HEADER ISOMERASE 27-DEC-13 4O8I
TITLE 1.45A RESOLUTION STRUCTURE OF PEG 400 BOUND CYCLOPHILIN D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE F, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PPIASE F, CYCLOPHILIN D, CYP-D, CYPD, CYCLOPHILIN F,
COMPND 5 MITOCHONDRIAL CYCLOPHILIN, CYP-M, ROTAMASE F;
COMPND 6 EC: 5.2.1.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PPIF, CYP3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LOVELL,K.R.VALASANI,K.P.BATTAILE,C.WANG,S.S.YAN
REVDAT 4 20-SEP-23 4O8I 1 REMARK SEQADV
REVDAT 3 22-NOV-17 4O8I 1 REMARK
REVDAT 2 24-SEP-14 4O8I 1 JRNL
REVDAT 1 11-JUN-14 4O8I 0
JRNL AUTH K.R.VALASANI,E.A.CARLSON,K.P.BATTAILE,A.BISSON,C.WANG,
JRNL AUTH 2 S.LOVELL,S.SHIDU YAN
JRNL TITL HIGH-RESOLUTION CRYSTAL STRUCTURES OF TWO CRYSTAL FORMS OF
JRNL TITL 2 HUMAN CYCLOPHILIN D IN COMPLEX WITH PEG 400 MOLECULES.
JRNL REF ACTA CRYSTALLOGR F STRUCT V. 70 717 2014
JRNL REF 2 BIOL COMMUN
JRNL REFN ESSN 1744-3091
JRNL PMID 24915078
JRNL DOI 10.1107/S2053230X14009480
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1488
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 24089
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1231
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.1232 - 3.0155 1.00 2711 134 0.1509 0.1620
REMARK 3 2 3.0155 - 2.3937 1.00 2585 141 0.1504 0.1772
REMARK 3 3 2.3937 - 2.0912 1.00 2583 124 0.1413 0.1652
REMARK 3 4 2.0912 - 1.9000 1.00 2541 126 0.1458 0.1720
REMARK 3 5 1.9000 - 1.7638 1.00 2497 152 0.1617 0.2302
REMARK 3 6 1.7638 - 1.6598 1.00 2546 132 0.1864 0.2508
REMARK 3 7 1.6598 - 1.5767 1.00 2509 136 0.1922 0.2307
REMARK 3 8 1.5767 - 1.5081 0.99 2465 144 0.2145 0.2591
REMARK 3 9 1.5081 - 1.4500 0.96 2421 142 0.2381 0.2789
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.830
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.77
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 1276
REMARK 3 ANGLE : 0.909 1726
REMARK 3 CHIRALITY : 0.072 190
REMARK 3 PLANARITY : 0.005 226
REMARK 3 DIHEDRAL : 11.540 461
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5087 15.9153 -20.5473
REMARK 3 T TENSOR
REMARK 3 T11: 0.2284 T22: 0.1065
REMARK 3 T33: 0.1333 T12: -0.0475
REMARK 3 T13: -0.0170 T23: 0.0407
REMARK 3 L TENSOR
REMARK 3 L11: 0.4906 L22: 1.1017
REMARK 3 L33: 0.3942 L12: -0.2936
REMARK 3 L13: 0.0860 L23: 0.5502
REMARK 3 S TENSOR
REMARK 3 S11: -0.0902 S12: 0.1425 S13: 0.1027
REMARK 3 S21: -0.7770 S22: 0.2171 S23: -0.1685
REMARK 3 S31: -0.2206 S32: 0.0578 S33: 0.2916
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 25 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6119 6.3678 -15.6183
REMARK 3 T TENSOR
REMARK 3 T11: 0.0258 T22: 0.1241
REMARK 3 T33: 0.1734 T12: -0.0246
REMARK 3 T13: 0.0691 T23: -0.0629
REMARK 3 L TENSOR
REMARK 3 L11: 0.2820 L22: 1.3728
REMARK 3 L33: 0.0972 L12: 0.1019
REMARK 3 L13: -0.0155 L23: 0.3290
REMARK 3 S TENSOR
REMARK 3 S11: -0.0942 S12: 0.1305 S13: 0.1549
REMARK 3 S21: -0.3249 S22: 0.2057 S23: -0.5300
REMARK 3 S31: -0.1137 S32: 0.1196 S33: 0.0930
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 42 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2738 6.3289 -17.0913
REMARK 3 T TENSOR
REMARK 3 T11: 0.1434 T22: 0.1328
REMARK 3 T33: 0.1143 T12: -0.0065
REMARK 3 T13: 0.0112 T23: -0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 0.1520 L22: 0.1947
REMARK 3 L33: 0.0512 L12: 0.1022
REMARK 3 L13: 0.0919 L23: 0.0390
REMARK 3 S TENSOR
REMARK 3 S11: -0.1082 S12: -0.0669 S13: 0.0520
REMARK 3 S21: -0.1450 S22: 0.1264 S23: 0.0664
REMARK 3 S31: 0.0541 S32: 0.0650 S33: 0.0222
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 65 THROUGH 84 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.6825 -3.4180 -17.8550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0982 T22: 0.1192
REMARK 3 T33: 0.1438 T12: 0.0031
REMARK 3 T13: 0.0137 T23: -0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 0.0534 L22: 0.1399
REMARK 3 L33: -0.0040 L12: 0.0134
REMARK 3 L13: -0.0177 L23: 0.0354
REMARK 3 S TENSOR
REMARK 3 S11: -0.0127 S12: 0.0973 S13: -0.1722
REMARK 3 S21: -0.0529 S22: 0.0743 S23: -0.0011
REMARK 3 S31: 0.0666 S32: -0.0013 S33: 0.0014
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 85 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0969 6.9173 -6.2838
REMARK 3 T TENSOR
REMARK 3 T11: 0.1462 T22: 0.1231
REMARK 3 T33: 0.0927 T12: 0.0313
REMARK 3 T13: 0.0038 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.5931 L22: 0.2595
REMARK 3 L33: 0.2289 L12: -0.2606
REMARK 3 L13: -0.0820 L23: 0.2181
REMARK 3 S TENSOR
REMARK 3 S11: -0.1330 S12: -0.1392 S13: 0.0353
REMARK 3 S21: 0.3225 S22: 0.1550 S23: -0.0771
REMARK 3 S31: 0.0685 S32: 0.0040 S33: -0.0022
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 136 THROUGH 155 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.3514 14.2972 -14.2942
REMARK 3 T TENSOR
REMARK 3 T11: 0.0998 T22: 0.1039
REMARK 3 T33: 0.1670 T12: 0.0040
REMARK 3 T13: -0.0375 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.1375 L22: 0.0671
REMARK 3 L33: 0.0032 L12: -0.0063
REMARK 3 L13: -0.0357 L23: 0.0032
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: -0.0269 S13: 0.1352
REMARK 3 S21: -0.0488 S22: -0.0924 S23: 0.1294
REMARK 3 S31: -0.1063 S32: 0.0874 S33: -0.0027
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 156 THROUGH 165 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3263 12.7661 -23.8763
REMARK 3 T TENSOR
REMARK 3 T11: 0.3282 T22: 0.1471
REMARK 3 T33: 0.1180 T12: -0.0591
REMARK 3 T13: 0.0014 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.1392 L22: 1.1622
REMARK 3 L33: 0.0075 L12: -0.0677
REMARK 3 L13: -0.0393 L23: 0.1218
REMARK 3 S TENSOR
REMARK 3 S11: 0.0001 S12: 0.1128 S13: 0.0420
REMARK 3 S21: -0.7898 S22: 0.0785 S23: -0.0744
REMARK 3 S31: -0.0620 S32: -0.0132 S33: 0.0869
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4O8I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084175.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.29, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24241
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 40.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.01100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.2
REMARK 200 STARTING MODEL: 2BIT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 8000, 100 MM TRIS, 200
REMARK 280 MM MGCL2, 20% (V/V) PEG 400, PH 8.5, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
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 20.28200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.66800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.50550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 28.66800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.28200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.50550
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: 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 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 SER A 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 15 CG CD CE NZ
REMARK 470 LYS A 118 CD CE NZ
REMARK 470 LYS A 148 CD CE NZ
REMARK 470 ARG A 151 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 154 CD CE NZ
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 A 368 O HOH A 421 2.13
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 60 -78.98 -147.72
REMARK 500 THR A 119 59.97 -106.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PE A 201
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4O8H RELATED DB: PDB
DBREF 4O8I A 1 165 UNP P30405 PPIF_HUMAN 43 207
SEQADV 4O8I ILE A 133 UNP P30405 LYS 175 ENGINEERED MUTATION
SEQRES 1 A 165 SER GLY ASN PRO LEU VAL TYR LEU ASP VAL ASP ALA ASN
SEQRES 2 A 165 GLY LYS PRO LEU GLY ARG VAL VAL LEU GLU LEU LYS ALA
SEQRES 3 A 165 ASP VAL VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU
SEQRES 4 A 165 CYS THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER THR
SEQRES 5 A 165 PHE HIS ARG VAL ILE PRO SER PHE MET CYS GLN ALA GLY
SEQRES 6 A 165 ASP PHE THR ASN HIS ASN GLY THR GLY GLY LYS SER ILE
SEQRES 7 A 165 TYR GLY SER ARG PHE PRO ASP GLU ASN PHE THR LEU LYS
SEQRES 8 A 165 HIS VAL GLY PRO GLY VAL LEU SER MET ALA ASN ALA GLY
SEQRES 9 A 165 PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ILE
SEQRES 10 A 165 LYS THR ASP TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY
SEQRES 11 A 165 HIS VAL ILE GLU GLY MET ASP VAL VAL LYS LYS ILE GLU
SEQRES 12 A 165 SER PHE GLY SER LYS SER GLY ARG THR SER LYS LYS ILE
SEQRES 13 A 165 VAL ILE THR ASP CYS GLY GLN LEU SER
HET 1PE A 201 10
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 2 1PE C10 H22 O6
FORMUL 3 HOH *133(H2 O)
HELIX 1 1 VAL A 29 GLY A 42 1 14
HELIX 2 2 THR A 119 ASP A 123 5 5
HELIX 3 3 GLY A 135 PHE A 145 1 11
SHEET 1 A 8 PHE A 53 ILE A 57 0
SHEET 2 A 8 MET A 61 ALA A 64 -1 O GLN A 63 N ARG A 55
SHEET 3 A 8 PHE A 112 CYS A 115 -1 O PHE A 112 N ALA A 64
SHEET 4 A 8 VAL A 97 MET A 100 -1 N SER A 99 O PHE A 113
SHEET 5 A 8 VAL A 128 GLU A 134 -1 O PHE A 129 N LEU A 98
SHEET 6 A 8 LYS A 15 LEU A 24 -1 N VAL A 21 O ILE A 133
SHEET 7 A 8 LEU A 5 ALA A 12 -1 N VAL A 10 O LEU A 17
SHEET 8 A 8 ILE A 156 GLN A 163 -1 O ASP A 160 N ASP A 9
SITE 1 AC1 4 VAL A 93 PRO A 95 HIS A 131 HOH A 433
CRYST1 40.564 57.011 57.336 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 0.024652 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017540 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017441 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
