HEADER ISOMERASE/ISOMERASE INHIBITOR 06-JUN-14 4TOT
TITLE CRYSTAL STRUCTURE OF RAT CYCLOPHILIN D IN COMPLEX WITH A POTENT
TITLE 2 NONIMMUNOSUPPRESSIVE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE F, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 43-206;
COMPND 5 SYNONYM: PPIASE F,CYCLOPHILIN D,CYPD,CYCLOPHILIN F,ROTAMASE F;
COMPND 6 EC: 5.2.1.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: NONIMMUNOSUPPRESSIVE INHIBITOR;
COMPND 10 CHAIN: E, F, G, H;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: PPIF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 12 ORGANISM_TAXID: 32630
KEYWDS INHIBITOR, COMPLEX, CYCLOSPORIN, ISOMERASE-ISOMERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.S.KNAPP,R.A.ELLING
REVDAT 3 03-APR-24 4TOT 1 REMARK
REVDAT 2 27-DEC-23 4TOT 1 SOURCE JRNL REMARK DBREF
REVDAT 2 2 1 LINK
REVDAT 1 12-NOV-14 4TOT 0
JRNL AUTH J.FU,M.TJANDRA,C.BECKER,D.BEDNARCZYK,M.CAPPARELLI,R.ELLING,
JRNL AUTH 2 I.HANNA,R.FUJIMOTO,M.FUREGATI,S.KARUR,T.KASPRZYK,M.KNAPP,
JRNL AUTH 3 K.LEUNG,X.LI,P.LU,W.MERGO,C.MIAULT,S.NG,D.PARKER,Y.PENG,
JRNL AUTH 4 S.ROGGO,A.RIVKIN,R.L.SIMMONS,M.WANG,B.WIEDMANN,A.H.WEISS,
JRNL AUTH 5 L.XIAO,L.XIE,W.XU,A.YIFRU,S.YANG,B.ZHOU,Z.K.SWEENEY
JRNL TITL POTENT NONIMMUNOSUPPRESSIVE CYCLOPHILIN INHIBITORS WITH
JRNL TITL 2 IMPROVED PHARMACEUTICAL PROPERTIES AND DECREASED TRANSPORTER
JRNL TITL 3 INHIBITION.
JRNL REF J.MED.CHEM. V. 57 8503 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 25310383
JRNL DOI 10.1021/JM500862R
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 3 NUMBER OF REFLECTIONS : 29998
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1517
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.47
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.94
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2071
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2229
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1973
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE : 0.3013
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.73
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 98
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5324
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 298
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11150
REMARK 3 B22 (A**2) : -2.03810
REMARK 3 B33 (A**2) : 2.14960
REMARK 3 B12 (A**2) : -0.40180
REMARK 3 B13 (A**2) : 1.26940
REMARK 3 B23 (A**2) : -0.93740
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.300
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.416
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.241
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.540
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.247
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.901
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.868
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6168 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8900 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2096 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 116 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 808 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6168 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 708 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : 8 ; 1.000 ; HARMONIC
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 7267 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.83
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 14.98
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|2 - A|165 }
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0320 -16.0969 2.5827
REMARK 3 T TENSOR
REMARK 3 T11: 0.0492 T22: -0.1202
REMARK 3 T33: -0.0756 T12: 0.0066
REMARK 3 T13: -0.0329 T23: -0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 0.4244 L22: 1.1893
REMARK 3 L33: 0.8602 L12: 0.2657
REMARK 3 L13: 0.0024 L23: 0.0551
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.0251 S13: -0.0311
REMARK 3 S21: -0.0447 S22: 0.0430 S23: -0.0943
REMARK 3 S31: 0.0018 S32: 0.0885 S33: -0.0415
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|2 - B|165 }
REMARK 3 ORIGIN FOR THE GROUP (A): -18.2692 12.5836 19.8755
REMARK 3 T TENSOR
REMARK 3 T11: 0.0539 T22: -0.1063
REMARK 3 T33: -0.0892 T12: 0.0071
REMARK 3 T13: -0.0382 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.2042 L22: 1.4303
REMARK 3 L33: 1.0433 L12: -0.1741
REMARK 3 L13: -0.0216 L23: -0.0255
REMARK 3 S TENSOR
REMARK 3 S11: -0.0234 S12: -0.0294 S13: -0.0421
REMARK 3 S21: 0.0354 S22: 0.0298 S23: 0.1141
REMARK 3 S31: -0.0105 S32: -0.0522 S33: -0.0064
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|2 - C|165 }
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7173 -17.3557 47.0278
REMARK 3 T TENSOR
REMARK 3 T11: 0.0349 T22: -0.0807
REMARK 3 T33: -0.1075 T12: -0.0002
REMARK 3 T13: -0.0416 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.7568 L22: 1.4661
REMARK 3 L33: 0.6272 L12: 0.1275
REMARK 3 L13: 0.6169 L23: 0.4515
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: 0.1899 S13: 0.0286
REMARK 3 S21: -0.0607 S22: 0.0545 S23: -0.0207
REMARK 3 S31: -0.0363 S32: 0.1566 S33: -0.0502
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|2 - D|165 }
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6106 11.3164 50.2134
REMARK 3 T TENSOR
REMARK 3 T11: 0.0489 T22: -0.0819
REMARK 3 T33: -0.0949 T12: 0.0227
REMARK 3 T13: -0.0434 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.8004 L22: 0.5828
REMARK 3 L33: 0.9933 L12: -0.0044
REMARK 3 L13: 0.5141 L23: -0.3317
REMARK 3 S TENSOR
REMARK 3 S11: -0.0043 S12: -0.1978 S13: -0.0210
REMARK 3 S21: 0.0710 S22: 0.0870 S23: -0.0308
REMARK 3 S31: -0.0544 S32: -0.1852 S33: -0.0827
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { A|201 - A|202 C|201 - C|201 B|201 - B|202 E|1 -
REMARK 3 E|11 D|201 - D|201 G|1 - G|11 F|1 - F|11 H|1 - H|11 }
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6036 -2.4039 29.6640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0908 T22: -0.1155
REMARK 3 T33: -0.0798 T12: 0.0277
REMARK 3 T13: -0.0232 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.0384 L22: 0.1222
REMARK 3 L33: -0.0226 L12: 0.1528
REMARK 3 L13: 0.1028 L23: -0.1634
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: 0.0127 S13: -0.0085
REMARK 3 S21: 0.0711 S22: -0.0085 S23: 0.0529
REMARK 3 S31: 0.0073 S32: -0.0486 S33: 0.0043
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4TOT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000201853.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER PLATINUM 135
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30008
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.390
REMARK 200 RESOLUTION RANGE LOW (A) : 45.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 200 DATA REDUNDANCY : 3.220
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8200
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: IN-HOUSE STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.5, 5% (V/V) PEG 400,
REMARK 280 2M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 1450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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: 1480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F
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: 1380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 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: 1360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE NONIMMUNOSUPPRESSIVE INHIBITOR IS CYCLIC PEPTIDE, A MEMBER OF
REMARK 400 INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: NONIMMUNOSUPPRESSIVE INHIBITOR
REMARK 400 CHAIN: E, F, G, H
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 ALA A 1
REMARK 465 ALA B 1
REMARK 465 ALA C 1
REMARK 465 ALA D 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 148 CG CD CE NZ
REMARK 470 LYS D 148 CG CD CE NZ
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 -76.46 -146.04
REMARK 500 THR A 119 50.29 -99.39
REMARK 500 PHE B 60 -78.96 -146.03
REMARK 500 ASN B 71 12.45 -143.45
REMARK 500 THR B 119 50.32 -99.37
REMARK 500 PHE C 60 -78.26 -145.67
REMARK 500 THR C 119 50.35 -99.81
REMARK 500 PHE D 60 -79.46 -145.70
REMARK 500 ASN D 71 -1.23 -143.89
REMARK 500 THR D 119 50.51 -99.95
REMARK 500 MVA E 4 73.91 -117.72
REMARK 500 MVA F 4 76.43 -119.44
REMARK 500 MVA G 4 74.93 -110.36
REMARK 500 MVA H 4 74.74 -112.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 376 DISTANCE = 7.28 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for nonimmunosuppressive inhibitor
REMARK 800 chain E
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for nonimmunosuppressive inhibitor
REMARK 800 chain F
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for nonimmunosuppressive inhibitor
REMARK 800 chain G
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for nonimmunosuppressive inhibitor
REMARK 800 chain H
DBREF 4TOT A 2 165 UNP P29117 PPIF_RAT 43 206
DBREF 4TOT B 2 165 UNP P29117 PPIF_RAT 43 206
DBREF 4TOT C 2 165 UNP P29117 PPIF_RAT 43 206
DBREF 4TOT D 2 165 UNP P29117 PPIF_RAT 43 206
DBREF 4TOT E 1 11 PDB 4TOT 4TOT 1 11
DBREF 4TOT F 1 11 PDB 4TOT 4TOT 1 11
DBREF 4TOT G 1 11 PDB 4TOT 4TOT 1 11
DBREF 4TOT H 1 11 PDB 4TOT 4TOT 1 11
SEQADV 4TOT ALA A 1 UNP P29117 EXPRESSION TAG
SEQADV 4TOT ILE A 133 UNP P29117 LYS 174 ENGINEERED MUTATION
SEQADV 4TOT ALA B 1 UNP P29117 EXPRESSION TAG
SEQADV 4TOT ILE B 133 UNP P29117 LYS 174 ENGINEERED MUTATION
SEQADV 4TOT ALA C 1 UNP P29117 EXPRESSION TAG
SEQADV 4TOT ILE C 133 UNP P29117 LYS 174 ENGINEERED MUTATION
SEQADV 4TOT ALA D 1 UNP P29117 EXPRESSION TAG
SEQADV 4TOT ILE D 133 UNP P29117 LYS 174 ENGINEERED MUTATION
SEQRES 1 A 165 ALA GLN ASN PRO LEU VAL TYR LEU ASP VAL GLY ALA ASP
SEQRES 2 A 165 GLY GLN 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 ALA 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 LYS THR SER LYS LYS ILE
SEQRES 13 A 165 VAL ILE THR ASP CYS GLY GLN LEU SER
SEQRES 1 B 165 ALA GLN ASN PRO LEU VAL TYR LEU ASP VAL GLY ALA ASP
SEQRES 2 B 165 GLY GLN PRO LEU GLY ARG VAL VAL LEU GLU LEU LYS ALA
SEQRES 3 B 165 ASP VAL VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU
SEQRES 4 B 165 CYS THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER THR
SEQRES 5 B 165 PHE HIS ARG VAL ILE PRO ALA PHE MET CYS GLN ALA GLY
SEQRES 6 B 165 ASP PHE THR ASN HIS ASN GLY THR GLY GLY LYS SER ILE
SEQRES 7 B 165 TYR GLY SER ARG PHE PRO ASP GLU ASN PHE THR LEU LYS
SEQRES 8 B 165 HIS VAL GLY PRO GLY VAL LEU SER MET ALA ASN ALA GLY
SEQRES 9 B 165 PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ILE
SEQRES 10 B 165 LYS THR ASP TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY
SEQRES 11 B 165 HIS VAL ILE GLU GLY MET ASP VAL VAL LYS LYS ILE GLU
SEQRES 12 B 165 SER PHE GLY SER LYS SER GLY LYS THR SER LYS LYS ILE
SEQRES 13 B 165 VAL ILE THR ASP CYS GLY GLN LEU SER
SEQRES 1 C 165 ALA GLN ASN PRO LEU VAL TYR LEU ASP VAL GLY ALA ASP
SEQRES 2 C 165 GLY GLN PRO LEU GLY ARG VAL VAL LEU GLU LEU LYS ALA
SEQRES 3 C 165 ASP VAL VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU
SEQRES 4 C 165 CYS THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER THR
SEQRES 5 C 165 PHE HIS ARG VAL ILE PRO ALA PHE MET CYS GLN ALA GLY
SEQRES 6 C 165 ASP PHE THR ASN HIS ASN GLY THR GLY GLY LYS SER ILE
SEQRES 7 C 165 TYR GLY SER ARG PHE PRO ASP GLU ASN PHE THR LEU LYS
SEQRES 8 C 165 HIS VAL GLY PRO GLY VAL LEU SER MET ALA ASN ALA GLY
SEQRES 9 C 165 PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ILE
SEQRES 10 C 165 LYS THR ASP TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY
SEQRES 11 C 165 HIS VAL ILE GLU GLY MET ASP VAL VAL LYS LYS ILE GLU
SEQRES 12 C 165 SER PHE GLY SER LYS SER GLY LYS THR SER LYS LYS ILE
SEQRES 13 C 165 VAL ILE THR ASP CYS GLY GLN LEU SER
SEQRES 1 D 165 ALA GLN ASN PRO LEU VAL TYR LEU ASP VAL GLY ALA ASP
SEQRES 2 D 165 GLY GLN PRO LEU GLY ARG VAL VAL LEU GLU LEU LYS ALA
SEQRES 3 D 165 ASP VAL VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU
SEQRES 4 D 165 CYS THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER THR
SEQRES 5 D 165 PHE HIS ARG VAL ILE PRO ALA PHE MET CYS GLN ALA GLY
SEQRES 6 D 165 ASP PHE THR ASN HIS ASN GLY THR GLY GLY LYS SER ILE
SEQRES 7 D 165 TYR GLY SER ARG PHE PRO ASP GLU ASN PHE THR LEU LYS
SEQRES 8 D 165 HIS VAL GLY PRO GLY VAL LEU SER MET ALA ASN ALA GLY
SEQRES 9 D 165 PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ILE
SEQRES 10 D 165 LYS THR ASP TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY
SEQRES 11 D 165 HIS VAL ILE GLU GLY MET ASP VAL VAL LYS LYS ILE GLU
SEQRES 12 D 165 SER PHE GLY SER LYS SER GLY LYS THR SER LYS LYS ILE
SEQRES 13 D 165 VAL ILE THR ASP CYS GLY GLN LEU SER
SEQRES 1 E 11 DAL MLE MLE MVA BMT ABA 33X 34E VAL MLE ALA
SEQRES 1 F 11 DAL MLE MLE MVA BMT ABA 33X 34E VAL MLE ALA
SEQRES 1 G 11 DAL MLE MLE MVA BMT ABA 33X 34E VAL MLE ALA
SEQRES 1 H 11 DAL MLE MLE MVA BMT ABA 33X 34E VAL MLE ALA
HET DAL E 1 10
HET MLE E 2 22
HET MLE E 3 22
HET MVA E 4 19
HET BMT E 5 30
HET ABA E 6 13
HET 33X E 7 13
HET 34E E 8 43
HET MLE E 10 22
HET DAL F 1 10
HET MLE F 2 22
HET MLE F 3 22
HET MVA F 4 19
HET BMT F 5 30
HET ABA F 6 13
HET 33X F 7 13
HET 34E F 8 43
HET MLE F 10 22
HET DAL G 1 10
HET MLE G 2 22
HET MLE G 3 22
HET MVA G 4 19
HET BMT G 5 30
HET ABA G 6 13
HET 33X G 7 13
HET 34E G 8 43
HET MLE G 10 22
HET DAL H 1 10
HET MLE H 2 22
HET MLE H 3 22
HET MVA H 4 19
HET BMT H 5 30
HET ABA H 6 13
HET 33X H 7 13
HET 34E H 8 43
HET MLE H 10 22
HET P6G A 201 45
HET SO4 A 202 5
HET P6G B 201 45
HET SO4 B 202 5
HET P6G C 201 45
HET P6G D 201 45
HETNAM DAL D-ALANINE
HETNAM MLE N-METHYLLEUCINE
HETNAM MVA N-METHYLVALINE
HETNAM BMT 4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE
HETNAM ABA ALPHA-AMINOBUTYRIC ACID
HETNAM 33X N-METHYL-D-ALANINE
HETNAM 34E (3R)-4-[4-(2-METHOXYETHYL)PIPERAZIN-1-YL]-N-METHYL-L-
HETNAM 2 34E VALINE
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM SO4 SULFATE ION
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 5 DAL 4(C3 H7 N O2)
FORMUL 5 MLE 12(C7 H15 N O2)
FORMUL 5 MVA 4(C6 H13 N O2)
FORMUL 5 BMT 4(C10 H19 N O3)
FORMUL 5 ABA 4(C4 H9 N O2)
FORMUL 5 33X 4(C4 H9 N O2)
FORMUL 5 34E 4(C13 H27 N3 O3)
FORMUL 9 P6G 4(C12 H26 O7)
FORMUL 10 SO4 2(O4 S 2-)
FORMUL 15 HOH *298(H2 O)
HELIX 1 AA1 VAL A 29 GLY A 42 1 14
HELIX 2 AA2 THR A 119 ASP A 123 5 5
HELIX 3 AA3 GLY A 135 PHE A 145 1 11
HELIX 4 AA4 VAL B 29 GLY B 42 1 14
HELIX 5 AA5 THR B 119 ASP B 123 5 5
HELIX 6 AA6 GLY B 135 PHE B 145 1 11
HELIX 7 AA7 VAL C 29 GLY C 42 1 14
HELIX 8 AA8 THR C 119 ASP C 123 5 5
HELIX 9 AA9 GLY C 135 PHE C 145 1 11
HELIX 10 AB1 VAL D 29 GLY D 42 1 14
HELIX 11 AB2 THR D 119 ASP D 123 5 5
HELIX 12 AB3 GLY D 135 PHE D 145 1 11
SHEET 1 AA1 8 ARG A 55 ILE A 57 0
SHEET 2 AA1 8 MET A 61 ALA A 64 -1 O GLN A 63 N ARG A 55
SHEET 3 AA1 8 PHE A 112 CYS A 115 -1 O ILE A 114 N CYS A 62
SHEET 4 AA1 8 VAL A 97 MET A 100 -1 N VAL A 97 O CYS A 115
SHEET 5 AA1 8 VAL A 128 GLU A 134 -1 O GLY A 130 N LEU A 98
SHEET 6 AA1 8 GLN A 15 LEU A 24 -1 N VAL A 21 O GLU A 134
SHEET 7 AA1 8 LEU A 5 ALA A 12 -1 N VAL A 10 O LEU A 17
SHEET 8 AA1 8 ILE A 156 SER A 165 -1 O ASP A 160 N ASP A 9
SHEET 1 AA2 8 PHE B 53 ILE B 57 0
SHEET 2 AA2 8 MET B 61 ALA B 64 -1 O GLN B 63 N ARG B 55
SHEET 3 AA2 8 PHE B 112 CYS B 115 -1 O PHE B 112 N ALA B 64
SHEET 4 AA2 8 VAL B 97 MET B 100 -1 N VAL B 97 O CYS B 115
SHEET 5 AA2 8 VAL B 128 GLU B 134 -1 O GLY B 130 N LEU B 98
SHEET 6 AA2 8 GLN B 15 LEU B 24 -1 N VAL B 21 O GLU B 134
SHEET 7 AA2 8 LEU B 5 ALA B 12 -1 N VAL B 10 O LEU B 17
SHEET 8 AA2 8 ILE B 156 SER B 165 -1 O ASP B 160 N ASP B 9
SHEET 1 AA3 8 ARG C 55 ILE C 57 0
SHEET 2 AA3 8 MET C 61 ALA C 64 -1 O GLN C 63 N ARG C 55
SHEET 3 AA3 8 PHE C 112 CYS C 115 -1 O ILE C 114 N CYS C 62
SHEET 4 AA3 8 VAL C 97 MET C 100 -1 N SER C 99 O PHE C 113
SHEET 5 AA3 8 VAL C 128 GLU C 134 -1 O GLY C 130 N LEU C 98
SHEET 6 AA3 8 GLN C 15 LEU C 24 -1 N VAL C 21 O GLU C 134
SHEET 7 AA3 8 LEU C 5 ALA C 12 -1 N VAL C 10 O LEU C 17
SHEET 8 AA3 8 ILE C 156 SER C 165 -1 O ASP C 160 N ASP C 9
SHEET 1 AA4 8 ARG D 55 ILE D 57 0
SHEET 2 AA4 8 MET D 61 ALA D 64 -1 O GLN D 63 N ARG D 55
SHEET 3 AA4 8 PHE D 112 CYS D 115 -1 O PHE D 112 N ALA D 64
SHEET 4 AA4 8 VAL D 97 MET D 100 -1 N SER D 99 O PHE D 113
SHEET 5 AA4 8 VAL D 128 GLU D 134 -1 O GLY D 130 N LEU D 98
SHEET 6 AA4 8 GLN D 15 LEU D 24 -1 N VAL D 21 O GLU D 134
SHEET 7 AA4 8 LEU D 5 ALA D 12 -1 N ALA D 12 O GLN D 15
SHEET 8 AA4 8 ILE D 156 SER D 165 -1 O ASP D 160 N ASP D 9
LINK C DAL E 1 N MLE E 2 1555 1555 1.37
LINK N DAL E 1 C ALA E 11 1555 1555 1.33
LINK C MLE E 2 N MLE E 3 1555 1555 1.37
LINK C MLE E 3 N MVA E 4 1555 1555 1.37
LINK C MVA E 4 N BMT E 5 1555 1555 1.38
LINK C BMT E 5 N ABA E 6 1555 1555 1.36
LINK C ABA E 6 N 33X E 7 1555 1555 1.37
LINK C 33X E 7 N 34E E 8 1555 1555 1.37
LINK C 34E E 8 N VAL E 9 1555 1555 1.34
LINK C VAL E 9 N MLE E 10 1555 1555 1.38
LINK C MLE E 10 N ALA E 11 1555 1555 1.33
LINK C DAL F 1 N MLE F 2 1555 1555 1.36
LINK N DAL F 1 C ALA F 11 1555 1555 1.33
LINK C MLE F 2 N MLE F 3 1555 1555 1.38
LINK C MLE F 3 N MVA F 4 1555 1555 1.37
LINK C MVA F 4 N BMT F 5 1555 1555 1.38
LINK C BMT F 5 N ABA F 6 1555 1555 1.35
LINK C ABA F 6 N 33X F 7 1555 1555 1.37
LINK C 33X F 7 N 34E F 8 1555 1555 1.37
LINK C 34E F 8 N VAL F 9 1555 1555 1.34
LINK C VAL F 9 N MLE F 10 1555 1555 1.38
LINK C MLE F 10 N ALA F 11 1555 1555 1.33
LINK C DAL G 1 N MLE G 2 1555 1555 1.36
LINK N DAL G 1 C ALA G 11 1555 1555 1.34
LINK C MLE G 2 N MLE G 3 1555 1555 1.37
LINK C MLE G 3 N MVA G 4 1555 1555 1.37
LINK C MVA G 4 N BMT G 5 1555 1555 1.38
LINK C BMT G 5 N ABA G 6 1555 1555 1.34
LINK C ABA G 6 N 33X G 7 1555 1555 1.37
LINK C 33X G 7 N 34E G 8 1555 1555 1.37
LINK C 34E G 8 N VAL G 9 1555 1555 1.34
LINK C VAL G 9 N MLE G 10 1555 1555 1.37
LINK C MLE G 10 N ALA G 11 1555 1555 1.34
LINK C DAL H 1 N MLE H 2 1555 1555 1.37
LINK N DAL H 1 C ALA H 11 1555 1555 1.34
LINK C MLE H 2 N MLE H 3 1555 1555 1.38
LINK C MLE H 3 N MVA H 4 1555 1555 1.37
LINK C MVA H 4 N BMT H 5 1555 1555 1.37
LINK C BMT H 5 N ABA H 6 1555 1555 1.35
LINK C ABA H 6 N 33X H 7 1555 1555 1.38
LINK C 33X H 7 N 34E H 8 1555 1555 1.37
LINK C 34E H 8 N VAL H 9 1555 1555 1.34
LINK C VAL H 9 N MLE H 10 1555 1555 1.37
LINK C MLE H 10 N ALA H 11 1555 1555 1.35
SITE 1 AC1 7 VAL A 93 GLY A 94 PRO A 95 HIS A 131
SITE 2 AC1 7 LYS B 44 PHE B 46 ILE B 78
SITE 1 AC2 2 LYS A 148 LYS C 148
SITE 1 AC3 8 PHE A 46 ILE A 78 VAL B 93 GLY B 94
SITE 2 AC3 8 PRO B 95 HIS B 131 HOH B 306 HOH B 375
SITE 1 AC4 3 SER B 147 LYS B 148 HOH B 318
SITE 1 AC5 8 VAL C 93 GLY C 94 PRO C 95 HIS C 131
SITE 2 AC5 8 PHE D 46 SER D 77 ILE D 78 GLY D 80
SITE 1 AC6 6 PHE C 46 ILE C 78 VAL D 93 GLY D 94
SITE 2 AC6 6 PRO D 95 HIS D 131
SITE 1 AC7 22 ARG A 55 PHE A 60 MET A 61 GLN A 63
SITE 2 AC7 22 GLY A 72 THR A 73 ALA A 101 ASN A 102
SITE 3 AC7 22 ALA A 103 GLN A 111 PHE A 113 TRP A 121
SITE 4 AC7 22 HIS A 126 ALA C 59 ILE C 117 TRP C 121
SITE 5 AC7 22 HOH E 102 HOH E 103 HOH E 104 HOH E 105
SITE 6 AC7 22 HOH E 106 MLE G 2
SITE 1 AC8 19 ARG B 55 PHE B 60 GLN B 63 GLY B 72
SITE 2 AC8 19 THR B 73 ALA B 101 ASN B 102 ALA B 103
SITE 3 AC8 19 GLN B 111 PHE B 113 TRP B 121 HIS B 126
SITE 4 AC8 19 ALA D 59 ILE D 117 TRP D 121 HOH F 101
SITE 5 AC8 19 HOH F 102 HOH F 104 MLE H 2
SITE 1 AC9 21 PRO A 58 ALA A 59 ARG C 55 PHE C 60
SITE 2 AC9 21 MET C 61 GLN C 63 GLY C 72 THR C 73
SITE 3 AC9 21 ALA C 101 ASN C 102 ALA C 103 GLN C 111
SITE 4 AC9 21 PHE C 113 TRP C 121 LEU C 122 HIS C 126
SITE 5 AC9 21 SER D 144 SER D 153 LYS D 154 DAL E 1
SITE 6 AC9 21 HOH G 103
SITE 1 AD1 23 PRO B 58 ALA B 59 PHE C 145 LYS C 154
SITE 2 AD1 23 ARG D 55 PHE D 60 MET D 61 GLN D 63
SITE 3 AD1 23 GLY D 72 THR D 73 ALA D 101 ASN D 102
SITE 4 AD1 23 ALA D 103 GLN D 111 PHE D 113 TRP D 121
SITE 5 AD1 23 HIS D 126 DAL F 1 MLE F 2 HOH H 101
SITE 6 AD1 23 HOH H 102 HOH H 103 HOH H 105
CRYST1 50.197 57.286 75.274 89.95 83.81 89.86 P 1 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 0.019922 -0.000049 -0.002161 0.00000
SCALE2 0.000000 0.017456 -0.000011 0.00000
SCALE3 0.000000 0.000000 0.013363 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
