Header list of 1oca.pdb file
Complete list - b 23 2 Bytes
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 3 23-FEB-22 1OCA 1 REMARK
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 CYCLOPHILIN
JRNL TITL 2 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 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 THE
REMARK 3 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 100 THE DEPOSITION ID IS D_1000175426.
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)NH;
REMARK 210 CT-HNCA; HCCH-TOCSY; CT-HCCH-
REMARK 210 COSY; CLEAN-TOCSY; HMBC; (HB)
REMARK 210 CB(CGCD)HD; HB(CBCGCD)HD; TOCSY-
REMARK 210 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 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 APPLY THE FOLLOWING TO CHAINS: A
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HG1 THR A 116 OE2 GLU A 143 1.51
REMARK 500 HG1 THR A 5 OE1 GLU A 23 1.56
REMARK 500 O GLY A 47 HG SER A 51 1.57
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 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
REMARK 500 THIS ENTRY HAS 235 RAMACHANDRAN OUTLIERS.
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
MODEL 1
Complete list - b 23 2 Bytes