HEADER TRANSFERASE 02-JAN-03 1NJS
TITLE HUMAN GAR TFASE IN COMPLEX WITH HYDROLYZED FORM OF 10-TRIFLUOROACETYL-
TITLE 2 5,10-DIDEAZA-ACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GAR TFASE, GART, GAR TRANSFORMYLASE, 5'-
COMPND 5 PHOSPHORIBOSYLGLYCINAMIDE TRANSFORMYLASE;
COMPND 6 EC: 2.1.2.2;
COMPND 7 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: GART;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-COFACTOR ANALOGUE COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHANG,J.DESHARNAIS,T.H.MARSILJE,C.LI,M.P.HEDRICK,L.T.GOOLJARSINGH,
AUTHOR 2 A.TAVASSOLI,S.J.BENKOVIC,A.J.OLSON,D.L.BOGER,I.A.WILSON
REVDAT 3 16-AUG-23 1NJS 1 REMARK SEQADV HETSYN
REVDAT 2 24-FEB-09 1NJS 1 VERSN
REVDAT 1 10-JUN-03 1NJS 0
JRNL AUTH Y.ZHANG,J.DESHARNAIS,T.H.MARSILJE,C.LI,M.P.HEDRICK,
JRNL AUTH 2 L.T.GOOLJARSINGH,A.TAVASSOLI,S.J.BENKOVIC,A.J.OLSON,
JRNL AUTH 3 D.L.BOGER,I.A.WILSON
JRNL TITL RATIONAL DESIGN, SYNTHESIS, EVALUATION, AND CRYSTAL
JRNL TITL 2 STRUCTURE OF A POTENT INHIBITOR OF HUMAN GAR TFASE:
JRNL TITL 3 10-(TRIFLUOROACETYL)-5,10-DIDEAZAACYCLIC-5,6,7,
JRNL TITL 4 8-TETRAHYDROFOLIC ACID
JRNL REF BIOCHEMISTRY V. 42 6043 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12755606
JRNL DOI 10.1021/BI034219C
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 54999
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) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2913
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) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3599
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 196
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3014
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 91
REMARK 3 SOLVENT ATOMS : 251
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.17000
REMARK 3 B22 (A**2) : -0.17000
REMARK 3 B33 (A**2) : 0.26000
REMARK 3 B12 (A**2) : -0.09000
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): 0.132
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.125
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.765
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3152 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4286 ; 1.369 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 398 ; 5.978 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 524 ; 0.135 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2294 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1435 ; 0.206 ; 0.200
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): 254 ; 0.126 ; 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): 32 ; 0.183 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.068 ; 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): 1992 ; 0.614 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3216 ; 1.148 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1160 ; 2.146 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1070 ; 3.565 ; 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 : 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 200
REMARK 3 ORIGIN FOR THE GROUP (A): 73.6419 17.9835 22.9917
REMARK 3 T TENSOR
REMARK 3 T11: 0.0441 T22: 0.0133
REMARK 3 T33: 0.0452 T12: -0.0157
REMARK 3 T13: 0.0201 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.6259 L22: 1.7476
REMARK 3 L33: 1.2617 L12: -0.9803
REMARK 3 L13: 0.1061 L23: 0.1421
REMARK 3 S TENSOR
REMARK 3 S11: -0.0076 S12: 0.0399 S13: 0.0267
REMARK 3 S21: -0.1413 S22: 0.0124 S23: -0.2800
REMARK 3 S31: 0.0716 S32: 0.1541 S33: -0.0048
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 200
REMARK 3 ORIGIN FOR THE GROUP (A): 43.3607 41.7712 24.6335
REMARK 3 T TENSOR
REMARK 3 T11: 0.1003 T22: 0.0753
REMARK 3 T33: 0.0366 T12: 0.0348
REMARK 3 T13: -0.0144 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 2.8273 L22: 1.4325
REMARK 3 L33: 1.1178 L12: -1.1998
REMARK 3 L13: -0.2546 L23: 0.1093
REMARK 3 S TENSOR
REMARK 3 S11: -0.0602 S12: -0.2844 S13: 0.2196
REMARK 3 S21: 0.1414 S22: 0.0931 S23: 0.0313
REMARK 3 S31: -0.2453 S32: -0.1538 S33: -0.0329
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: NULL
REMARK 4
REMARK 4 1NJS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000017931.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57912
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 41.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 3.880
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.91
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.60100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.020
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: PDB CODE 1MEJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4K, 0.2 AMMONIUM SULFATE, 50MM
REMARK 280 HEPES 6.7-7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 282K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 31.47300
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 62.94600
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 62.94600
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 31.47300
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 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 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 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 LYS A 201
REMARK 465 GLU A 202
REMARK 465 GLU A 203
REMARK 465 HIS A 204
REMARK 465 HIS A 205
REMARK 465 HIS A 206
REMARK 465 HIS A 207
REMARK 465 HIS A 208
REMARK 465 HIS A 209
REMARK 465 LYS B 201
REMARK 465 GLU B 202
REMARK 465 GLU B 203
REMARK 465 HIS B 204
REMARK 465 HIS B 205
REMARK 465 HIS B 206
REMARK 465 HIS B 207
REMARK 465 HIS B 208
REMARK 465 HIS B 209
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 NZ LYS A 116 O HOH A 541 2.07
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 119 50.70 -115.63
REMARK 500 THR A 132 -150.22 -127.82
REMARK 500 ILE A 149 -60.62 -95.70
REMARK 500 ASN A 194 9.52 -61.78
REMARK 500 ASN B 13 -6.65 73.27
REMARK 500 THR B 132 -150.15 -123.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE LIGAND HAS A TRIFLUOROACETYL GROUP WHEN SYNTHESIZED AND
REMARK 600 IS NAMED 10-TRIFLUOROACETYL-5,10-DIDEAZA-ACYCLIC-5,6,7,8-
REMARK 600 TETRAHYDROFOLIC ACID. WHEN THE COMPOUND INTERACTS WITH
REMARK 600 PROTEIN HUMAN GAR TFASE, THE KETONE GROUP IS HYDROLYZED
REMARK 600 TO TWO HYDROXYL GROUPS ("GEM-DIOL"). THE HYDROLYZED FORM
REMARK 600 WAS THE BINDING FORM IN THE STRUCTURE. THE HYDROLYZED
REMARK 600 COMPOUND IS ONLY STABLE WHEN BOUND TO ENZYME.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KEU A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KEU B 610
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MEJ RELATED DB: PDB
REMARK 900 APO HUMAN GAR TFASE AT HIGH PH
REMARK 900 RELATED ID: 1MEN RELATED DB: PDB
REMARK 900 HUMAN GAR TFASE IN COMPLEX WITH SUBSTRATE
REMARK 900 RELATED ID: 1MEO RELATED DB: PDB
REMARK 900 APO HUMAN GAR TFASE AT LOW PH
DBREF 1NJS A 1 203 UNP P22102 PUR2_HUMAN 808 1010
DBREF 1NJS B 1 203 UNP P22102 PUR2_HUMAN 808 1010
SEQADV 1NJS HIS A 204 UNP P22102 EXPRESSION TAG
SEQADV 1NJS HIS A 205 UNP P22102 EXPRESSION TAG
SEQADV 1NJS HIS A 206 UNP P22102 EXPRESSION TAG
SEQADV 1NJS HIS A 207 UNP P22102 EXPRESSION TAG
SEQADV 1NJS HIS A 208 UNP P22102 EXPRESSION TAG
SEQADV 1NJS HIS A 209 UNP P22102 EXPRESSION TAG
SEQADV 1NJS HIS B 204 UNP P22102 EXPRESSION TAG
SEQADV 1NJS HIS B 205 UNP P22102 EXPRESSION TAG
SEQADV 1NJS HIS B 206 UNP P22102 EXPRESSION TAG
SEQADV 1NJS HIS B 207 UNP P22102 EXPRESSION TAG
SEQADV 1NJS HIS B 208 UNP P22102 EXPRESSION TAG
SEQADV 1NJS HIS B 209 UNP P22102 EXPRESSION TAG
SEQRES 1 A 209 ALA ARG VAL ALA VAL LEU ILE SER GLY THR GLY SER ASN
SEQRES 2 A 209 LEU GLN ALA LEU ILE ASP SER THR ARG GLU PRO ASN SER
SEQRES 3 A 209 SER ALA GLN ILE ASP ILE VAL ILE SER ASN LYS ALA ALA
SEQRES 4 A 209 VAL ALA GLY LEU ASP LYS ALA GLU ARG ALA GLY ILE PRO
SEQRES 5 A 209 THR ARG VAL ILE ASN HIS LYS LEU TYR LYS ASN ARG VAL
SEQRES 6 A 209 GLU PHE ASP SER ALA ILE ASP LEU VAL LEU GLU GLU PHE
SEQRES 7 A 209 SER ILE ASP ILE VAL CYS LEU ALA GLY PHE MET ARG ILE
SEQRES 8 A 209 LEU SER GLY PRO PHE VAL GLN LYS TRP ASN GLY LYS MET
SEQRES 9 A 209 LEU ASN ILE HIS PRO SER LEU LEU PRO SER PHE LYS GLY
SEQRES 10 A 209 SER ASN ALA HIS GLU GLN ALA LEU GLU THR GLY VAL THR
SEQRES 11 A 209 VAL THR GLY CYS THR VAL HIS PHE VAL ALA GLU ASP VAL
SEQRES 12 A 209 ASP ALA GLY GLN ILE ILE LEU GLN GLU ALA VAL PRO VAL
SEQRES 13 A 209 LYS ARG GLY ASP THR VAL ALA THR LEU SER GLU ARG VAL
SEQRES 14 A 209 LYS LEU ALA GLU HIS LYS ILE PHE PRO ALA ALA LEU GLN
SEQRES 15 A 209 LEU VAL ALA SER GLY THR VAL GLN LEU GLY GLU ASN GLY
SEQRES 16 A 209 LYS ILE CYS TRP VAL LYS GLU GLU HIS HIS HIS HIS HIS
SEQRES 17 A 209 HIS
SEQRES 1 B 209 ALA ARG VAL ALA VAL LEU ILE SER GLY THR GLY SER ASN
SEQRES 2 B 209 LEU GLN ALA LEU ILE ASP SER THR ARG GLU PRO ASN SER
SEQRES 3 B 209 SER ALA GLN ILE ASP ILE VAL ILE SER ASN LYS ALA ALA
SEQRES 4 B 209 VAL ALA GLY LEU ASP LYS ALA GLU ARG ALA GLY ILE PRO
SEQRES 5 B 209 THR ARG VAL ILE ASN HIS LYS LEU TYR LYS ASN ARG VAL
SEQRES 6 B 209 GLU PHE ASP SER ALA ILE ASP LEU VAL LEU GLU GLU PHE
SEQRES 7 B 209 SER ILE ASP ILE VAL CYS LEU ALA GLY PHE MET ARG ILE
SEQRES 8 B 209 LEU SER GLY PRO PHE VAL GLN LYS TRP ASN GLY LYS MET
SEQRES 9 B 209 LEU ASN ILE HIS PRO SER LEU LEU PRO SER PHE LYS GLY
SEQRES 10 B 209 SER ASN ALA HIS GLU GLN ALA LEU GLU THR GLY VAL THR
SEQRES 11 B 209 VAL THR GLY CYS THR VAL HIS PHE VAL ALA GLU ASP VAL
SEQRES 12 B 209 ASP ALA GLY GLN ILE ILE LEU GLN GLU ALA VAL PRO VAL
SEQRES 13 B 209 LYS ARG GLY ASP THR VAL ALA THR LEU SER GLU ARG VAL
SEQRES 14 B 209 LYS LEU ALA GLU HIS LYS ILE PHE PRO ALA ALA LEU GLN
SEQRES 15 B 209 LEU VAL ALA SER GLY THR VAL GLN LEU GLY GLU ASN GLY
SEQRES 16 B 209 LYS ILE CYS TRP VAL LYS GLU GLU HIS HIS HIS HIS HIS
SEQRES 17 B 209 HIS
HET PO4 A 521 5
HET PO4 A 522 5
HET KEU A 510 38
HET PO4 B 621 5
HET KEU B 610 38
HETNAM PO4 PHOSPHATE ION
HETNAM KEU N-{4-[(1R)-4-[(2R,4R,5S)-2,4-DIAMINO-6-
HETNAM 2 KEU OXOHEXAHYDROPYRIMIDIN-5-YL]-1-(2,2,2-TRIFLUORO-1,1-
HETNAM 3 KEU DIHYDROXYETHYL)BUTYL]BENZOYL}-D-GLUTAMIC ACID
HETSYN KEU 10-CF3C(OH)2-DDACTHF; HYDROLYZED FORM OF 10-
HETSYN 2 KEU TRIFLUOROACETYL-5,10-DIDEAZA-ACYCLIC-5,6,7,8-
HETSYN 3 KEU TETRAHYDROFOLIC ACID
FORMUL 3 PO4 3(O4 P 3-)
FORMUL 5 KEU 2(C22 H30 F3 N5 O8)
FORMUL 8 HOH *251(H2 O)
HELIX 1 1 GLY A 11 ARG A 22 1 12
HELIX 2 2 VAL A 40 ALA A 49 1 10
HELIX 3 3 ASN A 57 TYR A 61 5 5
HELIX 4 4 ASN A 63 PHE A 78 1 16
HELIX 5 5 SER A 93 TRP A 100 1 8
HELIX 6 6 ASN A 119 GLY A 128 1 10
HELIX 7 7 THR A 161 SER A 186 1 26
HELIX 8 8 ASN B 13 ARG B 22 1 10
HELIX 9 9 VAL B 40 ALA B 49 1 10
HELIX 10 10 ASN B 57 TYR B 61 5 5
HELIX 11 11 ASN B 63 PHE B 78 1 16
HELIX 12 12 SER B 93 TRP B 100 1 8
HELIX 13 13 ASN B 119 GLY B 128 1 10
HELIX 14 14 THR B 161 SER B 186 1 26
SHEET 1 A 7 THR A 53 VAL A 55 0
SHEET 2 A 7 GLN A 29 SER A 35 1 N SER A 35 O ARG A 54
SHEET 3 A 7 ARG A 2 ILE A 7 1 N VAL A 3 O GLN A 29
SHEET 4 A 7 ILE A 82 LEU A 85 1 O CYS A 84 N ALA A 4
SHEET 5 A 7 MET A 104 HIS A 108 1 O LEU A 105 N LEU A 85
SHEET 6 A 7 VAL A 131 PHE A 138 -1 O THR A 135 N HIS A 108
SHEET 7 A 7 ILE A 148 PRO A 155 -1 O ILE A 149 N VAL A 136
SHEET 1 B 2 VAL A 189 LEU A 191 0
SHEET 2 B 2 ILE A 197 TRP A 199 -1 O CYS A 198 N GLN A 190
SHEET 1 C 7 THR B 53 VAL B 55 0
SHEET 2 C 7 GLN B 29 SER B 35 1 N SER B 35 O ARG B 54
SHEET 3 C 7 ARG B 2 ILE B 7 1 N VAL B 3 O GLN B 29
SHEET 4 C 7 ILE B 82 LEU B 85 1 O CYS B 84 N ALA B 4
SHEET 5 C 7 MET B 104 HIS B 108 1 O LEU B 105 N LEU B 85
SHEET 6 C 7 VAL B 131 PHE B 138 -1 O THR B 135 N HIS B 108
SHEET 7 C 7 ILE B 148 PRO B 155 -1 O VAL B 154 N THR B 132
SHEET 1 D 2 VAL B 189 LEU B 191 0
SHEET 2 D 2 ILE B 197 TRP B 199 -1 O CYS B 198 N GLN B 190
CISPEP 1 LEU A 112 PRO A 113 0 10.59
CISPEP 2 LEU B 112 PRO B 113 0 10.53
SITE 1 AC1 8 THR A 10 GLY A 11 SER A 12 ASN A 13
SITE 2 AC1 8 LYS A 170 HOH A 527 HOH A 535 HOH A 577
SITE 1 AC2 4 LYS A 157 ARG A 168 HOH A 560 HOH A 611
SITE 1 AC3 11 GLY B 11 SER B 12 ASN B 13 LEU B 14
SITE 2 AC3 11 GLN B 15 ALA B 16 LYS B 45 HIS B 174
SITE 3 AC3 11 HOH B 652 HOH B 656 HOH B 705
SITE 1 AC4 24 ARG A 64 LEU A 85 MET A 89 ARG A 90
SITE 2 AC4 24 ILE A 91 LEU A 92 VAL A 97 ASN A 106
SITE 3 AC4 24 HIS A 108 PRO A 109 GLY A 117 SER A 118
SITE 4 AC4 24 VAL A 139 ALA A 140 GLU A 141 VAL A 143
SITE 5 AC4 24 ASP A 144 HOH A 528 HOH A 529 HOH A 533
SITE 6 AC4 24 HOH A 543 HOH A 563 HOH A 565 HOH B 661
SITE 1 AC5 17 ARG B 64 MET B 89 ARG B 90 ILE B 91
SITE 2 AC5 17 LEU B 92 VAL B 97 ASN B 106 HIS B 108
SITE 3 AC5 17 PRO B 109 GLY B 117 VAL B 139 ALA B 140
SITE 4 AC5 17 GLU B 141 VAL B 143 ASP B 144 HOH B 631
SITE 5 AC5 17 HOH B 684
CRYST1 126.235 126.235 94.419 90.00 90.00 120.00 P 31 2 1 12
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 0.007922 0.004574 0.000000 0.00000
SCALE2 0.000000 0.009147 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010591 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
