HEADER TRANSFERASE/TRANSFERASE INHIBITOR 22-MAY-15 4ZYY
TITLE HUMAN GAR TRANSFORMYLASE IN COMPLEX WITH GAR AND (S)-2-({5-[4-(2-
TITLE 2 AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]-PYRIMIDIN-6-YL)
TITLE 3 BUTYL]THIOPHENE-3-CARBONYL}AMINO)PENTANEDIOIC ACID (AGF118)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GAR TRANSFORMYLASE DOMAIN;
COMPND 5 EC: 2.1.2.2;
COMPND 6 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, PGFT, PRGS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS GAR TRANSFORMYLASE, ANTIFOLATE, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.DEIS,C.E.DANN III
REVDAT 5 27-SEP-23 4ZYY 1 REMARK
REVDAT 4 04-DEC-19 4ZYY 1 REMARK
REVDAT 3 20-SEP-17 4ZYY 1 REMARK
REVDAT 2 22-FEB-17 4ZYY 1 JRNL
REVDAT 1 20-APR-16 4ZYY 0
JRNL AUTH S.M.DEIS,A.DOSHI,Z.HOU,L.H.MATHERLY,A.GANGJEE,C.E.DANN
JRNL TITL STRUCTURAL AND ENZYMATIC ANALYSIS OF TUMOR-TARGETED
JRNL TITL 2 ANTIFOLATES THAT INHIBIT GLYCINAMIDE RIBONUCLEOTIDE
JRNL TITL 3 FORMYLTRANSFERASE.
JRNL REF BIOCHEMISTRY V. 55 4574 2016
JRNL REFN ISSN 1520-4995
JRNL PMID 27439469
JRNL DOI 10.1021/ACS.BIOCHEM.6B00412
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 27832
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.140
REMARK 3 FREE R VALUE TEST SET COUNT : 1988
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.8417 - 4.4489 0.97 1983 155 0.1396 0.1659
REMARK 3 2 4.4489 - 3.5319 1.00 1953 153 0.1463 0.1618
REMARK 3 3 3.5319 - 3.0856 1.00 1932 147 0.1793 0.2322
REMARK 3 4 3.0856 - 2.8036 1.00 1908 143 0.1882 0.2146
REMARK 3 5 2.8036 - 2.6027 1.00 1904 142 0.1881 0.2032
REMARK 3 6 2.6027 - 2.4493 1.00 1903 146 0.1766 0.2020
REMARK 3 7 2.4493 - 2.3266 1.00 1886 146 0.1674 0.1802
REMARK 3 8 2.3266 - 2.2254 1.00 1893 147 0.1594 0.2049
REMARK 3 9 2.2254 - 2.1397 1.00 1862 144 0.1626 0.1742
REMARK 3 10 2.1397 - 2.0659 1.00 1898 148 0.1679 0.1795
REMARK 3 11 2.0659 - 2.0013 1.00 1881 144 0.1842 0.2256
REMARK 3 12 2.0013 - 1.9441 1.00 1873 144 0.1888 0.2161
REMARK 3 13 1.9441 - 1.8929 0.93 1760 136 0.2144 0.2868
REMARK 3 14 1.8929 - 1.8467 0.65 1208 93 0.2247 0.2726
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.33
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 1707
REMARK 3 ANGLE : 1.056 2338
REMARK 3 CHIRALITY : 0.046 271
REMARK 3 PLANARITY : 0.005 307
REMARK 3 DIHEDRAL : 12.907 640
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 808 THROUGH 835 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.7847 -24.0651 24.6140
REMARK 3 T TENSOR
REMARK 3 T11: 0.1782 T22: 0.1695
REMARK 3 T33: 0.1603 T12: -0.0462
REMARK 3 T13: 0.0428 T23: 0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 0.8965 L22: 1.0523
REMARK 3 L33: 2.4977 L12: 0.0236
REMARK 3 L13: -0.4619 L23: 0.0870
REMARK 3 S TENSOR
REMARK 3 S11: 0.1006 S12: -0.1146 S13: 0.1397
REMARK 3 S21: 0.0380 S22: -0.0129 S23: -0.1185
REMARK 3 S31: -0.2774 S32: 0.2853 S33: -0.0725
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 836 THROUGH 855 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.4179 -15.5815 30.1046
REMARK 3 T TENSOR
REMARK 3 T11: 0.3226 T22: 0.3199
REMARK 3 T33: 0.3301 T12: -0.1883
REMARK 3 T13: 0.0291 T23: -0.0315
REMARK 3 L TENSOR
REMARK 3 L11: 2.2687 L22: 3.0852
REMARK 3 L33: 7.0216 L12: -0.4206
REMARK 3 L13: 0.3895 L23: 1.6811
REMARK 3 S TENSOR
REMARK 3 S11: 0.1907 S12: -0.4710 S13: 0.3873
REMARK 3 S21: 0.4157 S22: -0.1501 S23: -0.5539
REMARK 3 S31: -0.4134 S32: 0.4671 S33: -0.0318
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 856 THROUGH 884 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.8534 -4.9393 25.4436
REMARK 3 T TENSOR
REMARK 3 T11: 0.6347 T22: 0.2179
REMARK 3 T33: 0.5568 T12: -0.1360
REMARK 3 T13: 0.1968 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 1.1022 L22: 1.6374
REMARK 3 L33: 0.7555 L12: -0.4378
REMARK 3 L13: -0.0892 L23: -0.7914
REMARK 3 S TENSOR
REMARK 3 S11: 0.2252 S12: -0.1666 S13: 0.6441
REMARK 3 S21: 0.4148 S22: -0.0526 S23: -0.0561
REMARK 3 S31: -0.7564 S32: 0.0636 S33: -0.0482
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 885 THROUGH 954 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4987 -16.9537 28.0214
REMARK 3 T TENSOR
REMARK 3 T11: 0.3153 T22: 0.1344
REMARK 3 T33: 0.2364 T12: 0.0418
REMARK 3 T13: 0.0893 T23: 0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 0.8178 L22: 0.5572
REMARK 3 L33: 1.0555 L12: 0.4179
REMARK 3 L13: -0.5446 L23: -0.5284
REMARK 3 S TENSOR
REMARK 3 S11: 0.2173 S12: 0.1407 S13: 0.4281
REMARK 3 S21: -0.0084 S22: 0.0166 S23: 0.0306
REMARK 3 S31: -0.5179 S32: -0.1689 S33: -0.1637
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 955 THROUGH 992 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.4662 -29.1036 34.6167
REMARK 3 T TENSOR
REMARK 3 T11: 0.1247 T22: 0.0566
REMARK 3 T33: 0.0991 T12: -0.0010
REMARK 3 T13: 0.0207 T23: 0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 1.1411 L22: 0.6798
REMARK 3 L33: 3.4603 L12: -0.1564
REMARK 3 L13: -0.2252 L23: 0.4019
REMARK 3 S TENSOR
REMARK 3 S11: 0.0505 S12: 0.0252 S13: 0.1241
REMARK 3 S21: 0.0482 S22: 0.0136 S23: -0.0974
REMARK 3 S31: -0.1464 S32: -0.0374 S33: -0.0436
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 993 THROUGH 1007 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8234 -25.2976 12.8921
REMARK 3 T TENSOR
REMARK 3 T11: 0.2705 T22: 0.3839
REMARK 3 T33: 0.2256 T12: 0.0675
REMARK 3 T13: -0.0178 T23: 0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 1.6866 L22: 6.8154
REMARK 3 L33: 4.8691 L12: 1.1781
REMARK 3 L13: 0.2957 L23: 0.0198
REMARK 3 S TENSOR
REMARK 3 S11: 0.0016 S12: 0.9319 S13: 0.3923
REMARK 3 S21: -0.4809 S22: -0.2035 S23: 0.8602
REMARK 3 S31: -0.5649 S32: -0.7939 S33: 0.1319
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4ZYY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000210126.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0001
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK SI(111) SAGITALLY
REMARK 200 FOCUSED MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CMOS
REMARK 200 DETECTOR MANUFACTURER : RDI CMOS_8M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28587
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.48800
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: PHASER 2.5.6
REMARK 200 STARTING MODEL: 4X76
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18 % PEG4000, 2 % PEG400, 0.33 M NACL,
REMARK 280 PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.23533
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 33.61767
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 33.61767
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 67.23533
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 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 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 MET A 807
REMARK 465 LYS A 1008
REMARK 465 GLU A 1009
REMARK 465 GLU A 1010
REMARK 465 HIS A 1011
REMARK 465 HIS A 1012
REMARK 465 HIS A 1013
REMARK 465 HIS A 1014
REMARK 465 HIS A 1015
REMARK 465 HIS A 1016
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 LYS A 869 CG CD CE NZ
REMARK 470 GLU A1000 CG 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 PRO A 916 47.85 -86.28
REMARK 500 THR A 939 -151.65 -123.81
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 A1349 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A1350 DISTANCE = 6.67 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GAR A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3YC A 1102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EW2 RELATED DB: PDB
REMARK 900 4EW2 IS THE SAME PROTEIN COMPLEXED WITH 10S-METHYLTHIO-DDATHF
REMARK 900 RELATED ID: 4EW3 RELATED DB: PDB
REMARK 900 4EW3 IS THE SAME PROTEIN COMPLEXED WITH 10R-METHYLTHIO-DDATHF
REMARK 900 RELATED ID: 1RBM RELATED DB: PDB
REMARK 900 1RBM IS THE SAME PROTEIN COMPLEXED WITH POLYGLUTAMINATED 10-
REMARK 900 (TRIFLUOROACETYL)-5,10-DIDEAZAACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID
REMARK 900 RELATED ID: 1RBQ RELATED DB: PDB
REMARK 900 1RBQ IS THE SAME PROTEIN COMPLEXED WITH 10-(TRIFLUOROACETYL)-5,10-
REMARK 900 DIDEAZAACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID
REMARK 900 RELATED ID: 1RBY RELATED DB: PDB
REMARK 900 1RBY IS THE SAME PROTEIN COMPLEXED WITH 10-(TRIFLUOROACETYL)-5,10-
REMARK 900 DIDEAZAACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID AND BETA-GAR
REMARK 900 RELATED ID: 1RBZ RELATED DB: PDB
REMARK 900 1RBZ IS THE SAME PROTEIN COMPLEXED WITH POLYGLUTAMINATED 10-
REMARK 900 (TRIFLUOROACETYL)-5,10-DIDEAZAACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID
REMARK 900 RELATED ID: 1RC0 RELATED DB: PDB
REMARK 900 1RC0 IS THE SAME PROTEIN COMPLEXED WITH POLYGLUTAMINATED 10-
REMARK 900 (TRIFLUOROACETYL)-5,10-DIDEAZAACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID
REMARK 900 RELATED ID: 1RC1 RELATED DB: PDB
REMARK 900 1RC1 IS THE SAME PROTEIN COMPLEXED WITH POLYGLUTAMINATED 10-
REMARK 900 (TRIFLUOROACETYL)-5,10-DIDEAZAACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID
REMARK 900 RELATED ID: 1NJS RELATED DB: PDB
REMARK 900 1NJS IS THE SAME PROTEIN COMPLEXED WITH A HYDROLYZED FORM OF 10-
REMARK 900 (TRIFLUOROACETYL)-5,10-DIDEAZAACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID
REMARK 900 RELATED ID: 1MEN RELATED DB: PDB
REMARK 900 1MEN IS THE SAME PROTEIN COMPLEXED WITH BETA-GAR
REMARK 900 RELATED ID: 1MEJ RELATED DB: PDB
REMARK 900 1MEJ IS THE SAME PROTEIN IN APO FORM AT PH 8.5
REMARK 900 RELATED ID: 1MEO RELATED DB: PDB
REMARK 900 1MEO IS THE SAME PROTEIN IN APO FORM AT PH 4.2
REMARK 900 RELATED ID: 1ZLX RELATED DB: PDB
REMARK 900 1ZLX IS THE SAME PROTEIN IN APO FORM
REMARK 900 RELATED ID: 1ZLY RELATED DB: PDB
REMARK 900 1ZLY IS THE SAME PROTEIN COMPLEXED WITH 4-[(4-{[(2-AMINO-4-OXO-3,4-
REMARK 900 DIHYDROQUINAZOLIN- 6-YL)METHYL]AMINO}BENZOYL)AMINO]BUTANOIC ACID
REMARK 900 AND 5-O-PHOSPHONO-BETA-D-RIBOFURANOSYLAMINE
REMARK 900 RELATED ID: 4ZYT RELATED DB: PDB
REMARK 900 RELATED ID: 4ZYU RELATED DB: PDB
REMARK 900 RELATED ID: 4ZYV RELATED DB: PDB
REMARK 900 RELATED ID: 4ZYW RELATED DB: PDB
REMARK 900 RELATED ID: 4ZYX RELATED DB: PDB
REMARK 900 RELATED ID: 4ZYZ RELATED DB: PDB
REMARK 900 RELATED ID: 4ZZ0 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZZ1 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZZ2 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZZ3 RELATED DB: PDB
DBREF 4ZYY A 808 1010 UNP P22102 PUR2_HUMAN 808 1010
SEQADV 4ZYY MET A 807 UNP P22102 INITIATING METHIONINE
SEQADV 4ZYY HIS A 1011 UNP P22102 EXPRESSION TAG
SEQADV 4ZYY HIS A 1012 UNP P22102 EXPRESSION TAG
SEQADV 4ZYY HIS A 1013 UNP P22102 EXPRESSION TAG
SEQADV 4ZYY HIS A 1014 UNP P22102 EXPRESSION TAG
SEQADV 4ZYY HIS A 1015 UNP P22102 EXPRESSION TAG
SEQADV 4ZYY HIS A 1016 UNP P22102 EXPRESSION TAG
SEQRES 1 A 210 MET ALA ARG VAL ALA VAL LEU ILE SER GLY THR GLY SER
SEQRES 2 A 210 ASN LEU GLN ALA LEU ILE ASP SER THR ARG GLU PRO ASN
SEQRES 3 A 210 SER SER ALA GLN ILE ASP ILE VAL ILE SER ASN LYS ALA
SEQRES 4 A 210 ALA VAL ALA GLY LEU ASP LYS ALA GLU ARG ALA GLY ILE
SEQRES 5 A 210 PRO THR ARG VAL ILE ASN HIS LYS LEU TYR LYS ASN ARG
SEQRES 6 A 210 VAL GLU PHE ASP SER ALA ILE ASP LEU VAL LEU GLU GLU
SEQRES 7 A 210 PHE SER ILE ASP ILE VAL CYS LEU ALA GLY PHE MET ARG
SEQRES 8 A 210 ILE LEU SER GLY PRO PHE VAL GLN LYS TRP ASN GLY LYS
SEQRES 9 A 210 MET LEU ASN ILE HIS PRO SER LEU LEU PRO SER PHE LYS
SEQRES 10 A 210 GLY SER ASN ALA HIS GLU GLN ALA LEU GLU THR GLY VAL
SEQRES 11 A 210 THR VAL THR GLY CYS THR VAL HIS PHE VAL ALA GLU ASP
SEQRES 12 A 210 VAL ASP ALA GLY GLN ILE ILE LEU GLN GLU ALA VAL PRO
SEQRES 13 A 210 VAL LYS ARG GLY ASP THR VAL ALA THR LEU SER GLU ARG
SEQRES 14 A 210 VAL LYS LEU ALA GLU HIS LYS ILE PHE PRO ALA ALA LEU
SEQRES 15 A 210 GLN LEU VAL ALA SER GLY THR VAL GLN LEU GLY GLU ASN
SEQRES 16 A 210 GLY LYS ILE CYS TRP VAL LYS GLU GLU HIS HIS HIS HIS
SEQRES 17 A 210 HIS HIS
HET GAR A1101 18
HET 3YC A1102 32
HETNAM GAR GLYCINAMIDE RIBONUCLEOTIDE
HETNAM 3YC (S)-2-({5-[4-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-
HETNAM 2 3YC D]-PYRIMIDIN-6-YL)BUTYL]THIOPHENE-3-CARBONYL}AMINO)
HETNAM 3 3YC PENTANEDIOIC ACID
FORMUL 2 GAR C7 H13 N2 O8 P 2-
FORMUL 3 3YC C20 H23 N5 O6 S
FORMUL 4 HOH *150(H2 O)
HELIX 1 AA1 GLY A 818 ARG A 829 1 12
HELIX 2 AA2 VAL A 847 ALA A 856 1 10
HELIX 3 AA3 ASN A 864 TYR A 868 5 5
HELIX 4 AA4 ASN A 870 PHE A 885 1 16
HELIX 5 AA5 SER A 900 TRP A 907 1 8
HELIX 6 AA6 ASN A 926 GLY A 935 1 10
HELIX 7 AA7 THR A 968 SER A 993 1 26
SHEET 1 AA1 7 THR A 860 VAL A 862 0
SHEET 2 AA1 7 GLN A 836 SER A 842 1 N SER A 842 O ARG A 861
SHEET 3 AA1 7 ARG A 809 ILE A 814 1 N VAL A 810 O GLN A 836
SHEET 4 AA1 7 ILE A 889 LEU A 892 1 O CYS A 891 N LEU A 813
SHEET 5 AA1 7 MET A 911 HIS A 915 1 O LEU A 912 N LEU A 892
SHEET 6 AA1 7 VAL A 938 PHE A 945 -1 O THR A 942 N HIS A 915
SHEET 7 AA1 7 ILE A 955 PRO A 962 -1 O VAL A 961 N THR A 939
SHEET 1 AA2 2 VAL A 996 LEU A 998 0
SHEET 2 AA2 2 ILE A1004 TRP A1006 -1 O CYS A1005 N GLN A 997
CISPEP 1 LEU A 919 PRO A 920 0 12.69
SITE 1 AC1 18 THR A 817 GLY A 818 SER A 819 ASN A 820
SITE 2 AC1 18 GLY A 894 HIS A 915 PRO A 916 GLY A 924
SITE 3 AC1 18 LYS A 977 GLU A 980 3YC A1102 HOH A1201
SITE 4 AC1 18 HOH A1207 HOH A1232 HOH A1236 HOH A1253
SITE 5 AC1 18 HOH A1273 HOH A1279
SITE 1 AC2 16 ARG A 871 PHE A 895 MET A 896 ARG A 897
SITE 2 AC2 16 ILE A 898 LEU A 899 VAL A 904 HIS A 944
SITE 3 AC2 16 VAL A 946 ALA A 947 GLU A 948 VAL A 950
SITE 4 AC2 16 ASP A 951 GAR A1101 HOH A1238 HOH A1272
CRYST1 75.005 75.005 100.853 90.00 90.00 120.00 P 32 2 1 6
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 0.013332 0.007697 0.000000 0.00000
SCALE2 0.000000 0.015395 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009915 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
