HEADER TRANSFERASE 03-NOV-03 1RC1
TITLE HUMAN GAR TFASE COMPLEX STRUCTURE WITH POLYGLUTAMATED 10-
TITLE 2 (TRIFLUOROACETYL)-5,10-DIDEAZAACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: (RESIDUES 808-1010);
COMPND 5 SYNONYM: GART; GAR TRANSFORMYLASE; 5'-PHOSPHORIBOSYLGLYCINAMIDE
COMPND 6 TRANSFORMYLASE;
COMPND 7 EC: 2.1.2.2;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: PART OF TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN
COMPND 10 ADENOSINE-3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PURN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22A
KEYWDS PROTEIN-COFACTOR ANALOGUE COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHANG,J.DESHARNAIS,D.L.BOGER,I.A.WILSON
REVDAT 3 23-AUG-23 1RC1 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1RC1 1 VERSN
REVDAT 1 14-JUN-05 1RC1 0
JRNL AUTH Y.ZHANG,J.DESHARNAIS,D.L.BOGER,I.A.WILSON
JRNL TITL HUMAN GAR TFASE COMPLEX STRUCTURE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 39369
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) : 0.234
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1974
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2369
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.3310
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 : 86
REMARK 3 SOLVENT ATOMS : 130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.05000
REMARK 3 B12 (A**2) : 0.02000
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): 0.197
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.175
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.639
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3148 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4280 ; 1.370 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 398 ; 6.292 ; 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 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2294 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1314 ; 0.201 ; 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): 179 ; 0.125 ; 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): 41 ; 0.187 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.118 ; 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 ; 0.515 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3216 ; 0.996 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1156 ; 1.800 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1064 ; 3.123 ; 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): -10.6602 54.4514 6.9022
REMARK 3 T TENSOR
REMARK 3 T11: 0.0096 T22: 0.0846
REMARK 3 T33: 0.0738 T12: 0.0248
REMARK 3 T13: 0.0042 T23: -0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 1.2032 L22: 3.5066
REMARK 3 L33: 1.7378 L12: 0.5664
REMARK 3 L13: 0.3540 L23: 0.0488
REMARK 3 S TENSOR
REMARK 3 S11: -0.0180 S12: 0.1830 S13: -0.2855
REMARK 3 S21: -0.0198 S22: 0.0549 S23: -0.2456
REMARK 3 S31: 0.1759 S32: 0.0564 S33: -0.0369
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): -14.0504 58.4321 40.1008
REMARK 3 T TENSOR
REMARK 3 T11: 0.1547 T22: 0.1596
REMARK 3 T33: 0.1005 T12: -0.0113
REMARK 3 T13: -0.0262 T23: -0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 3.5934 L22: 2.3225
REMARK 3 L33: 1.3120 L12: 1.7644
REMARK 3 L13: -0.4234 L23: -0.4520
REMARK 3 S TENSOR
REMARK 3 S11: 0.1471 S12: -0.3030 S13: 0.1304
REMARK 3 S21: 0.2716 S22: -0.0947 S23: 0.3471
REMARK 3 S31: -0.0437 S32: -0.3583 S33: -0.0524
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 1RC1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020642.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-FEB-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.
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) : 0.9840
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 9
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41237
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 47.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.080
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.67000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: 1NJS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, CALCIUM CLORIDE, IMIDAZOLE MALATE
REMARK 280 BUFFER, PH 6., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 31.22667
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 62.45333
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 62.45333
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 31.22667
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: 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 B 81 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 142 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 25 46.54 -102.34
REMARK 500 PRO A 109 46.81 -81.33
REMARK 500 ASN A 119 52.54 -112.88
REMARK 500 THR A 132 -154.74 -128.34
REMARK 500 ASN B 13 -14.31 86.29
REMARK 500 PRO B 109 48.71 -82.63
REMARK 500 THR B 132 -150.10 -127.42
REMARK 500 ASN B 194 -9.99 -58.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 187 THR A 188 -138.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 KT3 A 510
REMARK 610 KT3 B 610
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 B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KT3 A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KT3 B 610
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NJS RELATED DB: PDB
REMARK 900 HUMAN GAR TFASE COMPLEX STRUCTURE WITH 10-(TRIFLUOROACETYL)-5,10-
REMARK 900 DIDEAZAACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID AT PHYSIOLOGICAL PH
REMARK 900 RELATED ID: 1MEJ RELATED DB: PDB
REMARK 900 APO HUMAN GAR TFASE STRUCTURE AT PH 8.5
REMARK 900 RELATED ID: 1MEO RELATED DB: PDB
REMARK 900 APO HUMAN GAR TFASE STRUCTURE AT PH 4.2
REMARK 900 RELATED ID: 1RBM RELATED DB: PDB
REMARK 900 RELATED ID: 1RBQ RELATED DB: PDB
REMARK 900 RELATED ID: 1RBY RELATED DB: PDB
REMARK 900 RELATED ID: 1RBZ RELATED DB: PDB
REMARK 900 RELATED ID: 1RC0 RELATED DB: PDB
DBREF 1RC1 A 1 203 UNP P22102 PUR2_HUMAN 808 1010
DBREF 1RC1 B 1 203 UNP P22102 PUR2_HUMAN 808 1010
SEQADV 1RC1 HIS A 204 UNP P22102 EXPRESSION TAG
SEQADV 1RC1 HIS A 205 UNP P22102 EXPRESSION TAG
SEQADV 1RC1 HIS A 206 UNP P22102 EXPRESSION TAG
SEQADV 1RC1 HIS A 207 UNP P22102 EXPRESSION TAG
SEQADV 1RC1 HIS A 208 UNP P22102 EXPRESSION TAG
SEQADV 1RC1 HIS A 209 UNP P22102 EXPRESSION TAG
SEQADV 1RC1 HIS B 204 UNP P22102 EXPRESSION TAG
SEQADV 1RC1 HIS B 205 UNP P22102 EXPRESSION TAG
SEQADV 1RC1 HIS B 206 UNP P22102 EXPRESSION TAG
SEQADV 1RC1 HIS B 207 UNP P22102 EXPRESSION TAG
SEQADV 1RC1 HIS B 208 UNP P22102 EXPRESSION TAG
SEQADV 1RC1 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 KT3 A 510 38
HET PO4 B 621 5
HET KT3 B 610 38
HETNAM PO4 PHOSPHATE ION
HETNAM KT3 N-{4-4-(2,4-DIAMINO-6-OXO-1,6-DIHYDRO-PYRIMIDIN-5-YL)-
HETNAM 2 KT3 1-(2,2,2-TRIFLUORO-1,1-DIHYDROXY-ETHYL)-BUT-2-YL-
HETNAM 3 KT3 BENZOYL}-GAMMA-GLUTAMYL-GAMMA-GLUTAMYL-GLUTAMIC ACID
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 4 KT3 2(C32 H40 F3 N7 O14)
FORMUL 7 HOH *130(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 VAL A 154 N THR A 132
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 ILE B 7 O ILE B 34
SHEET 4 C 7 ILE B 82 LEU B 85 1 O CYS B 84 N LEU B 6
SHEET 5 C 7 MET B 104 HIS B 108 1 O LEU B 105 N VAL B 83
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 5.87
CISPEP 2 LEU B 112 PRO B 113 0 7.29
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 524 HOH A 531 HOH A 532
SITE 1 AC2 8 GLY B 11 SER B 12 ASN B 13 LEU B 14
SITE 2 AC2 8 GLN B 15 ALA B 16 LYS B 45 HIS B 174
SITE 1 AC3 20 ARG A 64 MET A 89 ARG A 90 ILE A 91
SITE 2 AC3 20 LEU A 92 VAL A 97 ASN A 106 HIS A 108
SITE 3 AC3 20 PRO A 109 GLY A 117 SER A 118 VAL A 139
SITE 4 AC3 20 ALA A 140 GLU A 141 VAL A 143 ASP A 144
SITE 5 AC3 20 HOH A 525 HOH A 559 HOH A 569 HOH A 594
SITE 1 AC4 16 ARG B 64 LEU B 85 MET B 89 ARG B 90
SITE 2 AC4 16 ILE B 91 LEU B 92 ASN B 106 HIS B 108
SITE 3 AC4 16 PRO B 109 GLY B 117 VAL B 139 ALA B 140
SITE 4 AC4 16 GLU B 141 VAL B 143 ASP B 144 HOH B 636
CRYST1 126.664 126.664 93.680 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 0.007895 0.004558 0.000000 0.00000
SCALE2 0.000000 0.009116 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010675 0.00000
(ATOM LINES ARE NOT SHOWN.)
END