HEADER LIGASE 22-JUN-09 3HY4
TITLE STRUCTURE OF HUMAN MTHFS WITH N5-IMINIUM PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 5,10-METHENYL-TETRAHYDROFOLATE SYNTHETASE, METHENYL-THF
COMPND 5 SYNTHETASE, MTHFS;
COMPND 6 EC: 6.3.3.2;
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: MTHFS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS ANTIFOLATE, CANCER, N5-IMINIUM PHOSPHATE, ACETYLATION, ATP-BINDING,
KEYWDS 2 CYTOPLASM, FOLATE-BINDING, LIGASE, MAGNESIUM, NUCLEOTIDE-BINDING,
KEYWDS 3 POLYMORPHISM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.WU,Y.LI,G.SONG,C.CHENG,N.SHAW,Z.-J.LIU
REVDAT 4 01-NOV-23 3HY4 1 REMARK
REVDAT 3 20-OCT-09 3HY4 1 JRNL
REVDAT 2 28-JUL-09 3HY4 1 REMARK
REVDAT 1 14-JUL-09 3HY4 0
JRNL AUTH D.WU,Y.LI,G.SONG,C.CHENG,R.ZHANG,A.JOACHIMIAK,N.SHAW,
JRNL AUTH 2 Z.-J.LIU
JRNL TITL STRUCTURAL BASIS FOR THE INHIBITION OF HUMAN
JRNL TITL 2 5,10-METHENYLTETRAHYDROFOLATE SYNTHETASE BY N10-SUBSTITUTED
JRNL TITL 3 FOLATE ANALOGUES
JRNL REF CANCER RES. V. 69 7294 2009
JRNL REFN ISSN 0008-5472
JRNL PMID 19738041
JRNL DOI 10.1158/0008-5472.CAN-09-1927
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 5426
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.300
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.460
REMARK 3 FREE R VALUE TEST SET COUNT : 242
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 19.3210 - 3.5180 0.99 2644 125 0.2130 0.2750
REMARK 3 2 3.5180 - 2.7950 0.99 2540 117 0.2500 0.3490
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 : 0.37
REMARK 3 B_SOL : 32.49
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.480
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.800
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.88600
REMARK 3 B22 (A**2) : 1.45800
REMARK 3 B33 (A**2) : -7.34500
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 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 : 0.004 1617
REMARK 3 ANGLE : 0.769 2167
REMARK 3 CHIRALITY : 0.046 228
REMARK 3 PLANARITY : 0.005 276
REMARK 3 DIHEDRAL : 18.413 643
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE LIGAND N5G IN THIS ENTRY IS N5
REMARK 3 -IMINIUM PHOSPHATE. HOWEVER, THERE IS SOME DISCREPANCY IN THE
REMARK 3 GEOMETRY. THE GEOMETRY FOR N5G IS SUGGESTED BY THE REFINEMENT.
REMARK 3 THE CO-ORDINATES FIT WELL IN THE ELECTRON DENSITY MAP. THE MAP
REMARK 3 WAS GENERATED USING A DATASET COLLECTED AT 2.8 ANGSTROM
REMARK 3 RESOLUTION. THE DENSITY FOR THE LIGAND IS UNAMBIGUOUS AND
REMARK 3 THEREFORE THE GEOMETRIES ARE CORRECT AND ARE AS THEY WOULD BE IN
REMARK 3 A BIOLOGICAL MOLECULE, WHERE THE MICRO ENVIRONMENT HAS A
REMARK 3 PROFOUND INFLUENCE ON THE GEOMETRIES OF THE LIGAND.
REMARK 4
REMARK 4 3HY4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053725.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6020
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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
REMARK 200 STARTING MODEL: PDB ENTRY 3HXT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, PH6.6, 20MM MGCL2.6H2O,
REMARK 280 20MM NICL2.6H2O, 20% (W/V) PEG 3350, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
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 30.07450
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 30.07450
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 24.03250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.29150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.03250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.29150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 30.07450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.03250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 72.29150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 30.07450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.03250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 72.29150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 ALA A 23
REMARK 465 GLU A 187
REMARK 465 ASN A 188
REMARK 465 ASP A 199
REMARK 465 SER A 200
REMARK 465 SER A 201
REMARK 465 THR A 202
REMARK 465 ALA A 203
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 GLN A 19 CG CD OE1 NE2
REMARK 470 ARG A 22 CB CG CD NE CZ NH1 NH2
REMARK 470 MET A 24 CG SD CE
REMARK 470 GLN A 182 CG CD OE1 NE2
REMARK 470 VAL A 185 CG1 CG2
REMARK 470 ASP A 189 CG OD1 OD2
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 LEU A 21 -103.29 -67.41
REMARK 500 ASP A 60 35.33 -94.96
REMARK 500 SER A 87 -147.14 -120.05
REMARK 500 GLN A 162 -70.87 -61.92
REMARK 500 LEU A 181 -70.05 -67.58
REMARK 500 TYR A 197 -169.54 177.67
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 N5G A 501
REMARK 610 PO4 A 502
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 204 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 89 NE2
REMARK 620 2 ASP A 91 OD2 106.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N5G A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HXT RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MTHFS, APO ENZYME
REMARK 900 RELATED ID: 3HY3 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MTHFS COMPLEXED WITH 10-FORMYLTETRAHYDROFOLATE
REMARK 900 RELATED ID: 3HY6 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN MTHFS WITH ADP
DBREF 3HY4 A 1 203 UNP P49914 MTHFS_HUMAN 1 203
SEQRES 1 A 203 MET ALA ALA ALA ALA VAL SER SER ALA LYS ARG SER LEU
SEQRES 2 A 203 ARG GLY GLU LEU LYS GLN ARG LEU ARG ALA MET SER ALA
SEQRES 3 A 203 GLU GLU ARG LEU ARG GLN SER ARG VAL LEU SER GLN LYS
SEQRES 4 A 203 VAL ILE ALA HIS SER GLU TYR GLN LYS SER LYS ARG ILE
SEQRES 5 A 203 SER ILE PHE LEU SER MET GLN ASP GLU ILE GLU THR GLU
SEQRES 6 A 203 GLU ILE ILE LYS ASP ILE PHE GLN ARG GLY LYS ILE CYS
SEQRES 7 A 203 PHE ILE PRO ARG TYR ARG PHE GLN SER ASN HIS MET ASP
SEQRES 8 A 203 MET VAL ARG ILE GLU SER PRO GLU GLU ILE SER LEU LEU
SEQRES 9 A 203 PRO LYS THR SER TRP ASN ILE PRO GLN PRO GLY GLU GLY
SEQRES 10 A 203 ASP VAL ARG GLU GLU ALA LEU SER THR GLY GLY LEU ASP
SEQRES 11 A 203 LEU ILE PHE MET PRO GLY LEU GLY PHE ASP LYS HIS GLY
SEQRES 12 A 203 ASN ARG LEU GLY ARG GLY LYS GLY TYR TYR ASP ALA TYR
SEQRES 13 A 203 LEU LYS ARG CYS LEU GLN HIS GLN GLU VAL LYS PRO TYR
SEQRES 14 A 203 THR LEU ALA LEU ALA PHE LYS GLU GLN ILE CYS LEU GLN
SEQRES 15 A 203 VAL PRO VAL ASN GLU ASN ASP MET LYS VAL ASP GLU VAL
SEQRES 16 A 203 LEU TYR GLU ASP SER SER THR ALA
HET NI A 204 1
HET MG A 205 1
HET MG A 206 1
HET MG A 207 1
HET N5G A 501 34
HET PO4 A 502 4
HETNAM NI NICKEL (II) ION
HETNAM MG MAGNESIUM ION
HETNAM N5G N-({TRANS-4-[({(2R,4R,4AS,6S,8AS)-2-AMINO-4-HYDROXY-5-
HETNAM 2 N5G [(PHOSPHONOOXY)METHYL]DECAHYDROPTERIDIN-6-YL}METHYL)
HETNAM 3 N5G AMINO]CYCLOHEXYL}CARBONYL)-L-GLUTAMIC ACID
HETNAM PO4 PHOSPHATE ION
FORMUL 2 NI NI 2+
FORMUL 3 MG 3(MG 2+)
FORMUL 6 N5G C20 H38 N7 O10 P
FORMUL 7 PO4 O4 P 3-
FORMUL 8 HOH *46(H2 O)
HELIX 1 1 MET A 1 ARG A 22 1 22
HELIX 2 2 SER A 25 ALA A 42 1 18
HELIX 3 3 HIS A 43 SER A 49 1 7
HELIX 4 4 THR A 64 ARG A 74 1 11
HELIX 5 5 SER A 97 LEU A 103 5 7
HELIX 6 6 GLU A 122 THR A 126 5 5
HELIX 7 7 GLY A 151 GLN A 164 1 14
HELIX 8 8 PHE A 175 GLU A 177 5 3
SHEET 1 A 6 MET A 90 ARG A 94 0
SHEET 2 A 6 ILE A 77 TYR A 83 -1 N ILE A 80 O VAL A 93
SHEET 3 A 6 ARG A 51 SER A 53 1 N ILE A 52 O ILE A 77
SHEET 4 A 6 LEU A 131 MET A 134 1 O PHE A 133 N SER A 53
SHEET 5 A 6 TYR A 169 LEU A 173 1 O LEU A 171 N MET A 134
SHEET 6 A 6 GLU A 194 LEU A 196 1 O LEU A 196 N ALA A 172
SHEET 1 B 3 ARG A 145 LEU A 146 0
SHEET 2 B 3 GLY A 138 ASP A 140 -1 N GLY A 138 O LEU A 146
SHEET 3 B 3 ILE A 179 CYS A 180 1 O CYS A 180 N PHE A 139
LINK NE2 HIS A 89 NI NI A 204 1555 1555 2.52
LINK OD2 ASP A 91 NI NI A 204 1555 1555 2.33
SITE 1 AC1 5 ARG A 82 HIS A 89 ASP A 91 HIS A 163
SITE 2 AC1 5 HOH A 250
SITE 1 AC2 2 GLU A 27 HIS A 142
SITE 1 AC3 2 LEU A 181 HOH A 233
SITE 1 AC4 4 MET A 92 ALA A 123 LEU A 124 TYR A 156
SITE 1 AC5 16 PHE A 55 LEU A 56 GLU A 61 TYR A 83
SITE 2 AC5 16 MET A 90 TRP A 109 PRO A 135 ARG A 148
SITE 3 AC5 16 GLY A 149 LYS A 150 TYR A 152 TYR A 153
SITE 4 AC5 16 HOH A 217 HOH A 230 HOH A 251 PO4 A 502
SITE 1 AC6 10 ARG A 145 GLY A 147 ARG A 148 GLY A 149
SITE 2 AC6 10 LYS A 150 GLY A 151 TYR A 152 TYR A 153
SITE 3 AC6 10 ASP A 154 N5G A 501
CRYST1 48.065 144.583 60.149 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.020805 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006916 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016625 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
