HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 22-JAN-16 5HQY
TITLE HUMAN DIHYDROFOLATE REDUCTASE COMPLEX WITH NADPH AND 5-METHYL-6-(2',
TITLE 2 3',4'-TRIFLUOROPHENYLTHIO)THIENO[2,3-D]PYRIMIDINE-2,4-DIAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.5.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DHFR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDS5
KEYWDS OXIDOREDUCTASE TERNARY COMPLEX WITH TRIFLUOROMETHYL INHIBITOR,
KEYWDS 2 OXIDOREDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR V.CODY
REVDAT 4 27-SEP-23 5HQY 1 REMARK
REVDAT 3 11-DEC-19 5HQY 1 REMARK
REVDAT 2 20-SEP-17 5HQY 1 REMARK
REVDAT 1 25-JAN-17 5HQY 0
JRNL AUTH V.CODY,A.GANGJEE
JRNL TITL HUMAN DIHYDROFOLATE REDUCTASE TERNARY COMPLEX WITH A SERIES
JRNL TITL 2 OF FLUORINE SUBSTITUTED
JRNL TITL 3 5-METHYL-6-PHENYTHIO)THIENO[2,3-D]PYRIMIDINE-2,4-DIAMINES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 34399
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1805
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) : 1.46
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.50
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2484
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.3660
REMARK 3 BIN FREE R VALUE SET COUNT : 143
REMARK 3 BIN FREE R VALUE : 0.4220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1502
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 93
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.086
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.744
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1637 ; 0.029 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2227 ; 2.744 ; 2.051
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 185 ; 7.125 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 71 ;36.549 ;24.789
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 286 ;16.370 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;14.015 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 233 ; 0.201 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1228 ; 0.016 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 : NULL
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 5HQY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000217569.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.975
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36204
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460
REMARK 200 RESOLUTION RANGE LOW (A) : 34.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 1.500
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : 0.02000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 41.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1.40
REMARK 200 R MERGE FOR SHELL (I) : 0.09400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1U72
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM KP04, 60% AMSO4, 3%V/V ETOH, PH
REMARK 280 6.9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.25800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.97502
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 25.54900
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 43.25800
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 24.97502
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 25.54900
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 43.25800
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 24.97502
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 25.54900
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.95004
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 51.09800
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 49.95004
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 51.09800
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 49.95004
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 51.09800
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 TOTAL BURIED SURFACE AREA: 1190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS 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 TYR A 162 O HOH A 301 1.16
REMARK 500 CB SER A 59 O HOH A 304 1.47
REMARK 500 O ALA A 86 O HOH A 302 1.57
REMARK 500 C ALA A 86 O HOH A 302 1.67
REMARK 500 ND2 ASN A 5 O HOH A 303 1.74
REMARK 500 C TYR A 162 O HOH A 301 1.75
REMARK 500 CG ASN A 5 O HOH A 303 1.75
REMARK 500 O HOH A 328 O HOH A 385 1.83
REMARK 500 O HOH A 311 O HOH A 339 2.07
REMARK 500 O HOH A 355 O HOH A 381 2.13
REMARK 500 N HIS A 87 O HOH A 302 2.18
REMARK 500 O2D NDP A 201 FAE 63Y A 203 2.19
REMARK 500 CB SER A 167 O HOH A 317 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 345 O HOH A 386 8554 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 87 NE2 HIS A 87 CD2 -0.071
REMARK 500 HIS A 130 CG HIS A 130 CD2 0.061
REMARK 500 SER A 167 CB SER A 167 OG -0.091
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 70 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 70 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 VAL A 112 CA - CB - CG1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 ASP A 152 CB - CG - OD1 ANGL. DEV. = -6.5 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 ASP A 110 -95.02 -76.92
REMARK 500 MET A 139 34.58 -84.10
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 NDP A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 63Y A 202 and 63Y A
REMARK 800 203
DBREF 5HQY A 1 186 UNP P00374 DYR_HUMAN 2 187
SEQRES 1 A 186 VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN ASN
SEQRES 2 A 186 MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO PRO
SEQRES 3 A 186 LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR THR
SEQRES 4 A 186 THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE MET
SEQRES 5 A 186 GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN ARG
SEQRES 6 A 186 PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG GLU
SEQRES 7 A 186 LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER ARG
SEQRES 8 A 186 SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO GLU
SEQRES 9 A 186 LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY GLY
SEQRES 10 A 186 SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY HIS
SEQRES 11 A 186 LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE GLU
SEQRES 12 A 186 SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS TYR
SEQRES 13 A 186 LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP VAL
SEQRES 14 A 186 GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL TYR
SEQRES 15 A 186 GLU LYS ASN ASP
HET NDP A 201 48
HET 63Y A 202 22
HET 63Y A 203 22
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM 63Y 5-METHYL-6-[(2,3,4-TRIFLUOROPHENYL)SULFANYL]THIENO[2,3-
HETNAM 2 63Y D]PYRIMIDINE-2,4-DIAMINE
FORMUL 2 NDP C21 H30 N7 O17 P3
FORMUL 3 63Y 2(C13 H9 F3 N4 S2)
FORMUL 5 HOH *93(H2 O)
HELIX 1 AA1 LEU A 27 THR A 40 1 14
HELIX 2 AA2 LYS A 54 ILE A 60 1 7
HELIX 3 AA3 PRO A 61 ARG A 65 5 5
HELIX 4 AA4 SER A 92 GLU A 101 1 10
HELIX 5 AA5 GLN A 102 ASN A 107 1 6
HELIX 6 AA6 GLY A 117 ASN A 126 1 10
SHEET 1 AA1 8 PHE A 88 SER A 90 0
SHEET 2 AA1 8 ILE A 71 LEU A 75 1 N VAL A 74 O SER A 90
SHEET 3 AA1 8 GLN A 47 GLY A 53 1 N VAL A 50 O ILE A 71
SHEET 4 AA1 8 VAL A 109 ILE A 114 1 O TRP A 113 N LEU A 49
SHEET 5 AA1 8 LEU A 4 SER A 11 1 N ASN A 5 O ILE A 114
SHEET 6 AA1 8 HIS A 130 ILE A 138 1 O THR A 136 N VAL A 10
SHEET 7 AA1 8 ILE A 175 ASN A 185 -1 O LYS A 178 N ARG A 137
SHEET 8 AA1 8 LYS A 157 LEU A 158 -1 N LYS A 157 O GLU A 183
SHEET 1 AA2 8 PHE A 88 SER A 90 0
SHEET 2 AA2 8 ILE A 71 LEU A 75 1 N VAL A 74 O SER A 90
SHEET 3 AA2 8 GLN A 47 GLY A 53 1 N VAL A 50 O ILE A 71
SHEET 4 AA2 8 VAL A 109 ILE A 114 1 O TRP A 113 N LEU A 49
SHEET 5 AA2 8 LEU A 4 SER A 11 1 N ASN A 5 O ILE A 114
SHEET 6 AA2 8 HIS A 130 ILE A 138 1 O THR A 136 N VAL A 10
SHEET 7 AA2 8 ILE A 175 ASN A 185 -1 O LYS A 178 N ARG A 137
SHEET 8 AA2 8 GLN A 170 GLU A 172 -1 N GLN A 170 O TYR A 177
SHEET 1 AA3 2 GLY A 15 GLY A 17 0
SHEET 2 AA3 2 THR A 146 PHE A 147 -1 O THR A 146 N ILE A 16
LINK C4 63Y A 202 N3 63Y A 203 1555 1555 1.20
LINK C4 63Y A 202 C5 63Y A 203 1555 1555 1.63
LINK C4 63Y A 202 SAL 63Y A 203 1555 1555 1.88
LINK C5 63Y A 202 C4 63Y A 203 1555 1555 1.27
LINK C5 63Y A 202 C6 63Y A 203 1555 1555 1.41
LINK C6 63Y A 202 C5 63Y A 203 1555 1555 1.48
LINK N1 63Y A 202 C6 63Y A 203 1555 1555 1.56
LINK N3 63Y A 202 C2 63Y A 203 1555 1555 1.37
LINK N3 63Y A 202 C4 63Y A 203 1555 1555 1.50
LINK FAF 63Y A 202 CAG 63Y A 203 1555 1555 1.56
LINK CAS 63Y A 202 CAH 63Y A 203 1555 1555 1.49
LINK CAS 63Y A 202 SAK 63Y A 203 1555 1555 1.79
LINK CAQ 63Y A 202 CAQ 63Y A 203 1555 1555 1.34
LINK CAT 63Y A 202 CAT 63Y A 203 1555 1555 1.13
LINK CAT 63Y A 202 SAL 63Y A 203 1555 1555 1.89
LINK CAT 63Y A 202 CAP 63Y A 203 1555 1555 1.65
LINK SAL 63Y A 202 C4 63Y A 203 1555 1555 1.74
LINK SAL 63Y A 202 CAT 63Y A 203 1555 1555 1.91
LINK C2 63Y A 202 N3 63Y A 203 1555 1555 1.33
LINK C2 63Y A 202 N1 63Y A 203 1555 1555 1.55
LINK NAB 63Y A 202 C2 63Y A 203 1555 1555 1.56
LINK CAP 63Y A 202 C5 63Y A 203 1555 1555 1.35
LINK CAA 63Y A 202 CAA 63Y A 203 1555 1555 1.26
CISPEP 1 ARG A 65 PRO A 66 0 -8.94
CISPEP 2 GLY A 116 GLY A 117 0 12.34
SITE 1 AC1 31 VAL A 8 ALA A 9 ILE A 16 GLY A 17
SITE 2 AC1 31 GLY A 20 ASP A 21 LEU A 22 GLY A 53
SITE 3 AC1 31 LYS A 54 LYS A 55 THR A 56 SER A 59
SITE 4 AC1 31 LEU A 75 SER A 76 ARG A 77 GLU A 78
SITE 5 AC1 31 ARG A 91 SER A 92 VAL A 115 GLY A 117
SITE 6 AC1 31 SER A 118 SER A 119 TYR A 121 THR A 146
SITE 7 AC1 31 63Y A 202 63Y A 203 HOH A 306 HOH A 309
SITE 8 AC1 31 HOH A 319 HOH A 346 HOH A 356
SITE 1 AC2 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AC2 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AC2 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AC2 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AC2 18 NDP A 201 HOH A 391
SITE 1 AC3 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AC3 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AC3 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AC3 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AC3 18 NDP A 201 HOH A 391
SITE 1 AC4 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AC4 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AC4 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AC4 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AC4 18 NDP A 201 HOH A 391
SITE 1 AC5 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AC5 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AC5 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AC5 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AC5 18 NDP A 201 HOH A 391
SITE 1 AC6 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AC6 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AC6 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AC6 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AC6 18 NDP A 201 HOH A 391
SITE 1 AC7 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AC7 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AC7 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AC7 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AC7 18 NDP A 201 HOH A 391
SITE 1 AC8 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AC8 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AC8 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AC8 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AC8 18 NDP A 201 HOH A 391
SITE 1 AC9 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AC9 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AC9 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AC9 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AC9 18 NDP A 201 HOH A 391
SITE 1 AD1 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AD1 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AD1 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AD1 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AD1 18 NDP A 201 HOH A 391
SITE 1 AD2 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AD2 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AD2 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AD2 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AD2 18 NDP A 201 HOH A 391
SITE 1 AD3 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AD3 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AD3 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AD3 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AD3 18 NDP A 201 HOH A 391
SITE 1 AD4 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AD4 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AD4 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AD4 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AD4 18 NDP A 201 HOH A 391
SITE 1 AD5 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AD5 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AD5 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AD5 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AD5 18 NDP A 201 HOH A 391
SITE 1 AD6 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AD6 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AD6 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AD6 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AD6 18 NDP A 201 HOH A 391
SITE 1 AD7 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AD7 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AD7 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AD7 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AD7 18 NDP A 201 HOH A 391
SITE 1 AD8 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AD8 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AD8 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AD8 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AD8 18 NDP A 201 HOH A 391
SITE 1 AD9 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AD9 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AD9 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AD9 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AD9 18 NDP A 201 HOH A 391
SITE 1 AE1 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AE1 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AE1 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AE1 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AE1 18 NDP A 201 HOH A 391
SITE 1 AE2 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AE2 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AE2 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AE2 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AE2 18 NDP A 201 HOH A 391
SITE 1 AE3 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AE3 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AE3 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AE3 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AE3 18 NDP A 201 HOH A 391
SITE 1 AE4 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AE4 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AE4 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AE4 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AE4 18 NDP A 201 HOH A 391
SITE 1 AE5 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AE5 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AE5 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AE5 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AE5 18 NDP A 201 HOH A 391
SITE 1 AE6 18 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AE6 18 ASP A 21 LEU A 22 GLU A 30 PHE A 31
SITE 3 AE6 18 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AE6 18 LEU A 67 VAL A 115 TYR A 121 THR A 136
SITE 5 AE6 18 NDP A 201 HOH A 391
CRYST1 86.516 86.516 76.647 90.00 90.00 120.00 H 3 9
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 0.011559 0.006673 0.000000 0.00000
SCALE2 0.000000 0.013347 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013047 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
