HEADER OXIDOREDUCTASE 29-SEP-05 2C2S
TITLE HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND 2,4-DIAMINO-5-
TITLE 2 (1-O-CARBORANYLMETHYL)-6-METHYLPYRIMIDINE, A NOVEL BORON CONTAINING,
TITLE 3 NONCLASSICAL ANTIFOLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A, B;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET11A;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDFR
KEYWDS NONCLASSICAL ANTIFOLATES, LIPOPHILIC ANTIFOLATES, NADP, ONE- CARBON
KEYWDS 2 METABOLISM, OXIDOREDUCTASE, REDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.W.LEUNG,R.C.REYNOLDS,J.M.RIORDAN,D.W.BORHANI
REVDAT 6 08-MAY-19 2C2S 1 REMARK
REVDAT 5 06-MAR-19 2C2S 1 REMARK
REVDAT 4 24-FEB-09 2C2S 1 VERSN
REVDAT 3 17-JUL-07 2C2S 1 JRNL
REVDAT 2 26-JUN-07 2C2S 1 JRNL
REVDAT 1 10-APR-07 2C2S 0
JRNL AUTH R.C.REYNOLDS,S.R.CAMPBELL,R.G.FAIRCHILD,R.L.KISLIUK,
JRNL AUTH 2 P.L.MICCA,S.F.QUEENER,J.M.RIORDAN,W.D.SEDWICK,W.R.WAUD,
JRNL AUTH 3 A.K.W.LEUNG,R.W.DIXON,W.J.SULING,D.W.BORHANI
JRNL TITL NOVEL BORON-CONTAINING, NONCLASSICAL ANTIFOLATES: SYNTHESIS
JRNL TITL 2 AND PRELIMINARY BIOLOGICAL AND STRUCTURAL EVALUATION.
JRNL REF J.MED.CHEM. V. 50 3283 2007
JRNL REFN ISSN 0022-2623
JRNL PMID 17569517
JRNL DOI 10.1021/JM0701977
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.9
REMARK 3 NUMBER OF REFLECTIONS : 61984
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) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3260
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2295
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 42.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 122
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2962
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 146
REMARK 3 SOLVENT ATOMS : 556
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : -0.02000
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): 0.074
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.682
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3344 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2324 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4726 ; 1.553 ; 2.017
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5769 ; 1.213 ; 2.979
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 374 ; 6.022 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 144 ;39.123 ;25.278
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 595 ;12.650 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;12.302 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 493 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3465 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 580 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 512 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2256 ; 0.192 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1486 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1688 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 331 ; 0.132 ; 0.200
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): 10 ; 0.174 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 64 ; 0.202 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 47 ; 0.147 ; 0.200
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5380 23.7040 -1.1690
REMARK 3 T TENSOR
REMARK 3 T11: -0.1272 T22: -0.1407
REMARK 3 T33: -0.1257 T12: -0.0300
REMARK 3 T13: -0.0287 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 2.0098 L22: 1.1534
REMARK 3 L33: 1.6281 L12: 0.3200
REMARK 3 L13: -0.1374 L23: 0.2478
REMARK 3 S TENSOR
REMARK 3 S11: 0.0446 S12: -0.1704 S13: -0.0967
REMARK 3 S21: 0.1947 S22: -0.0426 S23: -0.1054
REMARK 3 S31: 0.1325 S32: 0.0099 S33: -0.0020
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 300
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1790 45.1760 22.7100
REMARK 3 T TENSOR
REMARK 3 T11: -0.1356 T22: -0.1278
REMARK 3 T33: -0.1332 T12: 0.0424
REMARK 3 T13: 0.0057 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 1.1822 L22: 1.5571
REMARK 3 L33: 1.9551 L12: -0.3139
REMARK 3 L13: -0.2629 L23: 0.6835
REMARK 3 S TENSOR
REMARK 3 S11: -0.0844 S12: -0.1846 S13: 0.0463
REMARK 3 S21: 0.1180 S22: 0.0334 S23: 0.0105
REMARK 3 S31: 0.0296 S32: 0.0064 S33: 0.0510
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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.
REMARK 4
REMARK 4 2C2S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1290025677.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAR-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.78300
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65300
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.0
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 43.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.30
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: UNPUBLISHED HUMAN DHFR STRUCTURE
REMARK 200
REMARK 200 REMARK: INTENSITIES WERE CONVERTED TO STRUCTURE FACTORS USING CCP4
REMARK 200 PROGRAM TRUNCATE.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE TERNARY COMPLEX OF DHFR WITH NADPH
REMARK 280 AND 34B WAS FORMED BY MIXING HUMAN DHFR (20 MG/ML IN 25 MM KPO4
REMARK 280 (PH 7.0), 0.1 MM EDTA, AND 3 MM NAN3) WITH 60 MM NADPH, FOLLOWED
REMARK 280 15 MINUTES LATER BY 60 MM OF INHIBITOR IN DMSO (FINAL
REMARK 280 CONCENTRATIONS OF 2 MM NADPH AND 2 MM INHIBITOR). THIS COMPLEX
REMARK 280 SOLUTION WAS MIXED WITH AN EQUAL VOLUME OF PRECIPITANT
REMARK 280 CONTAINING 24-33% PEG 4000, 0.2 M LI2SO4, 0.1 M TRIS CL (PH 7.9-
REMARK 280 8.4), 5% GLYCEROL, AND EQUILIBRATED WITH THE PRECIPITANT BY
REMARK 280 HANGING DROP VAPOR DIFFUSION AT 277 K. THE CRYSTAL GREW IN ABOUT
REMARK 280 3 WEEKS. THE CRYSTAL WAS FLASH-COOLED DIRECTLY IN LIQUID
REMARK 280 NITROGEN AFTER HARVESTING INTO MOTHER LIQUOR CONTAINING 10%
REMARK 280 GLYCEROL., PH 8.00, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.89100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.89100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 43.83550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.93200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.83550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.93200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 47.89100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.83550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 46.93200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 47.89100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.83550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 46.93200
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: PQS
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: PQS
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B2280 LIES ON A SPECIAL POSITION.
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 ARG A 28 NE CZ NH1 NH2
REMARK 470 LYS A 80 CG CD CE NZ
REMARK 470 ARG A 91 NE CZ NH1 NH2
REMARK 470 LYS A 108 CD CE NZ
REMARK 470 ARG B 28 NE CZ NH1 NH2
REMARK 470 GLU B 44 CG CD OE1 OE2
REMARK 470 LYS B 63 CG CD CE NZ
REMARK 470 GLU B 78 CD OE1 OE2
REMARK 470 ARG B 91 CD NE CZ NH1 NH2
REMARK 470 GLU B 150 CG CD OE1 OE2
REMARK 470 GLU B 161 CD OE1 OE2
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 -97.58 -95.22
REMARK 500 MET A 139 49.68 -87.24
REMARK 500 ASP B 110 -96.71 -100.96
REMARK 500 MET B 139 41.90 -88.88
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 A2012 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH A2020 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A2037 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH A2038 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A2100 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B2030 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B2041 DISTANCE = 6.36 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A1187
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 34B A1188
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B1187
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 34B B1188
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1189
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BOZ RELATED DB: PDB
REMARK 900 STRUCTURE-BASED DESIGN AND SYNTHESIS OF LIPOPHILIC 2,4- DIAMINO-6-
REMARK 900 SUBSTITUTED QUINAZOLINES AND THEIR EVALUATION AS INHIBITORS OF
REMARK 900 DIHYDROFOLATE REDUCTASE AND POTENTIAL ANTITUMOR AGENTS
REMARK 900 RELATED ID: 1DHF RELATED DB: PDB
REMARK 900 DIHYDROFOLATE REDUCTASE (DHFR) COMPLEX WITH FOLATE
REMARK 900 RELATED ID: 1DLR RELATED DB: PDB
REMARK 900 DIHYDROFOLATE REDUCTASE (DHFR) MUTANT WITH LEU 22 REPLACED BY PHE
REMARK 900 (L22F) COMPLEXED WITH NADPH AND PIRITREXIM (PTX)
REMARK 900 RELATED ID: 1DLS RELATED DB: PDB
REMARK 900 DIHYDROFOLATE REDUCTASE (DHFR) MUTANT WITH LEU 22 REPLACED BY TYR
REMARK 900 (L22Y) COMPLEXED WITH NADPH AND METHOTREXATE
REMARK 900 RELATED ID: 1DRF RELATED DB: PDB
REMARK 900 DIHYDROFOLATE REDUCTASE COMPLEX WITH FOLATE
REMARK 900 RELATED ID: 1HFP RELATED DB: PDB
REMARK 900 COMPARISON OF TERNARY CRYSTAL COMPLEXES OF HUMAN DIHYDROFOLATE
REMARK 900 REDUCTASE WITH NADPH AND A CLASSICAL ANTITUMOR FUROPYRIMDINE
REMARK 900 RELATED ID: 1HFQ RELATED DB: PDB
REMARK 900 COMPARISON OF TERNARY CRYSTAL COMPLEXES OF HUMAN DIHYDROFOLATE
REMARK 900 REDUCTASE WITH NADPH AND A CLASSICAL ANTITUMOR FUROPYRIMDINE
REMARK 900 RELATED ID: 1HFR RELATED DB: PDB
REMARK 900 COMPARISON OF TERNARY CRYSTAL COMPLEXES OF HUMAN DIHYDROFOLATE
REMARK 900 REDUCTASE WITH NADPH AND A CLASSICAL ANTITUMOR FUROPYRIMDINE
REMARK 900 RELATED ID: 1KMS RELATED DB: PDB
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND 6-([5-
REMARK 900 QUINOLYLAMINO]METHYL)-2,4 -DIAMINO-5-METHYLPYRIDO[2,3-D]PYRIMIDINE
REMARK 900 ( SRI-9439), A LIPOPHILIC ANTIFOLATE
REMARK 900 RELATED ID: 1KMV RELATED DB: PDB
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND (Z)-6-(2-[2,
REMARK 900 5-DIMETHOXYPHENYL] ETHEN-1-YL)-2,4-DIAMINO-5-METHYLPYRIDO[2 ,3-D]
REMARK 900 PYRIMIDINE (SRI-9662), A LIPOPHILICANTIFOLATE
REMARK 900 RELATED ID: 1MVS RELATED DB: PDB
REMARK 900 ANALYSIS OF TWO POLYMORPHIC FORMS OF A PYRIDO[2,3-D]PYRIMIDINE N9-
REMARK 900 C10 REVERSE- BRIDGE ANTIFOLATE BINARYCOMPLEX WITH HUMAN
REMARK 900 DIHYDROFOLATE REDUCTASE
REMARK 900 RELATED ID: 1MVT RELATED DB: PDB
REMARK 900 ANALYSIS OF TWO POLYMORPHIC FORMS OF A PYRIDO[2,3-D]PYRIMIDINE N9-
REMARK 900 C10 REVERSE- BRIDGE ANTIFOLATE BINARYCOMPLEX WITH HUMAN
REMARK 900 DIHYDROFOLATE REDUCTASE
REMARK 900 RELATED ID: 1OHJ RELATED DB: PDB
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE, MONOCLINIC (P21 ) CRYSTAL FORM
REMARK 900 RELATED ID: 1OHK RELATED DB: PDB
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE, ORTHORHOMBIC (P21 21 21) CRYSTAL FORM
REMARK 900 RELATED ID: 1PD8 RELATED DB: PDB
REMARK 900 ANALYSIS OF THREE CRYSTAL STRUCTURE DETERMINATIONS OF A 5-METHYL-6-
REMARK 900 N- METHYLANILINO PYRIDOPYRIMIDINE ANTIFOLATECOMPLEX WITH HUMAN
REMARK 900 DIHYDROFOLATE REDUCTASE
REMARK 900 RELATED ID: 1PD9 RELATED DB: PDB
REMARK 900 ANALYSIS OF THREE CRYSTAL STRUCTURE DETERMINATIONS OF A 5-METHYL-6-
REMARK 900 N- METHYLANILINO PYRIDOPYRIMIDINE ANTIFOLATECOMPLEX WITH HUMAN
REMARK 900 DIHYDROFOLATE REDUCTASE
REMARK 900 RELATED ID: 1PDB RELATED DB: PDB
REMARK 900 ANALYSIS OF THREE CRYSTAL STRUCTURE DETERMINATIONS OF A 5-METHYL-6-
REMARK 900 N- METHYLANILINO PYRIDOPYRIMIDINE ANTIFOLATECOMPLEX WITH HUMAN
REMARK 900 DIHYDROFOLATE REDUCTASE
REMARK 900 RELATED ID: 1S3U RELATED DB: PDB
REMARK 900 STRUCTURE DETERMINATION OF TETRAHYDROQUINAZOLINEANTIFOLATES IN
REMARK 900 COMPLEX WITH HUMAN AND PNEUMOCYSTIS CARINIIDIHYDROFOLATE REDUCTASE:
REMARK 900 CORRELATIONS OF ENZYMESELECTIVITY AND STEREOCHEMISTRY
REMARK 900 RELATED ID: 1S3V RELATED DB: PDB
REMARK 900 STRUCTURE DETERMINATION OF TETRAHYDROQUINAZOLINEANTIFOLATES IN
REMARK 900 COMPLEX WITH HUMAN AND PNEUMOCYSTIS CARINIIDIHYDROFOLATE REDUCTASE:
REMARK 900 CORRELATIONS OF ENZYMESELECTIVITY AND STEREOCHEMISTRY
REMARK 900 RELATED ID: 1S3W RELATED DB: PDB
REMARK 900 STRUCTURE DETERMINATION OF TETRAHYDROQUINAZOLINEANTIFOALTES IN
REMARK 900 COMPLEX WITH HUMAN AND PNEUMOCYSTIS CARINIIDIHYDROFOLATE REDUCTASE:
REMARK 900 CORRELATIONS OF ENZYMESELECTIVITY AND STEREOCHEMISTRY
REMARK 900 RELATED ID: 1U71 RELATED DB: PDB
REMARK 900 UNDERSTANDING THE ROLE OF LEU22 VARIANTS IN METHOTREXATERESISTANCE:
REMARK 900 COMPARISON OF WILD- TYPE AND LEU22ARG VARIANTMOUSE AND HUMAN
REMARK 900 DIHYDROFOLATE REDUCTASE TERNARY CRYSTALCOMPLEXES WITH METHOTREXATE
REMARK 900 AND NADPH
REMARK 900 RELATED ID: 1U72 RELATED DB: PDB
REMARK 900 UNDERSTANDING THE ROLE OF LEU22 VARIANTS IN METHOTREXATERESISTANCE:
REMARK 900 COMPARISON OF WILD- TYPE AND LEU22ARG VARIANTMOUSE AND HUMAN
REMARK 900 DIHYDRFOLATE REDUCTASE TERNARY CRYSTALCOMPLEXES WITH METHOTREXATE
REMARK 900 AND NADPH
REMARK 900 RELATED ID: 2C2T RELATED DB: PDB
REMARK 900 HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND 2,4-DIAMINO-
REMARK 900 5-((7,8- DICARBAUNDECABORAN-7-YL)METHYL)-6- METHYLPYRIMIDINE, A
REMARK 900 NOVEL BORON CONTANING, NONCLASSICAL ANTIFOLATE
REMARK 900 RELATED ID: 2DHF RELATED DB: PDB
REMARK 900 DIHYDROFOLATE REDUCTASE (DHFR) COMPLEX WITH 5 -DEAZAFOLATE
DBREF 2C2S A 1 186 UNP P00374 DYR_HUMAN 1 186
DBREF 2C2S B 1 186 UNP P00374 DYR_HUMAN 1 186
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
SEQRES 1 B 186 VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN ASN
SEQRES 2 B 186 MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO PRO
SEQRES 3 B 186 LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR THR
SEQRES 4 B 186 THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE MET
SEQRES 5 B 186 GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN ARG
SEQRES 6 B 186 PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG GLU
SEQRES 7 B 186 LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER ARG
SEQRES 8 B 186 SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO GLU
SEQRES 9 B 186 LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY GLY
SEQRES 10 B 186 SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY HIS
SEQRES 11 B 186 LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE GLU
SEQRES 12 B 186 SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS TYR
SEQRES 13 B 186 LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP VAL
SEQRES 14 B 186 GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL TYR
SEQRES 15 B 186 GLU LYS ASN ASP
HET NDP A1187 48
HET 34B A1188 22
HET NDP B1187 48
HET 34B B1188 22
HET GOL B1189 6
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM 34B 2,4-DIAMINO-5-(1-O-CARBORANYLMETHYL)-6-METHYLPYRIMIDINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NDP 2(C21 H30 N7 O17 P3)
FORMUL 4 34B 2(C8 H20 B10 N4)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *556(H2 O)
HELIX 1 1 LEU A 27 THR A 40 1 14
HELIX 2 2 LYS A 54 ILE A 60 1 7
HELIX 3 3 PRO A 61 ARG A 65 5 5
HELIX 4 4 SER A 92 THR A 100 1 9
HELIX 5 5 GLY A 117 HIS A 127 1 11
HELIX 6 6 LEU B 27 THR B 40 1 14
HELIX 7 7 LYS B 54 ILE B 60 1 7
HELIX 8 8 PRO B 61 ARG B 65 5 5
HELIX 9 9 SER B 92 THR B 100 1 9
HELIX 10 10 GLY B 117 ASN B 126 1 10
SHEET 1 AA 8 PHE A 88 SER A 90 0
SHEET 2 AA 8 ILE A 71 LEU A 75 1 O VAL A 74 N SER A 90
SHEET 3 AA 8 GLN A 47 GLY A 53 1 O ASN A 48 N ILE A 71
SHEET 4 AA 8 VAL A 109 ILE A 114 1 N ASP A 110 O GLN A 47
SHEET 5 AA 8 SER A 3 SER A 11 1 O ASN A 5 N ILE A 114
SHEET 6 AA 8 HIS A 130 ILE A 138 1 O HIS A 130 N LEU A 4
SHEET 7 AA 8 ILE A 175 LYS A 184 -1 O LYS A 178 N ARG A 137
SHEET 8 AA 8 LYS A 157 LEU A 158 -1 O LYS A 157 N GLU A 183
SHEET 1 AB 8 PHE A 88 SER A 90 0
SHEET 2 AB 8 ILE A 71 LEU A 75 1 O VAL A 74 N SER A 90
SHEET 3 AB 8 GLN A 47 GLY A 53 1 O ASN A 48 N ILE A 71
SHEET 4 AB 8 VAL A 109 ILE A 114 1 N ASP A 110 O GLN A 47
SHEET 5 AB 8 SER A 3 SER A 11 1 O ASN A 5 N ILE A 114
SHEET 6 AB 8 HIS A 130 ILE A 138 1 O HIS A 130 N LEU A 4
SHEET 7 AB 8 ILE A 175 LYS A 184 -1 O LYS A 178 N ARG A 137
SHEET 8 AB 8 GLN A 170 GLU A 172 -1 O GLN A 170 N TYR A 177
SHEET 1 AC 2 GLY A 15 GLY A 17 0
SHEET 2 AC 2 THR A 146 PHE A 147 -1 O THR A 146 N ILE A 16
SHEET 1 BA 8 PHE B 88 SER B 90 0
SHEET 2 BA 8 ARG B 70 LEU B 75 1 O VAL B 74 N SER B 90
SHEET 3 BA 8 GLN B 47 GLY B 53 1 O ASN B 48 N ILE B 71
SHEET 4 BA 8 VAL B 109 ILE B 114 1 N ASP B 110 O GLN B 47
SHEET 5 BA 8 SER B 3 VAL B 10 1 O ASN B 5 N ILE B 114
SHEET 6 BA 8 HIS B 130 ILE B 138 1 O HIS B 130 N LEU B 4
SHEET 7 BA 8 ILE B 175 LYS B 184 -1 O LYS B 178 N ARG B 137
SHEET 8 BA 8 LYS B 157 LEU B 158 -1 O LYS B 157 N GLU B 183
SHEET 1 BB 8 PHE B 88 SER B 90 0
SHEET 2 BB 8 ARG B 70 LEU B 75 1 O VAL B 74 N SER B 90
SHEET 3 BB 8 GLN B 47 GLY B 53 1 O ASN B 48 N ILE B 71
SHEET 4 BB 8 VAL B 109 ILE B 114 1 N ASP B 110 O GLN B 47
SHEET 5 BB 8 SER B 3 VAL B 10 1 O ASN B 5 N ILE B 114
SHEET 6 BB 8 HIS B 130 ILE B 138 1 O HIS B 130 N LEU B 4
SHEET 7 BB 8 ILE B 175 LYS B 184 -1 O LYS B 178 N ARG B 137
SHEET 8 BB 8 GLN B 170 GLU B 172 -1 O GLN B 170 N TYR B 177
SHEET 1 BC 2 GLY B 15 GLY B 17 0
SHEET 2 BC 2 THR B 146 PHE B 147 -1 O THR B 146 N ILE B 16
CISPEP 1 ARG A 65 PRO A 66 0 -7.17
CISPEP 2 GLY A 116 GLY A 117 0 0.63
CISPEP 3 ARG B 65 PRO B 66 0 -6.89
CISPEP 4 GLY B 116 GLY B 117 0 3.06
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 LEU A 75
SITE 4 AC1 31 SER A 76 ARG A 77 GLU A 78 ARG A 91
SITE 5 AC1 31 VAL A 115 GLY A 116 GLY A 117 SER A 118
SITE 6 AC1 31 SER A 119 VAL A 120 TYR A 121 GLU A 123
SITE 7 AC1 31 THR A 146 34B A1188 HOH A2179 HOH A2199
SITE 8 AC1 31 HOH A2266 HOH A2267 HOH A2268
SITE 1 AC2 9 ILE A 7 VAL A 8 ALA A 9 LEU A 22
SITE 2 AC2 9 GLU A 30 PHE A 34 VAL A 115 TYR A 121
SITE 3 AC2 9 NDP A1187
SITE 1 AC3 31 VAL B 8 ALA B 9 ILE B 16 GLY B 17
SITE 2 AC3 31 GLY B 20 ASP B 21 GLY B 53 LYS B 54
SITE 3 AC3 31 LYS B 55 THR B 56 LEU B 75 SER B 76
SITE 4 AC3 31 ARG B 77 GLU B 78 ARG B 91 VAL B 115
SITE 5 AC3 31 GLY B 117 SER B 118 SER B 119 VAL B 120
SITE 6 AC3 31 TYR B 121 GLU B 123 THR B 146 34B B1188
SITE 7 AC3 31 HOH B2195 HOH B2219 HOH B2220 HOH B2283
SITE 8 AC3 31 HOH B2284 HOH B2285 HOH B2286
SITE 1 AC4 8 ILE B 7 VAL B 8 ALA B 9 GLU B 30
SITE 2 AC4 8 PHE B 34 VAL B 115 TYR B 121 NDP B1187
SITE 1 AC5 7 LEU B 166 ASP B 168 VAL B 169 HOH B2251
SITE 2 AC5 7 HOH B2258 HOH B2287 HOH B2288
CRYST1 87.671 93.864 95.782 90.00 90.00 90.00 C 2 2 21 16
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 0.011406 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010654 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010440 0.00000
MTRIX1 1 -0.064193 0.996943 -0.044550 -2.42570 1
MTRIX2 1 -0.995562 -0.067055 -0.066028 47.20213 1
MTRIX3 1 -0.068813 0.040114 0.996823 22.86397 1
(ATOM LINES ARE NOT SHOWN.)
END
