMARK 500 17 ARG A 148      -23.40   -162.20
REMARK 500 18 VAL A   2     -174.26    -69.11
REMARK 500 18 ASN A   3      104.79    -33.83
REMARK 500 18 ASP A  13       13.76     53.50
REMARK 500 18 LYS A  28      -25.25   -145.82
REMARK 500 18 CYS A  52      175.99     56.38
REMARK 500 18 PHE A  60      -83.89   -125.10
REMARK 500 18 THR A  68      -31.57   -136.60
REMARK 500 18 ASN A  71      -27.52   -147.04
REMARK 500 18 SER A  77       44.93    -84.89
REMARK 500 18 ILE A  78      -43.59     49.27
REMARK 500 18 GLU A  81     -133.23   -127.84
REMARK 500 18 ASN A  87      156.42    167.72
REMARK 500 18 ALA A 101       41.79    -77.62
REMARK 500 18 ASN A 106       24.43     48.85
REMARK 500 18 LYS A 118       93.22    -66.54
REMARK 500 18 LYS A 125      -51.91   -137.04
REMARK 500 19 VAL A   2      179.35     52.42
REMARK 500 19 ASP A  13       13.07     57.44
REMARK 500 19 CYS A  52      170.29     47.11
REMARK 500 19 PHE A  60      -76.29   -134.56
REMARK 500 19 THR A  68      -60.66   -139.29
REMARK 500 19 ASN A  71       -0.90   -162.46
REMARK 500 19 SER A  77       22.57    -73.74
REMARK 500 19 ILE A  78      -22.39     49.16
REMARK 500 19 GLU A  81     -132.57     50.10
REMARK 500 19 ASN A 106       43.91     37.67
REMARK 500 19 SER A 110       33.88   -145.77
REMARK 500 19 LYS A 118       96.42    -68.47
REMARK 500 20 ASN A   3       98.24    -29.08
REMARK 500 20 ASP A  13       14.39     58.68
REMARK 500 20 LYS A  44        1.62    -68.06
REMARK 500 20 CYS A  52      144.64    106.76
REMARK 500 20 PHE A  60      -68.80   -143.07
REMARK 500 20 THR A  68      -67.91   -122.98
REMARK 500 20 HIS A  70       -3.81     60.45
REMARK 500 20 GLU A  81     -137.80   -132.44
REMARK 500 20 ASN A 106       48.71     33.62
REMARK 500 20 SER A 110      -28.86   -146.50
REMARK 500 20 THR A 119       40.67    -74.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 MET A    1     VAL A    2         19      -142.97
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  1 PHE A  36         0.09    SIDE_CHAIN
REMARK 500  1 ARG A  69         0.09    SIDE_CHAIN
REMARK 500  1 ARG A 144         0.09    SIDE_CHAIN
REMARK 500  2 ARG A  37         0.10    SIDE_CHAIN
REMARK 500  2 ARG A  55         0.10    SIDE_CHAIN
REMARK 500  3 ARG A  37         0.08    SIDE_CHAIN
REMARK 500  3 ARG A  55         0.12    SIDE_CHAIN
REMARK 500  4 TYR A  48         0.09    SIDE_CHAIN
REMARK 500  5 ARG A  19         0.10    SIDE_CHAIN
REMARK 500  5 ARG A  55         0.11    SIDE_CHAIN
REMARK 500  5 ARG A  69         0.10    SIDE_CHAIN
REMARK 500  5 PHE A 112         0.09    SIDE_CHAIN
REMARK 500  6 ARG A  55         0.16    SIDE_CHAIN
REMARK 500  7 ARG A  69         0.08    SIDE_CHAIN
REMARK 500  8 TYR A  48         0.08    SIDE_CHAIN
REMARK 500  9 TYR A  48         0.07    SIDE_CHAIN
REMARK 500  9 ARG A  55         0.09    SIDE_CHAIN
REMARK 500 10 ARG A  19         0.11    SIDE_CHAIN
REMARK 500 10 TYR A  48         0.19    SIDE_CHAIN
REMARK 500 10 ARG A  69         0.08    SIDE_CHAIN
REMARK 500 11 TYR A  48         0.07    SIDE_CHAIN
REMARK 500 11 ARG A 144         0.08    SIDE_CHAIN
REMARK 500 12 ARG A  19         0.09    SIDE_CHAIN
REMARK 500 12 TYR A  48         0.08    SIDE_CHAIN
REMARK 500 12 ARG A  69         0.15    SIDE_CHAIN
REMARK 500 12 PHE A 112         0.10    SIDE_CHAIN
REMARK 500 13 TYR A  48         0.12    SIDE_CHAIN
REMARK 500 13 ARG A  55         0.12    SIDE_CHAIN
REMARK 500 14 TYR A  48         0.07    SIDE_CHAIN
REMARK 500 16 TYR A  48         0.07    SIDE_CHAIN
REMARK 500 17 ARG A  55         0.10    SIDE_CHAIN
REMARK 500 17 ARG A  69         0.10    SIDE_CHAIN
REMARK 500 19 ARG A  19         0.08    SIDE_CHAIN
REMARK 500 19 ARG A  69         0.08    SIDE_CHAIN
REMARK 500 20 ARG A  19         0.08    SIDE_CHAIN
REMARK 500 20 PHE A  36         0.09    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF  1OCA A    2   165  UNP    P62937   PPIA_HUMAN       1    164
SEQRES   1 A  165  MET VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP
SEQRES   2 A  165  GLY GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA
SEQRES   3 A  165  ASP LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU
SEQRES   4 A  165  SER THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS
SEQRES   5 A  165  PHE HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY
SEQRES   6 A  165  ASP PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE
SEQRES   7 A  165  TYR GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS
SEQRES   8 A  165  HIS THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY
SEQRES   9 A  165  PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA
SEQRES  10 A  165  LYS THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY
SEQRES  11 A  165  LYS VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU
SEQRES  12 A  165  ARG PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE
SEQRES  13 A  165  THR ILE ALA ASP CYS GLY GLN LEU GLU
HELIX    1   1 PRO A   30  THR A   41  1                                  12
HELIX    2   2 GLU A  120  LEU A  122  5                                   3
HELIX    3   3 MET A  136  PHE A  145  1                                  10
SHEET    1   A 8 ILE A 156  GLN A 163  0
SHEET    2   A 8 THR A   5  VAL A  12 -1  N  ALA A  11   O  THR A 157
SHEET    3   A 8 GLU A  15  LEU A  24 -1  N  PHE A  22   O  VAL A   6
SHEET    4   A 8 VAL A 127  GLU A 134 -1  N  GLU A 134   O  SER A  21
SHEET    5   A 8 ILE A  97  MET A 100 -1  N  MET A 100   O  VAL A 127
SHEET    6   A 8 PHE A 112  CYS A 115 -1  N  PHE A 113   O  SER A  99
SHEET    7   A 8 MET A  61  GLY A  64 -1  N  GLY A  64   O  PHE A 112
SHEET    8   A 8 PHE A  53  ILE A  57 -1  N  ILE A  57   O  MET A  61
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1
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      1.000000  0.000000  0.000000        0.00000
SCALE2      0.000000  1.000000  0.000000        0.00000
SCALE3      0.000000  0.000000  1.000000        0.00000
      
PROCHECK
Go to PROCHECK summary
 References