HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 18-FEB-13 4JA8
TITLE COMPLEX OF MITOCHONDRIAL ISOCITRATE DEHYDROGENASE R140Q MUTANT WITH
TITLE 2 AGI-6780 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 41-452;
COMPND 5 SYNONYM: IDH, ICD-M, IDP, NADP(+)-SPECIFIC ICDH, OXALOSUCCINATE
COMPND 6 DECARBOXYLASE;
COMPND 7 EC: 1.1.1.42;
COMPND 8 ENGINEERED: YES;
COMPND 9 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: IDH2
KEYWDS PROTEIN-INHIBITOR COMPLEX, METABOLIC ENZYME ONCOMETABOLITE,
KEYWDS 2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR W.WEI,L.CHEN,M.WU,F.JIANG,J.TRAVINS,K.QIAN,B.DELABARRE
REVDAT 5 28-FEB-24 4JA8 1 REMARK SEQADV LINK
REVDAT 4 15-NOV-17 4JA8 1 REMARK
REVDAT 3 15-MAY-13 4JA8 1 JRNL
REVDAT 2 17-APR-13 4JA8 1 JRNL
REVDAT 1 10-APR-13 4JA8 0
JRNL AUTH F.WANG,J.TRAVINS,B.DELABARRE,V.PENARD-LACRONIQUE,S.SCHALM,
JRNL AUTH 2 E.HANSEN,K.STRALEY,A.KERNYTSKY,W.LIU,C.GLISER,H.YANG,
JRNL AUTH 3 S.GROSS,E.ARTIN,V.SAADA,E.MYLONAS,C.QUIVORON,
JRNL AUTH 4 J.POPOVICI-MULLER,J.O.SAUNDERS,F.G.SALITURO,S.YAN,S.MURRAY,
JRNL AUTH 5 W.WEI,Y.GAO,L.DANG,M.DORSCH,S.AGRESTA,D.P.SCHENKEIN,
JRNL AUTH 6 S.A.BILLER,S.M.SU,S.DE BOTTON,K.E.YEN
JRNL TITL TARGETED INHIBITION OF MUTANT IDH2 IN LEUKEMIA CELLS INDUCES
JRNL TITL 2 CELLULAR DIFFERENTIATION.
JRNL REF SCIENCE V. 340 622 2013
JRNL REFN ISSN 0036-8075
JRNL PMID 23558173
JRNL DOI 10.1126/SCIENCE.1234769
REMARK 2
REMARK 2 RESOLUTION. 1.55 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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 127987
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6429
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8533
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE SET COUNT : 479
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6537
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 154
REMARK 3 SOLVENT ATOMS : 746
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.01000
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): 0.083
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.086
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.053
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.438
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7061 ; 0.028 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9584 ; 2.145 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 856 ; 6.217 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 318 ;34.082 ;24.308
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1228 ;14.552 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;18.280 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1033 ; 0.285 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5324 ; 0.013 ; 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): 4185 ; 1.300 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6786 ; 2.100 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2876 ; 3.187 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2792 ; 4.721 ; 4.500
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 : 1.40
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4JA8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000077791.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
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 : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 128343
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.42200
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF THE IDH2/R140Q:AGI-6780
REMARK 280 COMPLEX WERE GROWN BY HANGING DROP VAPOR DIFFUSION AT 18C AFTER
REMARK 280 MIXING THE IDH2/R140Q:AGI-6780 SAMPLE WITH A 2 TO 1 VOLUME OF
REMARK 280 PROTEIN TO RESERVOIR SOLUTION. RESERVOIR SOLUTION WAS COMPRISED
REMARK 280 OF 0.2 M CALCIUM CHLORIDE, 0.1 M TRIS (PH 8.5) AND 25 % W/V PEG
REMARK 280 4000. SEEDING METHODS WERE USED TO GROW DIFFRACTION QUALITY
REMARK 280 CRYSTALS, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 29.32800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.77100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.83050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.77100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.32800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.83050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 ASP B 41
REMARK 465 LYS B 42
REMARK 465 LEU B 449
REMARK 465 GLY B 450
REMARK 465 ARG B 451
REMARK 465 GLN B 452
REMARK 465 HIS B 453
REMARK 465 HIS B 454
REMARK 465 HIS B 455
REMARK 465 HIS B 456
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 CE MET A 330 O HOH A 993 2.04
REMARK 500 O HOH A 930 O HOH A 993 2.06
REMARK 500 OE2 GLU B 286 NH1 ARG B 288 2.06
REMARK 500 O HOH B 620 O HOH B 849 2.06
REMARK 500 O HOH A 1026 O HOH B 679 2.11
REMARK 500 O HOH A 936 O HOH A 989 2.11
REMARK 500 O HOH B 874 O HOH B 875 2.16
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 VAL A 185 CB VAL A 185 CG1 0.141
REMARK 500 VAL A 209 CB VAL A 209 CG1 0.132
REMARK 500 GLY A 216 N GLY A 216 CA 0.097
REMARK 500 TYR A 238 CE2 TYR A 238 CD2 0.092
REMARK 500 TYR B 285 CE1 TYR B 285 CZ 0.080
REMARK 500 GLU B 345 CD GLU B 345 OE2 0.074
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 ASP A 177 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 271 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 356 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 362 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG A 362 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 447 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 89 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 57 -133.39 55.64
REMARK 500 ILE A 71 -60.36 -105.14
REMARK 500 SER A 108 -16.27 81.62
REMARK 500 ALA A 174 55.25 -96.94
REMARK 500 ASP A 177 -132.12 54.89
REMARK 500 LYS A 180 37.51 -141.26
REMARK 500 GLU B 57 -134.65 57.82
REMARK 500 ILE B 71 -71.67 -99.17
REMARK 500 SER B 108 -22.10 84.45
REMARK 500 ALA B 174 52.65 -99.51
REMARK 500 ASP B 177 -136.84 51.35
REMARK 500 ALA B 214 -168.63 -162.52
REMARK 500 GLU B 429 -63.01 -103.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 291 OD2
REMARK 620 2 HOH A 601 O 71.3
REMARK 620 3 ASP B 314 OD2 90.2 93.4
REMARK 620 4 ASP B 318 OD2 72.7 135.1 112.7
REMARK 620 5 ASP B 318 OD1 117.1 134.1 129.5 49.2
REMARK 620 6 HOH B 603 O 163.7 120.2 78.0 101.2 64.7
REMARK 620 7 HOH B 819 O 81.8 67.6 160.9 81.6 69.3 112.7
REMARK 620 8 HOH B 847 O 142.9 78.8 113.4 118.5 70.2 53.4 66.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 314 OD2
REMARK 620 2 ASP A 318 OD2 113.8
REMARK 620 3 ASP A 318 OD1 129.5 50.5
REMARK 620 4 HOH A 871 O 79.6 101.9 62.7
REMARK 620 5 ASP B 291 OD1 92.7 75.0 119.3 169.9
REMARK 620 6 HOH B 601 O 89.8 142.7 133.2 110.9 75.4
REMARK 620 7 HOH B 602 O 157.6 82.6 72.6 113.1 76.3 68.6
REMARK 620 N 1 2 3 4 5 6
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1K9 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 502
DBREF 4JA8 A 41 452 UNP P48735 IDHP_HUMAN 41 452
DBREF 4JA8 B 41 452 UNP P48735 IDHP_HUMAN 41 452
SEQADV 4JA8 GLN A 140 UNP P48735 ARG 140 ENGINEERED MUTATION
SEQADV 4JA8 HIS A 453 UNP P48735 EXPRESSION TAG
SEQADV 4JA8 HIS A 454 UNP P48735 EXPRESSION TAG
SEQADV 4JA8 HIS A 455 UNP P48735 EXPRESSION TAG
SEQADV 4JA8 HIS A 456 UNP P48735 EXPRESSION TAG
SEQADV 4JA8 GLN B 140 UNP P48735 ARG 140 ENGINEERED MUTATION
SEQADV 4JA8 HIS B 453 UNP P48735 EXPRESSION TAG
SEQADV 4JA8 HIS B 454 UNP P48735 EXPRESSION TAG
SEQADV 4JA8 HIS B 455 UNP P48735 EXPRESSION TAG
SEQADV 4JA8 HIS B 456 UNP P48735 EXPRESSION TAG
SEQRES 1 A 416 ASP LYS ARG ILE LYS VAL ALA LYS PRO VAL VAL GLU MET
SEQRES 2 A 416 ASP GLY ASP GLU MET THR ARG ILE ILE TRP GLN PHE ILE
SEQRES 3 A 416 LYS GLU LYS LEU ILE LEU PRO HIS VAL ASP ILE GLN LEU
SEQRES 4 A 416 LYS TYR PHE ASP LEU GLY LEU PRO ASN ARG ASP GLN THR
SEQRES 5 A 416 ASP ASP GLN VAL THR ILE ASP SER ALA LEU ALA THR GLN
SEQRES 6 A 416 LYS TYR SER VAL ALA VAL LYS CYS ALA THR ILE THR PRO
SEQRES 7 A 416 ASP GLU ALA ARG VAL GLU GLU PHE LYS LEU LYS LYS MET
SEQRES 8 A 416 TRP LYS SER PRO ASN GLY THR ILE GLN ASN ILE LEU GLY
SEQRES 9 A 416 GLY THR VAL PHE ARG GLU PRO ILE ILE CYS LYS ASN ILE
SEQRES 10 A 416 PRO ARG LEU VAL PRO GLY TRP THR LYS PRO ILE THR ILE
SEQRES 11 A 416 GLY ARG HIS ALA HIS GLY ASP GLN TYR LYS ALA THR ASP
SEQRES 12 A 416 PHE VAL ALA ASP ARG ALA GLY THR PHE LYS MET VAL PHE
SEQRES 13 A 416 THR PRO LYS ASP GLY SER GLY VAL LYS GLU TRP GLU VAL
SEQRES 14 A 416 TYR ASN PHE PRO ALA GLY GLY VAL GLY MET GLY MET TYR
SEQRES 15 A 416 ASN THR ASP GLU SER ILE SER GLY PHE ALA HIS SER CYS
SEQRES 16 A 416 PHE GLN TYR ALA ILE GLN LYS LYS TRP PRO LEU TYR MET
SEQRES 17 A 416 SER THR LYS ASN THR ILE LEU LYS ALA TYR ASP GLY ARG
SEQRES 18 A 416 PHE LYS ASP ILE PHE GLN GLU ILE PHE ASP LYS HIS TYR
SEQRES 19 A 416 LYS THR ASP PHE ASP LYS ASN LYS ILE TRP TYR GLU HIS
SEQRES 20 A 416 ARG LEU ILE ASP ASP MET VAL ALA GLN VAL LEU LYS SER
SEQRES 21 A 416 SER GLY GLY PHE VAL TRP ALA CYS LYS ASN TYR ASP GLY
SEQRES 22 A 416 ASP VAL GLN SER ASP ILE LEU ALA GLN GLY PHE GLY SER
SEQRES 23 A 416 LEU GLY LEU MET THR SER VAL LEU VAL CYS PRO ASP GLY
SEQRES 24 A 416 LYS THR ILE GLU ALA GLU ALA ALA HIS GLY THR VAL THR
SEQRES 25 A 416 ARG HIS TYR ARG GLU HIS GLN LYS GLY ARG PRO THR SER
SEQRES 26 A 416 THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG GLY
SEQRES 27 A 416 LEU GLU HIS ARG GLY LYS LEU ASP GLY ASN GLN ASP LEU
SEQRES 28 A 416 ILE ARG PHE ALA GLN MET LEU GLU LYS VAL CYS VAL GLU
SEQRES 29 A 416 THR VAL GLU SER GLY ALA MET THR LYS ASP LEU ALA GLY
SEQRES 30 A 416 CYS ILE HIS GLY LEU SER ASN VAL LYS LEU ASN GLU HIS
SEQRES 31 A 416 PHE LEU ASN THR THR ASP PHE LEU ASP THR ILE LYS SER
SEQRES 32 A 416 ASN LEU ASP ARG ALA LEU GLY ARG GLN HIS HIS HIS HIS
SEQRES 1 B 416 ASP LYS ARG ILE LYS VAL ALA LYS PRO VAL VAL GLU MET
SEQRES 2 B 416 ASP GLY ASP GLU MET THR ARG ILE ILE TRP GLN PHE ILE
SEQRES 3 B 416 LYS GLU LYS LEU ILE LEU PRO HIS VAL ASP ILE GLN LEU
SEQRES 4 B 416 LYS TYR PHE ASP LEU GLY LEU PRO ASN ARG ASP GLN THR
SEQRES 5 B 416 ASP ASP GLN VAL THR ILE ASP SER ALA LEU ALA THR GLN
SEQRES 6 B 416 LYS TYR SER VAL ALA VAL LYS CYS ALA THR ILE THR PRO
SEQRES 7 B 416 ASP GLU ALA ARG VAL GLU GLU PHE LYS LEU LYS LYS MET
SEQRES 8 B 416 TRP LYS SER PRO ASN GLY THR ILE GLN ASN ILE LEU GLY
SEQRES 9 B 416 GLY THR VAL PHE ARG GLU PRO ILE ILE CYS LYS ASN ILE
SEQRES 10 B 416 PRO ARG LEU VAL PRO GLY TRP THR LYS PRO ILE THR ILE
SEQRES 11 B 416 GLY ARG HIS ALA HIS GLY ASP GLN TYR LYS ALA THR ASP
SEQRES 12 B 416 PHE VAL ALA ASP ARG ALA GLY THR PHE LYS MET VAL PHE
SEQRES 13 B 416 THR PRO LYS ASP GLY SER GLY VAL LYS GLU TRP GLU VAL
SEQRES 14 B 416 TYR ASN PHE PRO ALA GLY GLY VAL GLY MET GLY MET TYR
SEQRES 15 B 416 ASN THR ASP GLU SER ILE SER GLY PHE ALA HIS SER CYS
SEQRES 16 B 416 PHE GLN TYR ALA ILE GLN LYS LYS TRP PRO LEU TYR MET
SEQRES 17 B 416 SER THR LYS ASN THR ILE LEU LYS ALA TYR ASP GLY ARG
SEQRES 18 B 416 PHE LYS ASP ILE PHE GLN GLU ILE PHE ASP LYS HIS TYR
SEQRES 19 B 416 LYS THR ASP PHE ASP LYS ASN LYS ILE TRP TYR GLU HIS
SEQRES 20 B 416 ARG LEU ILE ASP ASP MET VAL ALA GLN VAL LEU LYS SER
SEQRES 21 B 416 SER GLY GLY PHE VAL TRP ALA CYS LYS ASN TYR ASP GLY
SEQRES 22 B 416 ASP VAL GLN SER ASP ILE LEU ALA GLN GLY PHE GLY SER
SEQRES 23 B 416 LEU GLY LEU MET THR SER VAL LEU VAL CYS PRO ASP GLY
SEQRES 24 B 416 LYS THR ILE GLU ALA GLU ALA ALA HIS GLY THR VAL THR
SEQRES 25 B 416 ARG HIS TYR ARG GLU HIS GLN LYS GLY ARG PRO THR SER
SEQRES 26 B 416 THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG GLY
SEQRES 27 B 416 LEU GLU HIS ARG GLY LYS LEU ASP GLY ASN GLN ASP LEU
SEQRES 28 B 416 ILE ARG PHE ALA GLN MET LEU GLU LYS VAL CYS VAL GLU
SEQRES 29 B 416 THR VAL GLU SER GLY ALA MET THR LYS ASP LEU ALA GLY
SEQRES 30 B 416 CYS ILE HIS GLY LEU SER ASN VAL LYS LEU ASN GLU HIS
SEQRES 31 B 416 PHE LEU ASN THR THR ASP PHE LEU ASP THR ILE LYS SER
SEQRES 32 B 416 ASN LEU ASP ARG ALA LEU GLY ARG GLN HIS HIS HIS HIS
HET NDP A 501 48
HET 1K9 A 502 64
HET CA A 503 1
HET GOL A 504 6
HET GOL A 505 6
HET GOL A 506 6
HET GOL A 507 6
HET NDP B 501 48
HET CA B 502 1
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM 1K9 1-[5-(CYCLOPROPYLSULFAMOYL)-2-THIOPHEN-3-YL-PHENYL]-3-
HETNAM 2 1K9 [3-(TRIFLUOROMETHYL)PHENYL]UREA
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NDP 2(C21 H30 N7 O17 P3)
FORMUL 4 1K9 C21 H18 F3 N3 O3 S2
FORMUL 5 CA 2(CA 2+)
FORMUL 6 GOL 4(C3 H8 O3)
FORMUL 12 HOH *746(H2 O)
HELIX 1 1 ASP A 56 LEU A 70 1 15
HELIX 2 2 GLY A 85 THR A 92 1 8
HELIX 3 3 ASP A 94 SER A 108 1 15
HELIX 4 4 ASP A 119 LYS A 127 1 9
HELIX 5 5 SER A 134 GLY A 144 1 11
HELIX 6 6 GLY A 176 ALA A 181 5 6
HELIX 7 7 ASP A 225 LYS A 243 1 19
HELIX 8 8 ALA A 257 TYR A 274 1 18
HELIX 9 9 TYR A 274 ASN A 281 1 8
HELIX 10 10 ILE A 290 SER A 300 1 11
HELIX 11 11 LYS A 309 PHE A 324 1 16
HELIX 12 12 SER A 326 GLY A 328 5 3
HELIX 13 13 VAL A 351 LYS A 360 1 10
HELIX 14 14 PRO A 368 GLY A 387 1 20
HELIX 15 15 ASN A 388 SER A 408 1 21
HELIX 16 16 THR A 412 GLY A 421 1 10
HELIX 17 17 LEU A 422 VAL A 425 5 4
HELIX 18 18 ASN A 433 HIS A 456 1 24
HELIX 19 19 ASP B 56 LEU B 70 1 15
HELIX 20 20 ILE B 71 PRO B 73 5 3
HELIX 21 21 GLY B 85 THR B 92 1 8
HELIX 22 22 ASP B 94 SER B 108 1 15
HELIX 23 23 ASP B 119 LYS B 127 1 9
HELIX 24 24 SER B 134 GLY B 144 1 11
HELIX 25 25 GLY B 176 ALA B 181 5 6
HELIX 26 26 ASP B 225 LYS B 243 1 19
HELIX 27 27 ALA B 257 TYR B 274 1 18
HELIX 28 28 TYR B 274 ASN B 281 1 8
HELIX 29 29 ILE B 290 SER B 300 1 11
HELIX 30 30 LYS B 309 PHE B 324 1 16
HELIX 31 31 SER B 326 GLY B 328 5 3
HELIX 32 32 VAL B 351 LYS B 360 1 10
HELIX 33 33 PRO B 368 ASP B 386 1 19
HELIX 34 34 ASN B 388 GLY B 409 1 22
HELIX 35 35 THR B 412 GLY B 421 1 10
HELIX 36 36 LEU B 422 VAL B 425 5 4
HELIX 37 37 ASN B 433 ALA B 448 1 16
SHEET 1 A 2 ILE A 44 LYS A 45 0
SHEET 2 A 2 VAL A 75 ASP A 76 1 O ASP A 76 N ILE A 44
SHEET 1 B10 LEU A 79 ASP A 83 0
SHEET 2 B10 VAL A 50 ASP A 54 1 N GLU A 52 O PHE A 82
SHEET 3 B10 VAL A 109 LYS A 112 1 O VAL A 109 N VAL A 51
SHEET 4 B10 ILE A 342 ALA A 346 1 O ALA A 344 N ALA A 110
SHEET 5 B10 MET A 330 VAL A 335 -1 N LEU A 334 O GLU A 343
SHEET 6 B10 THR A 146 PRO A 151 -1 N THR A 146 O VAL A 335
SHEET 7 B10 ILE A 168 ARG A 172 -1 O ILE A 170 N ARG A 149
SHEET 8 B10 PHE A 304 CYS A 308 1 O TRP A 306 N THR A 169
SHEET 9 B10 LEU A 246 THR A 250 1 N TYR A 247 O ALA A 307
SHEET 10 B10 TYR A 285 LEU A 289 1 O ARG A 288 N MET A 248
SHEET 1 C 4 THR A 182 ALA A 186 0
SHEET 2 C 4 GLY A 216 THR A 224 -1 O GLY A 216 N ALA A 186
SHEET 3 C 4 GLY B 216 THR B 224 -1 O ASN B 223 N VAL A 217
SHEET 4 C 4 THR B 182 ALA B 186 -1 N THR B 182 O GLY B 220
SHEET 1 D 4 LYS A 205 PHE A 212 0
SHEET 2 D 4 GLY A 190 PRO A 198 -1 N PHE A 192 O TYR A 210
SHEET 3 D 4 GLY B 190 PRO B 198 -1 O LYS B 193 N VAL A 195
SHEET 4 D 4 LYS B 205 PHE B 212 -1 O TYR B 210 N PHE B 192
SHEET 1 E 2 ILE B 44 LYS B 45 0
SHEET 2 E 2 VAL B 75 ASP B 76 1 O ASP B 76 N ILE B 44
SHEET 1 F10 LEU B 79 ASP B 83 0
SHEET 2 F10 VAL B 50 ASP B 54 1 N ASP B 54 O PHE B 82
SHEET 3 F10 VAL B 109 LYS B 112 1 O VAL B 111 N MET B 53
SHEET 4 F10 ILE B 342 ALA B 346 1 O ALA B 344 N LYS B 112
SHEET 5 F10 MET B 330 VAL B 335 -1 N LEU B 334 O GLU B 343
SHEET 6 F10 THR B 146 PRO B 151 -1 N THR B 146 O VAL B 335
SHEET 7 F10 ILE B 168 ARG B 172 -1 O ILE B 170 N ARG B 149
SHEET 8 F10 PHE B 304 CYS B 308 1 O CYS B 308 N GLY B 171
SHEET 9 F10 LEU B 246 THR B 250 1 N TYR B 247 O ALA B 307
SHEET 10 F10 TYR B 285 LEU B 289 1 O ARG B 288 N MET B 248
LINK OD2 ASP A 291 CA CA B 502 1555 1555 2.34
LINK OD2 ASP A 314 CA CA A 503 1555 1555 2.10
LINK OD2 ASP A 318 CA CA A 503 1555 1555 2.52
LINK OD1 ASP A 318 CA CA A 503 1555 1555 2.62
LINK CA CA A 503 O HOH A 871 1555 1555 2.66
LINK CA CA A 503 OD1 ASP B 291 1555 1555 2.30
LINK CA CA A 503 O HOH B 601 1555 1555 2.62
LINK CA CA A 503 O HOH B 602 1555 1555 2.56
LINK O HOH A 601 CA CA B 502 1555 1555 2.45
LINK OD2 ASP B 314 CA CA B 502 1555 1555 2.20
LINK OD2 ASP B 318 CA CA B 502 1555 1555 2.42
LINK OD1 ASP B 318 CA CA B 502 1555 1555 2.70
LINK CA CA B 502 O HOH B 603 1555 1555 2.53
LINK CA CA B 502 O HOH B 819 1555 1555 2.56
LINK CA CA B 502 O HOH B 847 1555 1555 2.46
SITE 1 AC1 26 LYS A 112 ALA A 114 THR A 115 ILE A 116
SITE 2 AC1 26 THR A 117 ARG A 122 ASN A 136 GLU A 345
SITE 3 AC1 26 HIS A 348 GLY A 349 THR A 350 VAL A 351
SITE 4 AC1 26 THR A 352 ARG A 353 HIS A 354 ASN A 367
SITE 5 AC1 26 GOL A 505 HOH A 608 HOH A 642 HOH A 659
SITE 6 AC1 26 HOH A 668 HOH A 686 HOH A 692 HOH A 784
SITE 7 AC1 26 HOH A 874 HOH A 980
SITE 1 AC2 22 TRP A 164 VAL A 294 VAL A 297 LEU A 298
SITE 2 AC2 22 TRP A 306 TYR A 311 ASP A 312 VAL A 315
SITE 3 AC2 22 GLN A 316 ILE A 319 LEU A 320 TRP B 164
SITE 4 AC2 22 VAL B 294 VAL B 297 LEU B 298 TRP B 306
SITE 5 AC2 22 TYR B 311 ASP B 312 VAL B 315 GLN B 316
SITE 6 AC2 22 ILE B 319 LEU B 320
SITE 1 AC3 6 ASP A 314 ASP A 318 HOH A 871 ASP B 291
SITE 2 AC3 6 HOH B 601 HOH B 602
SITE 1 AC4 7 ASP A 271 LYS A 272 HIS A 273 TYR A 274
SITE 2 AC4 7 LYS A 275 THR A 276 HOH A 799
SITE 1 AC5 4 THR A 117 SER A 134 ASN A 136 NDP A 501
SITE 1 AC6 8 VAL A 185 ALA A 186 ASP A 187 ARG A 188
SITE 2 AC6 8 HOH A 954 PHE B 196 LYS B 205 HOH B 735
SITE 1 AC7 8 LYS A 280 LYS A 282 GLU A 404 ASN A 444
SITE 2 AC7 8 HOH A 660 HOH A 739 HOH A 830 HOH A1019
SITE 1 AC8 24 LYS B 112 ALA B 114 THR B 115 THR B 117
SITE 2 AC8 24 ARG B 122 ASN B 136 LEU B 327 GLU B 345
SITE 3 AC8 24 HIS B 348 GLY B 349 THR B 350 VAL B 351
SITE 4 AC8 24 THR B 352 ARG B 353 HIS B 354 ASN B 367
SITE 5 AC8 24 HOH B 673 HOH B 685 HOH B 704 HOH B 765
SITE 6 AC8 24 HOH B 781 HOH B 800 HOH B 839 HOH B 864
SITE 1 AC9 7 ASP A 291 HOH A 601 ASP B 314 ASP B 318
SITE 2 AC9 7 HOH B 603 HOH B 819 HOH B 847
CRYST1 58.656 119.661 125.542 90.00 90.00 90.00 P 21 21 21 8
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 0.017049 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008357 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007965 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
