HEADER COMPLEX (ISOMERASE/PEPTIDE) 05-OCT-97 1AWV
TITLE CYPA COMPLEXED WITH HVGPIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLOPHILIN A;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 5.2.1.8;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PEPTIDE FROM THE HIV-1 CAPSID PROTEIN;
COMPND 8 CHAIN: G, H, I, J, K, L;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 6 GENE: CYCLOPHILIN;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_GENE: CYCLOPHILIN;
SOURCE 10 MOL_ID: 2
KEYWDS COMPLEX (ISOMERASE-PEPTIDE), CYCLOPHILIN A, HIV-1 CAPSID, PSEUDO-
KEYWDS 2 SYMMETRY, COMPLEX (ISOMERASE-PEPTIDE) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.F.VAJDOS
REVDAT 3 02-AUG-23 1AWV 1 REMARK
REVDAT 2 24-FEB-09 1AWV 1 VERSN
REVDAT 1 18-MAR-98 1AWV 0
JRNL AUTH F.F.VAJDOS,S.YOO,M.HOUSEWEART,W.I.SUNDQUIST,C.P.HILL
JRNL TITL CRYSTAL STRUCTURE OF CYCLOPHILIN A COMPLEXED WITH A BINDING
JRNL TITL 2 SITE PEPTIDE FROM THE HIV-1 CAPSID PROTEIN.
JRNL REF PROTEIN SCI. V. 6 2297 1997
JRNL REFN ISSN 0961-8368
JRNL PMID 9385632
REMARK 2
REMARK 2 RESOLUTION. 2.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 83.1
REMARK 3 NUMBER OF REFLECTIONS : 35605
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 SET) : 0.358
REMARK 3 FREE R VALUE : 0.460
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1781
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.34
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5004
REMARK 3 BIN R VALUE (WORKING SET) : 0.4130
REMARK 3 BIN FREE R VALUE : 0.4480
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 270
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7800
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 175
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.60
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) : 0.47
REMARK 3 ESD FROM SIGMAA (A) : 0.44
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.66
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.46
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.330
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.210 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.930 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.350 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.870 ; 2.500
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : TIP3P.PARAMETER
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TIP3P.TOPOLOGY
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 3
REMARK 3 THE HIGH R-VALUE FOR THIS STRUCTURE STEMS FROM THE EXTREME
REMARK 3 NON-RANDOM DISTRIBUTION OF STRUCTURE FACTOR AMPLITUDES IN
REMARK 3 THE DATA.
REMARK 4
REMARK 4 1AWV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171354.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : FEB-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 42633
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29400
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2CYH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
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 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 95.20000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 47.60000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 142.80000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, K
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, J
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, L
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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 GLY G 103
REMARK 475 PRO G 104
REMARK 475 GLY K 103
REMARK 475 PRO K 104
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 PRO B1105 C - N - CA ANGL. DEV. = 12.2 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 GLU A1043 24.04 -54.00
REMARK 500 PHE A1060 -73.98 -100.27
REMARK 500 HIS A1070 12.96 48.76
REMARK 500 GLU A1081 -109.35 -78.91
REMARK 500 GLU A1086 -51.61 -26.04
REMARK 500 ASN A1106 30.00 71.21
REMARK 500 SER A1110 -16.91 -143.17
REMARK 500 PHE A1145 63.98 -106.88
REMARK 500 PRO B1004 138.26 -38.40
REMARK 500 ASP B1013 78.65 66.27
REMARK 500 VAL B1029 70.95 -115.17
REMARK 500 ARG B1037 -80.96 -70.55
REMARK 500 PHE B1046 -133.81 -119.87
REMARK 500 LYS B1049 103.77 -46.95
REMARK 500 PHE B1060 -76.59 -102.86
REMARK 500 HIS B1070 -55.52 70.19
REMARK 500 GLU B1081 -17.71 -177.17
REMARK 500 GLU B1086 -50.54 -1.78
REMARK 500 ASN B1087 -172.57 -171.35
REMARK 500 PHE B1088 44.98 -143.23
REMARK 500 ALA B1103 65.23 -118.62
REMARK 500 PRO B1105 131.99 -13.25
REMARK 500 THR B1107 45.73 -154.40
REMARK 500 ALA B1117 175.79 179.58
REMARK 500 PHE B1145 40.55 -101.63
REMARK 500 ASP C1013 -4.03 62.94
REMARK 500 PHE C1025 70.69 -109.44
REMARK 500 GLU C1043 25.71 -75.65
REMARK 500 PHE C1060 -75.56 -105.75
REMARK 500 GLU C1081 -79.43 -143.16
REMARK 500 HIS C1092 72.28 -68.61
REMARK 500 ALA C1103 49.76 -109.71
REMARK 500 ASN C1106 36.20 70.64
REMARK 500 ALA C1117 170.18 179.72
REMARK 500 SER C1147 -164.53 -104.88
REMARK 500 LYS C1151 132.14 -18.12
REMARK 500 ASP D1013 70.97 66.20
REMARK 500 LYS D1028 -73.11 -95.86
REMARK 500 VAL D1029 74.82 -100.86
REMARK 500 PHE D1046 -139.53 -128.94
REMARK 500 LYS D1049 106.97 -56.05
REMARK 500 PHE D1060 -79.02 -105.45
REMARK 500 THR D1068 -61.46 -99.31
REMARK 500 LYS D1076 140.73 -172.06
REMARK 500 TYR D1079 -125.45 -109.84
REMARK 500 GLU D1081 -36.40 -143.39
REMARK 500 PHE D1083 147.72 178.87
REMARK 500 ASP D1085 98.80 -65.85
REMARK 500 ASN D1087 -159.10 -161.29
REMARK 500 PHE D1088 43.62 -155.05
REMARK 500
REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AWV A 1002 1165 UNP P62937 PPIA_HUMAN 1 164
DBREF 1AWV B 1002 1165 UNP P62937 PPIA_HUMAN 1 164
DBREF 1AWV C 1002 1165 UNP P62937 PPIA_HUMAN 1 164
DBREF 1AWV D 1002 1165 UNP P62937 PPIA_HUMAN 1 164
DBREF 1AWV E 1002 1165 UNP P62937 PPIA_HUMAN 1 164
DBREF 1AWV F 1002 1165 UNP P62937 PPIA_HUMAN 1 164
DBREF 1AWV G 101 106 PDB 1AWV 1AWV 101 106
DBREF 1AWV H 101 106 PDB 1AWV 1AWV 101 106
DBREF 1AWV I 101 106 PDB 1AWV 1AWV 101 106
DBREF 1AWV J 101 106 PDB 1AWV 1AWV 101 106
DBREF 1AWV K 101 106 PDB 1AWV 1AWV 101 106
DBREF 1AWV L 101 106 PDB 1AWV 1AWV 101 106
SEQRES 1 A 164 VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP GLY
SEQRES 2 A 164 GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA ASP
SEQRES 3 A 164 LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU SER
SEQRES 4 A 164 THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS PHE
SEQRES 5 A 164 HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY ASP
SEQRES 6 A 164 PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE TYR
SEQRES 7 A 164 GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS HIS
SEQRES 8 A 164 THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY PRO
SEQRES 9 A 164 ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA LYS
SEQRES 10 A 164 THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY LYS
SEQRES 11 A 164 VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU ARG
SEQRES 12 A 164 PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE THR
SEQRES 13 A 164 ILE ALA ASP CYS GLY GLN LEU GLU
SEQRES 1 B 164 VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP GLY
SEQRES 2 B 164 GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA ASP
SEQRES 3 B 164 LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU SER
SEQRES 4 B 164 THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS PHE
SEQRES 5 B 164 HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY ASP
SEQRES 6 B 164 PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE TYR
SEQRES 7 B 164 GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS HIS
SEQRES 8 B 164 THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY PRO
SEQRES 9 B 164 ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA LYS
SEQRES 10 B 164 THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY LYS
SEQRES 11 B 164 VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU ARG
SEQRES 12 B 164 PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE THR
SEQRES 13 B 164 ILE ALA ASP CYS GLY GLN LEU GLU
SEQRES 1 C 164 VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP GLY
SEQRES 2 C 164 GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA ASP
SEQRES 3 C 164 LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU SER
SEQRES 4 C 164 THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS PHE
SEQRES 5 C 164 HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY ASP
SEQRES 6 C 164 PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE TYR
SEQRES 7 C 164 GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS HIS
SEQRES 8 C 164 THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY PRO
SEQRES 9 C 164 ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA LYS
SEQRES 10 C 164 THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY LYS
SEQRES 11 C 164 VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU ARG
SEQRES 12 C 164 PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE THR
SEQRES 13 C 164 ILE ALA ASP CYS GLY GLN LEU GLU
SEQRES 1 D 164 VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP GLY
SEQRES 2 D 164 GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA ASP
SEQRES 3 D 164 LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU SER
SEQRES 4 D 164 THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS PHE
SEQRES 5 D 164 HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY ASP
SEQRES 6 D 164 PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE TYR
SEQRES 7 D 164 GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS HIS
SEQRES 8 D 164 THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY PRO
SEQRES 9 D 164 ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA LYS
SEQRES 10 D 164 THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY LYS
SEQRES 11 D 164 VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU ARG
SEQRES 12 D 164 PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE THR
SEQRES 13 D 164 ILE ALA ASP CYS GLY GLN LEU GLU
SEQRES 1 E 164 VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP GLY
SEQRES 2 E 164 GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA ASP
SEQRES 3 E 164 LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU SER
SEQRES 4 E 164 THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS PHE
SEQRES 5 E 164 HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY ASP
SEQRES 6 E 164 PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE TYR
SEQRES 7 E 164 GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS HIS
SEQRES 8 E 164 THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY PRO
SEQRES 9 E 164 ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA LYS
SEQRES 10 E 164 THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY LYS
SEQRES 11 E 164 VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU ARG
SEQRES 12 E 164 PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE THR
SEQRES 13 E 164 ILE ALA ASP CYS GLY GLN LEU GLU
SEQRES 1 F 164 VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP GLY
SEQRES 2 F 164 GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA ASP
SEQRES 3 F 164 LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU SER
SEQRES 4 F 164 THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS PHE
SEQRES 5 F 164 HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY ASP
SEQRES 6 F 164 PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE TYR
SEQRES 7 F 164 GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS HIS
SEQRES 8 F 164 THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY PRO
SEQRES 9 F 164 ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA LYS
SEQRES 10 F 164 THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY LYS
SEQRES 11 F 164 VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU ARG
SEQRES 12 F 164 PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE THR
SEQRES 13 F 164 ILE ALA ASP CYS GLY GLN LEU GLU
SEQRES 1 G 6 HIS VAL GLY PRO ILE ALA
SEQRES 1 H 6 HIS VAL GLY PRO ILE ALA
SEQRES 1 I 6 HIS VAL GLY PRO ILE ALA
SEQRES 1 J 6 HIS VAL GLY PRO ILE ALA
SEQRES 1 K 6 HIS VAL GLY PRO ILE ALA
SEQRES 1 L 6 HIS VAL GLY PRO ILE ALA
FORMUL 13 HOH *175(H2 O)
HELIX 1 1 PRO A 1030 SER A 1040 1 11
HELIX 2 2 GLU A 1120 LEU A 1122 5 3
HELIX 3 3 MET A 1136 ARG A 1144 1 9
HELIX 4 4 PRO B 1030 SER B 1040 1 11
HELIX 5 5 GLU B 1120 LEU B 1122 5 3
HELIX 6 6 MET B 1136 ALA B 1141 1 6
HELIX 7 7 PRO C 1030 THR C 1041 1 12
HELIX 8 8 GLU C 1120 LEU C 1122 5 3
HELIX 9 9 MET C 1136 PHE C 1145 1 10
HELIX 10 10 PRO D 1030 LEU D 1039 1 10
HELIX 11 11 GLU D 1120 LEU D 1122 5 3
HELIX 12 12 MET D 1136 PHE D 1145 1 10
HELIX 13 13 PRO E 1030 THR E 1041 1 12
HELIX 14 14 GLU E 1120 LEU E 1122 5 3
HELIX 15 15 MET E 1136 PHE E 1145 1 10
HELIX 16 16 PRO F 1030 ALA F 1038 1 9
HELIX 17 17 GLU F 1120 LEU F 1122 5 3
HELIX 18 18 MET F 1136 VAL F 1139 1 4
SHEET 1 A 8 ARG A1055 ILE A1057 0
SHEET 2 A 8 MET A1061 GLY A1064 -1 N GLN A1063 O ARG A1055
SHEET 3 A 8 PHE A1112 CYS A1115 -1 N ILE A1114 O CYS A1062
SHEET 4 A 8 ILE A1097 MET A1100 -1 N SER A1099 O PHE A1113
SHEET 5 A 8 VAL A1128 GLU A1134 -1 N GLY A1130 O LEU A1098
SHEET 6 A 8 GLU A1015 LEU A1024 -1 N GLU A1023 O LYS A1131
SHEET 7 A 8 THR A1005 VAL A1012 -1 N VAL A1012 O GLU A1015
SHEET 8 A 8 ILE A1156 GLN A1163 -1 N GLY A1162 O PHE A1007
SHEET 1 B 5 ARG B1055 ILE B1057 0
SHEET 2 B 5 MET B1061 GLY B1064 -1 N GLN B1063 O ARG B1055
SHEET 3 B 5 PHE B1112 CYS B1115 -1 N ILE B1114 O CYS B1062
SHEET 4 B 5 ILE B1097 MET B1100 -1 N SER B1099 O PHE B1113
SHEET 5 B 5 VAL B1128 LYS B1131 -1 N GLY B1130 O LEU B1098
SHEET 1 C 3 PRO B1016 GLU B1023 0
SHEET 2 C 3 THR B1005 VAL B1012 -1 N ILE B1010 O LEU B1017
SHEET 3 C 3 ILE B1156 GLN B1163 -1 N GLY B1162 O PHE B1007
SHEET 1 D 8 ARG C1055 ILE C1057 0
SHEET 2 D 8 MET C1061 GLY C1064 -1 N GLN C1063 O ARG C1055
SHEET 3 D 8 PHE C1112 CYS C1115 -1 N ILE C1114 O CYS C1062
SHEET 4 D 8 ILE C1097 MET C1100 -1 N SER C1099 O PHE C1113
SHEET 5 D 8 VAL C1128 GLU C1134 -1 N GLY C1130 O LEU C1098
SHEET 6 D 8 GLU C1015 LEU C1024 -1 N GLU C1023 O LYS C1131
SHEET 7 D 8 THR C1005 VAL C1012 -1 N VAL C1012 O GLU C1015
SHEET 8 D 8 ILE C1156 GLN C1163 -1 N GLY C1162 O PHE C1007
SHEET 1 E 8 ARG D1055 ILE D1057 0
SHEET 2 E 8 MET D1061 GLY D1064 -1 N GLN D1063 O ARG D1055
SHEET 3 E 8 PHE D1112 CYS D1115 -1 N ILE D1114 O CYS D1062
SHEET 4 E 8 ILE D1097 MET D1100 -1 N SER D1099 O PHE D1113
SHEET 5 E 8 VAL D1128 GLU D1134 -1 N GLY D1130 O LEU D1098
SHEET 6 E 8 GLU D1015 LEU D1024 -1 N GLU D1023 O LYS D1131
SHEET 7 E 8 THR D1005 VAL D1012 -1 N VAL D1012 O GLU D1015
SHEET 8 E 8 ILE D1156 GLN D1163 -1 N GLY D1162 O PHE D1007
SHEET 1 F 8 ARG E1055 ILE E1057 0
SHEET 2 F 8 MET E1061 GLY E1064 -1 N GLN E1063 O ARG E1055
SHEET 3 F 8 PHE E1112 CYS E1115 -1 N ILE E1114 O CYS E1062
SHEET 4 F 8 ILE E1097 MET E1100 -1 N SER E1099 O PHE E1113
SHEET 5 F 8 VAL E1128 GLU E1134 -1 N GLY E1130 O LEU E1098
SHEET 6 F 8 GLU E1015 LEU E1024 -1 N GLU E1023 O LYS E1131
SHEET 7 F 8 THR E1005 VAL E1012 -1 N VAL E1012 O GLU E1015
SHEET 8 F 8 ILE E1156 GLN E1163 -1 N GLY E1162 O PHE E1007
SHEET 1 G 8 ARG F1055 ILE F1057 0
SHEET 2 G 8 MET F1061 GLY F1064 -1 N GLN F1063 O ARG F1055
SHEET 3 G 8 PHE F1112 CYS F1115 -1 N ILE F1114 O CYS F1062
SHEET 4 G 8 ILE F1097 MET F1100 -1 N SER F1099 O PHE F1113
SHEET 5 G 8 VAL F1128 GLU F1134 -1 N GLY F1130 O LEU F1098
SHEET 6 G 8 GLU F1015 LEU F1024 -1 N GLU F1023 O LYS F1131
SHEET 7 G 8 PRO F1004 VAL F1012 -1 N VAL F1012 O GLU F1015
SHEET 8 G 8 ILE F1156 GLN F1163 -1 N GLY F1162 O PHE F1007
CRYST1 74.000 74.000 190.400 90.00 90.00 90.00 P 41 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 0.013514 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013514 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005252 0.00000
MTRIX1 1 0.999861 0.001421 -0.016643 -0.09511 1
MTRIX2 1 -0.002204 0.998888 -0.047093 0.72127 1
MTRIX3 1 0.016558 0.047123 0.998752 125.85183 1
MTRIX1 2 0.993750 0.109133 0.023496 -2.30208 1
MTRIX2 2 -0.109199 0.994019 0.001541 2.44480 1
MTRIX3 2 -0.023188 -0.004097 0.999723 64.03819 1
MTRIX1 3 0.983917 0.178561 0.004839 33.72785 1
MTRIX2 3 -0.178381 0.983626 -0.025707 41.14758 1
MTRIX3 3 -0.009350 0.024431 0.999658 -0.18907 1
MTRIX1 4 0.998728 -0.050003 -0.006495 37.85891 1
MTRIX2 4 0.049786 0.998308 -0.030050 36.32781 1
MTRIX3 4 0.007986 0.029688 0.999527 126.22861 1
MTRIX1 5 0.994504 0.089688 0.054024 35.25095 1
MTRIX2 5 -0.096305 0.986035 0.135866 38.86013 1
MTRIX3 5 -0.041085 -0.140322 0.989253 67.00388 1
(ATOM LINES ARE NOT SHOWN.)
END
