HEADER HYDROLASE INHIBITOR 25-NOV-11 3UT3
TITLE A NOVEL PAI-I INHIBITOR AND ITS STRUCTURAL MECHANISM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMINOGEN ACTIVATOR INHIBITOR 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PAI, PAI-1, ENDOTHELIAL PLASMINOGEN ACTIVATOR INHIBITOR,
COMPND 5 SERPIN E1;
COMPND 6 ENGINEERED: YES;
COMPND 7 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: SERPINE1, PAI1, PLANH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7-PL
KEYWDS SERPIN, HYDROLASE INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.H.LIN,Z.B.HONG,X.L.SHI,L.H.HU,P.A.ANDREASEN,M.D.HUANG
REVDAT 2 08-NOV-23 3UT3 1 REMARK SEQADV
REVDAT 1 06-FEB-13 3UT3 0
JRNL AUTH Z.H.LIN,Z.B.HONG,X.L.SHI,L.H.HU,P.A.ANDREASEN,M.D.HUANG
JRNL TITL A NOVEL PAI-I INHIBITOR AND ITS STRUCTURAL MECHANISM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 61573
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3288
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.42
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4545
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE SET COUNT : 230
REMARK 3 BIN FREE R VALUE : 0.3820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11617
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.08000
REMARK 3 B22 (A**2) : -1.63000
REMARK 3 B33 (A**2) : 2.73000
REMARK 3 B12 (A**2) : -0.63000
REMARK 3 B13 (A**2) : 0.18000
REMARK 3 B23 (A**2) : -0.17000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.444
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.265
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.189
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.353
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11920 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 11449 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16160 ; 1.692 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 26304 ; 0.870 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1447 ; 5.901 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 546 ;35.943 ;23.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2039 ;16.367 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 70 ;21.788 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1812 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13366 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2820 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3UT3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000069174.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64869
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420
REMARK 200 RESOLUTION RANGE LOW (A) : 103.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.67900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: PDB ENTRIES 1DVM AND 1B3K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 6.1, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 293K
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: 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 350
REMARK 350 BIOMOLECULE: 2
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: B
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 PRO A 5
REMARK 465 SER A 6
REMARK 465 VAL A 334
REMARK 465 ALA A 335
REMARK 465 SER A 336
REMARK 465 SER A 337
REMARK 465 SER A 338
REMARK 465 THR A 339
REMARK 465 THR B 333
REMARK 465 VAL B 334
REMARK 465 ALA B 335
REMARK 465 SER B 336
REMARK 465 SER B 337
REMARK 465 SER B 338
REMARK 465 THR B 339
REMARK 465 ALA B 340
REMARK 465 VAL B 341
REMARK 465 ILE B 342
REMARK 465 VAL B 343
REMARK 465 SER B 344
REMARK 465 ALA B 345
REMARK 465 ARG B 346
REMARK 465 MET B 347
REMARK 465 PRO C 5
REMARK 465 SER C 6
REMARK 465 ALA C 335
REMARK 465 SER C 336
REMARK 465 SER C 337
REMARK 465 SER C 338
REMARK 465 THR C 339
REMARK 465 THR D 333
REMARK 465 VAL D 334
REMARK 465 ALA D 335
REMARK 465 SER D 336
REMARK 465 SER D 337
REMARK 465 SER D 338
REMARK 465 THR D 339
REMARK 465 ALA D 340
REMARK 465 VAL D 341
REMARK 465 ILE D 342
REMARK 465 VAL D 343
REMARK 465 SER D 344
REMARK 465 ALA D 345
REMARK 465 ARG D 346
REMARK 465 MET D 347
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 ASN C 87 OE2 GLU C 90 2.14
REMARK 500 O ASN A 87 OE2 GLU A 90 2.19
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 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 LEU A 169 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 ARG A 187 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 LEU C 169 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 LEU D 321 CA - CB - CG ANGL. DEV. = 13.9 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 ASN A 87 -80.50 -46.54
REMARK 500 LYS A 88 37.23 86.18
REMARK 500 THR A 94 136.72 -176.09
REMARK 500 ALA A 96 140.21 179.54
REMARK 500 ARG A 101 -71.05 -48.17
REMARK 500 ASP A 102 40.11 -88.33
REMARK 500 ARG A 118 46.24 38.87
REMARK 500 VAL A 129 -88.75 43.02
REMARK 500 ASP A 193 -19.80 -35.55
REMARK 500 GLU A 244 -32.55 87.44
REMARK 500 PHE A 306 42.29 -103.19
REMARK 500 SER A 310 111.64 -165.29
REMARK 500 ASP A 311 33.43 -98.85
REMARK 500 GLN A 312 -67.85 -104.16
REMARK 500 SER A 331 -121.49 -159.18
REMARK 500 LYS B 69 129.89 -38.94
REMARK 500 ASN B 87 -84.32 -40.02
REMARK 500 LYS B 88 57.23 82.16
REMARK 500 ASP B 231 -1.69 62.50
REMARK 500 GLU B 244 -3.43 -170.76
REMARK 500 ASN B 265 23.20 -77.89
REMARK 500 GLN B 301 -60.30 -28.57
REMARK 500 GLN B 312 -77.70 -70.59
REMARK 500 ASN B 329 -158.11 -132.01
REMARK 500 SER B 331 86.45 165.40
REMARK 500 GLU B 378 104.86 -165.93
REMARK 500 ASN C 87 -78.56 -47.62
REMARK 500 LYS C 88 33.19 90.27
REMARK 500 ALA C 96 140.25 -170.55
REMARK 500 ARG C 101 -84.42 -51.44
REMARK 500 ASP C 102 42.93 -67.23
REMARK 500 ASN C 172 96.50 -163.77
REMARK 500 GLU C 244 -37.61 88.07
REMARK 500 GLN C 312 -74.69 -101.56
REMARK 500 THR C 333 2.13 99.25
REMARK 500 SER D 6 -55.45 54.22
REMARK 500 SER D 27 57.47 -140.42
REMARK 500 ASN D 87 -78.20 -60.93
REMARK 500 LYS D 88 54.76 70.41
REMARK 500 SER D 182 0.64 -69.74
REMARK 500 ASP D 231 -9.07 75.89
REMARK 500 GLU D 244 -35.45 104.02
REMARK 500 GLN D 303 -33.56 -140.19
REMARK 500 GLN D 312 -95.55 -109.22
REMARK 500 PRO D 314 68.23 -57.01
REMARK 500 SER D 331 24.56 -161.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMJ B 401
DBREF 3UT3 A 5 379 UNP P05121 PAI1_HUMAN 28 402
DBREF 3UT3 B 5 379 UNP P05121 PAI1_HUMAN 28 402
DBREF 3UT3 C 5 379 UNP P05121 PAI1_HUMAN 28 402
DBREF 3UT3 D 5 379 UNP P05121 PAI1_HUMAN 28 402
SEQADV 3UT3 HIS A 150 UNP P05121 ASN 173 ENGINEERED MUTATION
SEQADV 3UT3 THR A 154 UNP P05121 LYS 177 ENGINEERED MUTATION
SEQADV 3UT3 LEU A 319 UNP P05121 GLN 342 ENGINEERED MUTATION
SEQADV 3UT3 ILE A 354 UNP P05121 MET 377 ENGINEERED MUTATION
SEQADV 3UT3 HIS B 150 UNP P05121 ASN 173 ENGINEERED MUTATION
SEQADV 3UT3 THR B 154 UNP P05121 LYS 177 ENGINEERED MUTATION
SEQADV 3UT3 LEU B 319 UNP P05121 GLN 342 ENGINEERED MUTATION
SEQADV 3UT3 ILE B 354 UNP P05121 MET 377 ENGINEERED MUTATION
SEQADV 3UT3 HIS C 150 UNP P05121 ASN 173 ENGINEERED MUTATION
SEQADV 3UT3 THR C 154 UNP P05121 LYS 177 ENGINEERED MUTATION
SEQADV 3UT3 LEU C 319 UNP P05121 GLN 342 ENGINEERED MUTATION
SEQADV 3UT3 ILE C 354 UNP P05121 MET 377 ENGINEERED MUTATION
SEQADV 3UT3 HIS D 150 UNP P05121 ASN 173 ENGINEERED MUTATION
SEQADV 3UT3 THR D 154 UNP P05121 LYS 177 ENGINEERED MUTATION
SEQADV 3UT3 LEU D 319 UNP P05121 GLN 342 ENGINEERED MUTATION
SEQADV 3UT3 ILE D 354 UNP P05121 MET 377 ENGINEERED MUTATION
SEQRES 1 A 375 PRO SER TYR VAL ALA HIS LEU ALA SER ASP PHE GLY VAL
SEQRES 2 A 375 ARG VAL PHE GLN GLN VAL ALA GLN ALA SER LYS ASP ARG
SEQRES 3 A 375 ASN VAL VAL PHE SER PRO TYR GLY VAL ALA SER VAL LEU
SEQRES 4 A 375 ALA MET LEU GLN LEU THR THR GLY GLY GLU THR GLN GLN
SEQRES 5 A 375 GLN ILE GLN ALA ALA MET GLY PHE LYS ILE ASP ASP LYS
SEQRES 6 A 375 GLY MET ALA PRO ALA LEU ARG HIS LEU TYR LYS GLU LEU
SEQRES 7 A 375 MET GLY PRO TRP ASN LYS ASP GLU ILE SER THR THR ASP
SEQRES 8 A 375 ALA ILE PHE VAL GLN ARG ASP LEU LYS LEU VAL GLN GLY
SEQRES 9 A 375 PHE MET PRO HIS PHE PHE ARG LEU PHE ARG SER THR VAL
SEQRES 10 A 375 LYS GLN VAL ASP PHE SER GLU VAL GLU ARG ALA ARG PHE
SEQRES 11 A 375 ILE ILE ASN ASP TRP VAL LYS THR HIS THR LYS GLY MET
SEQRES 12 A 375 ILE SER HIS LEU LEU GLY THR GLY ALA VAL ASP GLN LEU
SEQRES 13 A 375 THR ARG LEU VAL LEU VAL ASN ALA LEU TYR PHE ASN GLY
SEQRES 14 A 375 GLN TRP LYS THR PRO PHE PRO ASP SER SER THR HIS ARG
SEQRES 15 A 375 ARG LEU PHE HIS LYS SER ASP GLY SER THR VAL SER VAL
SEQRES 16 A 375 PRO MET MET ALA GLN THR ASN LYS PHE ASN TYR THR GLU
SEQRES 17 A 375 PHE THR THR PRO ASP GLY HIS TYR TYR ASP ILE LEU GLU
SEQRES 18 A 375 LEU PRO TYR HIS GLY ASP THR LEU SER MET PHE ILE ALA
SEQRES 19 A 375 ALA PRO TYR GLU LYS GLU VAL PRO LEU SER ALA LEU THR
SEQRES 20 A 375 ASN ILE LEU SER ALA GLN LEU ILE SER HIS TRP LYS GLY
SEQRES 21 A 375 ASN MET THR ARG LEU PRO ARG LEU LEU VAL LEU PRO LYS
SEQRES 22 A 375 PHE SER LEU GLU THR GLU VAL ASP LEU ARG LYS PRO LEU
SEQRES 23 A 375 GLU ASN LEU GLY MET THR ASP MET PHE ARG GLN PHE GLN
SEQRES 24 A 375 ALA ASP PHE THR SER LEU SER ASP GLN GLU PRO LEU HIS
SEQRES 25 A 375 VAL ALA LEU ALA LEU GLN LYS VAL LYS ILE GLU VAL ASN
SEQRES 26 A 375 GLU SER GLY THR VAL ALA SER SER SER THR ALA VAL ILE
SEQRES 27 A 375 VAL SER ALA ARG MET ALA PRO GLU GLU ILE ILE ILE ASP
SEQRES 28 A 375 ARG PRO PHE LEU PHE VAL VAL ARG HIS ASN PRO THR GLY
SEQRES 29 A 375 THR VAL LEU PHE MET GLY GLN VAL MET GLU PRO
SEQRES 1 B 375 PRO SER TYR VAL ALA HIS LEU ALA SER ASP PHE GLY VAL
SEQRES 2 B 375 ARG VAL PHE GLN GLN VAL ALA GLN ALA SER LYS ASP ARG
SEQRES 3 B 375 ASN VAL VAL PHE SER PRO TYR GLY VAL ALA SER VAL LEU
SEQRES 4 B 375 ALA MET LEU GLN LEU THR THR GLY GLY GLU THR GLN GLN
SEQRES 5 B 375 GLN ILE GLN ALA ALA MET GLY PHE LYS ILE ASP ASP LYS
SEQRES 6 B 375 GLY MET ALA PRO ALA LEU ARG HIS LEU TYR LYS GLU LEU
SEQRES 7 B 375 MET GLY PRO TRP ASN LYS ASP GLU ILE SER THR THR ASP
SEQRES 8 B 375 ALA ILE PHE VAL GLN ARG ASP LEU LYS LEU VAL GLN GLY
SEQRES 9 B 375 PHE MET PRO HIS PHE PHE ARG LEU PHE ARG SER THR VAL
SEQRES 10 B 375 LYS GLN VAL ASP PHE SER GLU VAL GLU ARG ALA ARG PHE
SEQRES 11 B 375 ILE ILE ASN ASP TRP VAL LYS THR HIS THR LYS GLY MET
SEQRES 12 B 375 ILE SER HIS LEU LEU GLY THR GLY ALA VAL ASP GLN LEU
SEQRES 13 B 375 THR ARG LEU VAL LEU VAL ASN ALA LEU TYR PHE ASN GLY
SEQRES 14 B 375 GLN TRP LYS THR PRO PHE PRO ASP SER SER THR HIS ARG
SEQRES 15 B 375 ARG LEU PHE HIS LYS SER ASP GLY SER THR VAL SER VAL
SEQRES 16 B 375 PRO MET MET ALA GLN THR ASN LYS PHE ASN TYR THR GLU
SEQRES 17 B 375 PHE THR THR PRO ASP GLY HIS TYR TYR ASP ILE LEU GLU
SEQRES 18 B 375 LEU PRO TYR HIS GLY ASP THR LEU SER MET PHE ILE ALA
SEQRES 19 B 375 ALA PRO TYR GLU LYS GLU VAL PRO LEU SER ALA LEU THR
SEQRES 20 B 375 ASN ILE LEU SER ALA GLN LEU ILE SER HIS TRP LYS GLY
SEQRES 21 B 375 ASN MET THR ARG LEU PRO ARG LEU LEU VAL LEU PRO LYS
SEQRES 22 B 375 PHE SER LEU GLU THR GLU VAL ASP LEU ARG LYS PRO LEU
SEQRES 23 B 375 GLU ASN LEU GLY MET THR ASP MET PHE ARG GLN PHE GLN
SEQRES 24 B 375 ALA ASP PHE THR SER LEU SER ASP GLN GLU PRO LEU HIS
SEQRES 25 B 375 VAL ALA LEU ALA LEU GLN LYS VAL LYS ILE GLU VAL ASN
SEQRES 26 B 375 GLU SER GLY THR VAL ALA SER SER SER THR ALA VAL ILE
SEQRES 27 B 375 VAL SER ALA ARG MET ALA PRO GLU GLU ILE ILE ILE ASP
SEQRES 28 B 375 ARG PRO PHE LEU PHE VAL VAL ARG HIS ASN PRO THR GLY
SEQRES 29 B 375 THR VAL LEU PHE MET GLY GLN VAL MET GLU PRO
SEQRES 1 C 375 PRO SER TYR VAL ALA HIS LEU ALA SER ASP PHE GLY VAL
SEQRES 2 C 375 ARG VAL PHE GLN GLN VAL ALA GLN ALA SER LYS ASP ARG
SEQRES 3 C 375 ASN VAL VAL PHE SER PRO TYR GLY VAL ALA SER VAL LEU
SEQRES 4 C 375 ALA MET LEU GLN LEU THR THR GLY GLY GLU THR GLN GLN
SEQRES 5 C 375 GLN ILE GLN ALA ALA MET GLY PHE LYS ILE ASP ASP LYS
SEQRES 6 C 375 GLY MET ALA PRO ALA LEU ARG HIS LEU TYR LYS GLU LEU
SEQRES 7 C 375 MET GLY PRO TRP ASN LYS ASP GLU ILE SER THR THR ASP
SEQRES 8 C 375 ALA ILE PHE VAL GLN ARG ASP LEU LYS LEU VAL GLN GLY
SEQRES 9 C 375 PHE MET PRO HIS PHE PHE ARG LEU PHE ARG SER THR VAL
SEQRES 10 C 375 LYS GLN VAL ASP PHE SER GLU VAL GLU ARG ALA ARG PHE
SEQRES 11 C 375 ILE ILE ASN ASP TRP VAL LYS THR HIS THR LYS GLY MET
SEQRES 12 C 375 ILE SER HIS LEU LEU GLY THR GLY ALA VAL ASP GLN LEU
SEQRES 13 C 375 THR ARG LEU VAL LEU VAL ASN ALA LEU TYR PHE ASN GLY
SEQRES 14 C 375 GLN TRP LYS THR PRO PHE PRO ASP SER SER THR HIS ARG
SEQRES 15 C 375 ARG LEU PHE HIS LYS SER ASP GLY SER THR VAL SER VAL
SEQRES 16 C 375 PRO MET MET ALA GLN THR ASN LYS PHE ASN TYR THR GLU
SEQRES 17 C 375 PHE THR THR PRO ASP GLY HIS TYR TYR ASP ILE LEU GLU
SEQRES 18 C 375 LEU PRO TYR HIS GLY ASP THR LEU SER MET PHE ILE ALA
SEQRES 19 C 375 ALA PRO TYR GLU LYS GLU VAL PRO LEU SER ALA LEU THR
SEQRES 20 C 375 ASN ILE LEU SER ALA GLN LEU ILE SER HIS TRP LYS GLY
SEQRES 21 C 375 ASN MET THR ARG LEU PRO ARG LEU LEU VAL LEU PRO LYS
SEQRES 22 C 375 PHE SER LEU GLU THR GLU VAL ASP LEU ARG LYS PRO LEU
SEQRES 23 C 375 GLU ASN LEU GLY MET THR ASP MET PHE ARG GLN PHE GLN
SEQRES 24 C 375 ALA ASP PHE THR SER LEU SER ASP GLN GLU PRO LEU HIS
SEQRES 25 C 375 VAL ALA LEU ALA LEU GLN LYS VAL LYS ILE GLU VAL ASN
SEQRES 26 C 375 GLU SER GLY THR VAL ALA SER SER SER THR ALA VAL ILE
SEQRES 27 C 375 VAL SER ALA ARG MET ALA PRO GLU GLU ILE ILE ILE ASP
SEQRES 28 C 375 ARG PRO PHE LEU PHE VAL VAL ARG HIS ASN PRO THR GLY
SEQRES 29 C 375 THR VAL LEU PHE MET GLY GLN VAL MET GLU PRO
SEQRES 1 D 375 PRO SER TYR VAL ALA HIS LEU ALA SER ASP PHE GLY VAL
SEQRES 2 D 375 ARG VAL PHE GLN GLN VAL ALA GLN ALA SER LYS ASP ARG
SEQRES 3 D 375 ASN VAL VAL PHE SER PRO TYR GLY VAL ALA SER VAL LEU
SEQRES 4 D 375 ALA MET LEU GLN LEU THR THR GLY GLY GLU THR GLN GLN
SEQRES 5 D 375 GLN ILE GLN ALA ALA MET GLY PHE LYS ILE ASP ASP LYS
SEQRES 6 D 375 GLY MET ALA PRO ALA LEU ARG HIS LEU TYR LYS GLU LEU
SEQRES 7 D 375 MET GLY PRO TRP ASN LYS ASP GLU ILE SER THR THR ASP
SEQRES 8 D 375 ALA ILE PHE VAL GLN ARG ASP LEU LYS LEU VAL GLN GLY
SEQRES 9 D 375 PHE MET PRO HIS PHE PHE ARG LEU PHE ARG SER THR VAL
SEQRES 10 D 375 LYS GLN VAL ASP PHE SER GLU VAL GLU ARG ALA ARG PHE
SEQRES 11 D 375 ILE ILE ASN ASP TRP VAL LYS THR HIS THR LYS GLY MET
SEQRES 12 D 375 ILE SER HIS LEU LEU GLY THR GLY ALA VAL ASP GLN LEU
SEQRES 13 D 375 THR ARG LEU VAL LEU VAL ASN ALA LEU TYR PHE ASN GLY
SEQRES 14 D 375 GLN TRP LYS THR PRO PHE PRO ASP SER SER THR HIS ARG
SEQRES 15 D 375 ARG LEU PHE HIS LYS SER ASP GLY SER THR VAL SER VAL
SEQRES 16 D 375 PRO MET MET ALA GLN THR ASN LYS PHE ASN TYR THR GLU
SEQRES 17 D 375 PHE THR THR PRO ASP GLY HIS TYR TYR ASP ILE LEU GLU
SEQRES 18 D 375 LEU PRO TYR HIS GLY ASP THR LEU SER MET PHE ILE ALA
SEQRES 19 D 375 ALA PRO TYR GLU LYS GLU VAL PRO LEU SER ALA LEU THR
SEQRES 20 D 375 ASN ILE LEU SER ALA GLN LEU ILE SER HIS TRP LYS GLY
SEQRES 21 D 375 ASN MET THR ARG LEU PRO ARG LEU LEU VAL LEU PRO LYS
SEQRES 22 D 375 PHE SER LEU GLU THR GLU VAL ASP LEU ARG LYS PRO LEU
SEQRES 23 D 375 GLU ASN LEU GLY MET THR ASP MET PHE ARG GLN PHE GLN
SEQRES 24 D 375 ALA ASP PHE THR SER LEU SER ASP GLN GLU PRO LEU HIS
SEQRES 25 D 375 VAL ALA LEU ALA LEU GLN LYS VAL LYS ILE GLU VAL ASN
SEQRES 26 D 375 GLU SER GLY THR VAL ALA SER SER SER THR ALA VAL ILE
SEQRES 27 D 375 VAL SER ALA ARG MET ALA PRO GLU GLU ILE ILE ILE ASP
SEQRES 28 D 375 ARG PRO PHE LEU PHE VAL VAL ARG HIS ASN PRO THR GLY
SEQRES 29 D 375 THR VAL LEU PHE MET GLY GLN VAL MET GLU PRO
HET EMJ B 401 21
HETNAM EMJ 2,5-DIHYDROXY-3-UNDECYLCYCLOHEXA-2,5-DIENE-1,4-DIONE
FORMUL 5 EMJ C17 H26 O4
HELIX 1 1 TYR A 7 SER A 27 1 21
HELIX 2 2 SER A 35 THR A 49 1 15
HELIX 3 3 GLY A 51 GLY A 63 1 13
HELIX 4 4 GLY A 70 MET A 83 1 14
HELIX 5 5 GLY A 108 ARG A 118 1 11
HELIX 6 6 ASP A 125 GLU A 128 5 4
HELIX 7 7 VAL A 129 THR A 144 1 16
HELIX 8 8 LEU A 151 VAL A 157 5 7
HELIX 9 9 PRO A 180 THR A 184 5 5
HELIX 10 10 HIS A 229 ASP A 231 5 3
HELIX 11 11 LEU A 247 ASN A 252 1 6
HELIX 12 12 SER A 255 MET A 266 1 12
HELIX 13 13 LEU A 286 ASN A 292 1 7
HELIX 14 14 THR A 296 ARG A 300 5 5
HELIX 15 15 SER B 6 ALA B 26 1 21
HELIX 16 16 SER B 35 THR B 49 1 15
HELIX 17 17 GLY B 51 GLY B 63 1 13
HELIX 18 18 GLY B 70 MET B 83 1 14
HELIX 19 19 GLY B 108 ARG B 118 1 11
HELIX 20 20 GLU B 128 HIS B 143 1 16
HELIX 21 21 LEU B 151 VAL B 157 5 7
HELIX 22 22 PRO B 180 THR B 184 5 5
HELIX 23 23 LEU B 247 ASN B 252 1 6
HELIX 24 24 SER B 255 ASN B 265 1 11
HELIX 25 25 LEU B 286 ASN B 292 1 7
HELIX 26 26 THR B 296 ARG B 300 5 5
HELIX 27 27 VAL C 8 ALA C 26 1 19
HELIX 28 28 SER C 35 THR C 49 1 15
HELIX 29 29 GLY C 51 GLY C 63 1 13
HELIX 30 30 GLY C 70 MET C 83 1 14
HELIX 31 31 GLY C 108 ARG C 118 1 11
HELIX 32 32 GLU C 128 THR C 144 1 17
HELIX 33 33 LEU C 151 VAL C 157 5 7
HELIX 34 34 PRO C 180 THR C 184 5 5
HELIX 35 35 HIS C 229 ASP C 231 5 3
HELIX 36 36 LEU C 247 ASN C 252 1 6
HELIX 37 37 SER C 255 ASN C 265 1 11
HELIX 38 38 LEU C 286 ASN C 292 1 7
HELIX 39 39 THR C 296 ARG C 300 5 5
HELIX 40 40 SER D 6 ALA D 26 1 21
HELIX 41 41 SER D 35 LEU D 48 1 14
HELIX 42 42 GLY D 51 GLY D 63 1 13
HELIX 43 43 GLY D 70 LEU D 82 1 13
HELIX 44 44 GLY D 108 ARG D 118 1 11
HELIX 45 45 GLU D 128 HIS D 143 1 16
HELIX 46 46 LEU D 151 VAL D 157 5 7
HELIX 47 47 PRO D 180 THR D 184 5 5
HELIX 48 48 LEU D 247 ASN D 252 1 6
HELIX 49 49 SER D 255 ASN D 265 1 11
HELIX 50 50 LEU D 286 ASN D 292 1 7
SHEET 1 A 7 VAL A 32 PHE A 34 0
SHEET 2 A 7 VAL A 370 VAL A 376 -1 O MET A 373 N PHE A 34
SHEET 3 A 7 PHE A 358 HIS A 364 -1 N VAL A 362 O PHE A 372
SHEET 4 A 7 LEU A 233 PRO A 240 -1 N PHE A 236 O VAL A 361
SHEET 5 A 7 TYR A 220 PRO A 227 -1 N LEU A 226 O MET A 235
SHEET 6 A 7 THR A 196 THR A 214 -1 N PHE A 213 O TYR A 221
SHEET 7 A 7 HIS A 185 HIS A 190 -1 N HIS A 185 O MET A 201
SHEET 1 B 8 VAL A 32 PHE A 34 0
SHEET 2 B 8 VAL A 370 VAL A 376 -1 O MET A 373 N PHE A 34
SHEET 3 B 8 PHE A 358 HIS A 364 -1 N VAL A 362 O PHE A 372
SHEET 4 B 8 LEU A 233 PRO A 240 -1 N PHE A 236 O VAL A 361
SHEET 5 B 8 TYR A 220 PRO A 227 -1 N LEU A 226 O MET A 235
SHEET 6 B 8 THR A 196 THR A 214 -1 N PHE A 213 O TYR A 221
SHEET 7 B 8 THR A 267 PRO A 276 -1 O LEU A 275 N MET A 202
SHEET 8 B 8 GLU A 350 ILE A 353 1 O ILE A 352 N LEU A 272
SHEET 1 C 4 ILE A 91 SER A 92 0
SHEET 2 C 4 LEU A 163 PHE A 171 -1 O TYR A 170 N SER A 92
SHEET 3 C 4 ASP A 95 GLN A 100 -1 N PHE A 98 O VAL A 164
SHEET 4 C 4 LYS A 122 VAL A 124 1 O LYS A 122 N VAL A 99
SHEET 1 D 4 ILE A 91 SER A 92 0
SHEET 2 D 4 LEU A 163 PHE A 171 -1 O TYR A 170 N SER A 92
SHEET 3 D 4 LEU A 319 VAL A 328 1 O GLU A 327 N PHE A 171
SHEET 4 D 4 PHE A 278 ASP A 285 -1 N PHE A 278 O VAL A 328
SHEET 1 E 6 ILE A 342 ARG A 346 0
SHEET 2 E 6 PHE C 278 ASP C 285 -1 O GLU C 281 N ALA A 345
SHEET 3 E 6 LEU C 319 VAL C 328 -1 O VAL C 328 N PHE C 278
SHEET 4 E 6 LEU C 163 PHE C 171 1 N LEU C 165 O LEU C 319
SHEET 5 E 6 ILE C 91 GLN C 100 -1 N PHE C 98 O VAL C 164
SHEET 6 E 6 LYS C 122 VAL C 124 1 O LYS C 122 N VAL C 99
SHEET 1 F 7 VAL B 32 PHE B 34 0
SHEET 2 F 7 THR B 369 VAL B 376 -1 O MET B 373 N PHE B 34
SHEET 3 F 7 PHE B 358 HIS B 364 -1 N HIS B 364 O THR B 369
SHEET 4 F 7 LEU B 233 PRO B 240 -1 N SER B 234 O ARG B 363
SHEET 5 F 7 TYR B 220 PRO B 227 -1 N ASP B 222 O ALA B 239
SHEET 6 F 7 THR B 196 THR B 214 -1 N PHE B 213 O TYR B 221
SHEET 7 F 7 HIS B 185 HIS B 190 -1 N HIS B 185 O MET B 201
SHEET 1 G 8 VAL B 32 PHE B 34 0
SHEET 2 G 8 THR B 369 VAL B 376 -1 O MET B 373 N PHE B 34
SHEET 3 G 8 PHE B 358 HIS B 364 -1 N HIS B 364 O THR B 369
SHEET 4 G 8 LEU B 233 PRO B 240 -1 N SER B 234 O ARG B 363
SHEET 5 G 8 TYR B 220 PRO B 227 -1 N ASP B 222 O ALA B 239
SHEET 6 G 8 THR B 196 THR B 214 -1 N PHE B 213 O TYR B 221
SHEET 7 G 8 THR B 267 PRO B 276 -1 O LEU B 269 N PHE B 208
SHEET 8 G 8 GLU B 351 ILE B 353 1 O ILE B 352 N LEU B 272
SHEET 1 H 5 LYS B 122 VAL B 124 0
SHEET 2 H 5 ILE B 91 GLN B 100 1 N VAL B 99 O LYS B 122
SHEET 3 H 5 LEU B 163 ASN B 172 -1 O VAL B 166 N ALA B 96
SHEET 4 H 5 LEU B 319 VAL B 328 1 O LEU B 319 N LEU B 165
SHEET 5 H 5 PHE B 278 ASP B 285 -1 N PHE B 278 O VAL B 328
SHEET 1 I 7 VAL C 32 PHE C 34 0
SHEET 2 I 7 VAL C 370 VAL C 376 -1 O GLN C 375 N VAL C 32
SHEET 3 I 7 PHE C 358 HIS C 364 -1 N PHE C 358 O VAL C 376
SHEET 4 I 7 LEU C 233 PRO C 240 -1 N PHE C 236 O VAL C 361
SHEET 5 I 7 TYR C 220 PRO C 227 -1 N ASP C 222 O ALA C 239
SHEET 6 I 7 THR C 196 THR C 214 -1 N PHE C 213 O TYR C 221
SHEET 7 I 7 HIS C 185 HIS C 190 -1 N HIS C 185 O MET C 201
SHEET 1 J 8 VAL C 32 PHE C 34 0
SHEET 2 J 8 VAL C 370 VAL C 376 -1 O GLN C 375 N VAL C 32
SHEET 3 J 8 PHE C 358 HIS C 364 -1 N PHE C 358 O VAL C 376
SHEET 4 J 8 LEU C 233 PRO C 240 -1 N PHE C 236 O VAL C 361
SHEET 5 J 8 TYR C 220 PRO C 227 -1 N ASP C 222 O ALA C 239
SHEET 6 J 8 THR C 196 THR C 214 -1 N PHE C 213 O TYR C 221
SHEET 7 J 8 THR C 267 PRO C 276 -1 O LEU C 275 N MET C 202
SHEET 8 J 8 GLU C 350 ILE C 353 1 O ILE C 352 N LEU C 272
SHEET 1 K 7 VAL D 32 PHE D 34 0
SHEET 2 K 7 VAL D 370 VAL D 376 -1 O MET D 373 N PHE D 34
SHEET 3 K 7 PHE D 358 HIS D 364 -1 N PHE D 358 O VAL D 376
SHEET 4 K 7 LEU D 233 PRO D 240 -1 N ALA D 238 O LEU D 359
SHEET 5 K 7 TYR D 220 PRO D 227 -1 N LEU D 226 O MET D 235
SHEET 6 K 7 THR D 196 THR D 214 -1 N PHE D 213 O TYR D 221
SHEET 7 K 7 HIS D 185 HIS D 190 -1 N ARG D 187 O VAL D 199
SHEET 1 L 8 VAL D 32 PHE D 34 0
SHEET 2 L 8 VAL D 370 VAL D 376 -1 O MET D 373 N PHE D 34
SHEET 3 L 8 PHE D 358 HIS D 364 -1 N PHE D 358 O VAL D 376
SHEET 4 L 8 LEU D 233 PRO D 240 -1 N ALA D 238 O LEU D 359
SHEET 5 L 8 TYR D 220 PRO D 227 -1 N LEU D 226 O MET D 235
SHEET 6 L 8 THR D 196 THR D 214 -1 N PHE D 213 O TYR D 221
SHEET 7 L 8 THR D 267 PRO D 276 -1 O ARG D 271 N ASN D 206
SHEET 8 L 8 GLU D 351 ILE D 353 1 O ILE D 352 N LEU D 272
SHEET 1 M 5 LYS D 122 VAL D 124 0
SHEET 2 M 5 ILE D 91 GLN D 100 1 N VAL D 99 O LYS D 122
SHEET 3 M 5 LEU D 163 ASN D 172 -1 O VAL D 164 N PHE D 98
SHEET 4 M 5 LEU D 319 VAL D 328 1 O GLU D 327 N PHE D 171
SHEET 5 M 5 PHE D 278 ASP D 285 -1 N PHE D 278 O VAL D 328
SITE 1 AC1 12 MET B 45 TYR B 79 THR B 93 THR B 94
SITE 2 AC1 12 ASP B 95 SER B 119 THR B 120 LYS B 122
SITE 3 AC1 12 TRP B 139 PRO D 111 HIS D 112 ARG D 115
CRYST1 65.252 74.953 103.775 90.89 93.33 115.72 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 0.015325 0.007382 0.001227 0.00000
SCALE2 0.000000 0.014809 0.000671 0.00000
SCALE3 0.000000 0.000000 0.009662 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
