HEADER TRANSFERASE 15-SEP-06 2IDK
TITLE CRYSTAL STRUCTURE OF RAT GLYCINE N-METHYLTRANSFERASE COMPLEXED WITH
TITLE 2 FOLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCINE N-METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: FOLATE-BINDING PROTEIN;
COMPND 5 EC: 2.1.1.20;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 STRAIN: SPRAGUE-DAWLEY;
SOURCE 6 GENE: GNMT;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PET17-B;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PR6
KEYWDS GLYCINE N-METHYLTRANSFERASE, RAT, FOLATE BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.LUKA,S.PAKHOMOVA,L.V.LOUKACHEVITCH,M.EGLI,M.E.NEWCOMER,C.WAGNER
REVDAT 5 30-AUG-23 2IDK 1 REMARK
REVDAT 4 18-OCT-17 2IDK 1 REMARK
REVDAT 3 24-FEB-09 2IDK 1 VERSN
REVDAT 2 01-MAY-07 2IDK 1 JRNL
REVDAT 1 19-DEC-06 2IDK 0
JRNL AUTH Z.LUKA,S.PAKHOMOVA,L.V.LOUKACHEVITCH,M.EGLI,M.E.NEWCOMER,
JRNL AUTH 2 C.WAGNER
JRNL TITL 5-METHYLTETRAHYDROFOLATE IS BOUND IN INTERSUBUNIT AREAS OF
JRNL TITL 2 RAT LIVER FOLATE-BINDING PROTEIN GLYCINE
JRNL TITL 3 N-METHYLTRANSFERASE.
JRNL REF J.BIOL.CHEM. V. 282 4069 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17158459
JRNL DOI 10.1074/JBC.M610384200
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.8
REMARK 3 NUMBER OF REFLECTIONS : 36594
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 SET) : 0.240
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1773
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.71
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.4100
REMARK 3 BIN FREE R VALUE : 0.4260
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 211
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.029
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8768
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 14
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.70000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : -11.47000
REMARK 3 B13 (A**2) : 2.77000
REMARK 3 B23 (A**2) : -0.97000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM SIGMAA (A) : 0.52
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.50
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.64
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.720
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2IDK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-06.
REMARK 100 THE DEPOSITION ID IS D_1000039449.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38846
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ID 1BHJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1 M CA ACETATE, 0.025
REMARK 280 M TRIS, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 42.37550
REMARK 290 SMTRY3 2 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 VAL A 1
REMARK 465 ASP A 197
REMARK 465 LEU A 198
REMARK 465 THR A 199
REMARK 465 VAL A 224
REMARK 465 PRO A 225
REMARK 465 GLY A 226
REMARK 465 ALA A 227
REMARK 465 GLY A 228
REMARK 465 ARG A 229
REMARK 465 ASP A 230
REMARK 465 GLY A 231
REMARK 465 ALA A 232
REMARK 465 PRO A 233
REMARK 465 GLY A 234
REMARK 465 GLY B 228
REMARK 465 ARG B 229
REMARK 465 ASP B 230
REMARK 465 GLY B 231
REMARK 465 ALA B 232
REMARK 465 PRO B 233
REMARK 465 GLY B 234
REMARK 465 VAL C 224
REMARK 465 PRO C 225
REMARK 465 GLY C 226
REMARK 465 ALA C 227
REMARK 465 GLY C 228
REMARK 465 ARG C 229
REMARK 465 ASP C 230
REMARK 465 GLY C 231
REMARK 465 ALA C 232
REMARK 465 PRO C 233
REMARK 465 GLY C 234
REMARK 465 GLY D 228
REMARK 465 ARG D 229
REMARK 465 ASP D 230
REMARK 465 GLY D 231
REMARK 465 ALA D 232
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 GLU A 25 CG CD OE1 OE2
REMARK 470 ASP A 36 CG OD1 OD2
REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 45 CG CD CE NZ
REMARK 470 HIS A 55 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 128 CG OD1 OD2
REMARK 470 LYS A 190 CG CD CE NZ
REMARK 470 ASN A 191 CG OD1 ND2
REMARK 470 TYR A 194 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 223 CG CD OE1 NE2
REMARK 470 PHE A 235 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL B 1 CG1 CG2
REMARK 470 ARG B 38 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 128 CG OD1 OD2
REMARK 470 GLN B 223 CG CD OE1 NE2
REMARK 470 PRO B 225 CG CD
REMARK 470 PHE B 235 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL C 1 CG1 CG2
REMARK 470 GLU C 25 CG CD OE1 OE2
REMARK 470 ASP C 36 CG OD1 OD2
REMARK 470 ASP C 128 CG OD1 OD2
REMARK 470 PRO C 188 CG CD
REMARK 470 LYS C 190 CG CD CE NZ
REMARK 470 TYR C 194 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 195 CG CD CE NZ
REMARK 470 SER C 196 OG
REMARK 470 ASP C 197 CG OD1 OD2
REMARK 470 GLN C 223 CG CD OE1 NE2
REMARK 470 ARG C 261 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 1 CG1 CG2
REMARK 470 ARG D 38 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 190 CG CD CE NZ
REMARK 470 GLN D 223 CG CD OE1 NE2
REMARK 470 PRO D 225 CG CD
REMARK 470 PRO D 233 CG CD
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 OD2 ASP C 173 OH TYR C 193 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG B 102 O GLY B 276 2555 2.08
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 TYR A 21 -1.00 72.03
REMARK 500 ASP A 36 32.89 -83.26
REMARK 500 THR A 37 20.78 -161.72
REMARK 500 HIS A 55 1.04 -163.50
REMARK 500 HIS A 58 -41.17 -135.15
REMARK 500 PRO A 105 -32.05 -36.64
REMARK 500 THR A 119 27.66 -144.91
REMARK 500 ALA A 126 -70.49 -113.03
REMARK 500 GLN A 150 -2.68 59.42
REMARK 500 SER A 162 29.89 -69.69
REMARK 500 ASN A 191 94.36 -59.50
REMARK 500 ILE A 192 -14.84 -144.07
REMARK 500 TYR A 193 -31.36 -136.03
REMARK 500 TYR A 194 -147.62 -138.80
REMARK 500 LYS A 195 59.58 -177.29
REMARK 500 ARG A 261 67.46 -66.47
REMARK 500 LEU A 267 -159.58 -107.97
REMARK 500 ASP A 269 46.46 71.97
REMARK 500 LYS A 290 83.30 -69.81
REMARK 500 THR A 291 -85.86 -50.95
REMARK 500 GLN B 20 -78.48 -10.21
REMARK 500 SER B 39 103.36 168.05
REMARK 500 GLN B 54 -4.87 -47.79
REMARK 500 PRO B 105 -35.59 -39.55
REMARK 500 ALA B 126 -82.17 -130.74
REMARK 500 CYS B 135 85.65 -151.05
REMARK 500 PRO B 187 149.49 -25.06
REMARK 500 PRO B 188 65.22 -55.16
REMARK 500 PHE B 270 -5.46 75.25
REMARK 500 TYR C 21 -1.21 71.44
REMARK 500 ASP C 36 32.21 -82.56
REMARK 500 THR C 37 20.81 -160.66
REMARK 500 ARG C 38 36.01 -95.32
REMARK 500 HIS C 55 -3.71 -161.53
REMARK 500 HIS C 58 -41.15 -135.06
REMARK 500 PRO C 105 -32.09 -36.28
REMARK 500 THR C 119 26.38 -145.09
REMARK 500 ALA C 126 -80.96 -88.08
REMARK 500 GLN C 150 -1.53 59.41
REMARK 500 SER C 162 30.34 -69.98
REMARK 500 ILE C 192 -0.76 -154.63
REMARK 500 TYR C 193 -76.75 -111.82
REMARK 500 ARG C 261 71.96 -67.28
REMARK 500 SER C 265 141.33 179.71
REMARK 500 PHE C 270 -27.83 86.11
REMARK 500 PRO C 272 171.82 -56.01
REMARK 500 THR C 291 -85.16 -50.63
REMARK 500 GLN D 20 -78.11 -9.90
REMARK 500 SER D 39 102.76 168.28
REMARK 500 GLN D 54 -5.88 -45.66
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C2F A 1410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C2F B 1420
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BHJ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, ORTHORHOMBIC FORM
REMARK 900 RELATED ID: 1NBH RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH SAM AND ACETATE
REMARK 900 RELATED ID: 1NBI RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH SAM
REMARK 900 RELATED ID: 1R74 RELATED DB: PDB
REMARK 900 HUMAN GNMT
REMARK 900 RELATED ID: 1R8X RELATED DB: PDB
REMARK 900 TETRAGONAL FORM OF MOUSE GNMT
REMARK 900 RELATED ID: 2IDJ RELATED DB: PDB
DBREF 2IDK A 1 292 UNP P13255 GNMT_RAT 1 292
DBREF 2IDK B 1 292 UNP P13255 GNMT_RAT 1 292
DBREF 2IDK C 1 292 UNP P13255 GNMT_RAT 1 292
DBREF 2IDK D 1 292 UNP P13255 GNMT_RAT 1 292
SEQRES 1 A 292 VAL ASP SER VAL TYR ARG THR ARG SER LEU GLY VAL ALA
SEQRES 2 A 292 ALA GLU GLY ILE PRO ASP GLN TYR ALA ASP GLY GLU ALA
SEQRES 3 A 292 ALA ARG VAL TRP GLN LEU TYR ILE GLY ASP THR ARG SER
SEQRES 4 A 292 ARG THR ALA GLU TYR LYS ALA TRP LEU LEU GLY LEU LEU
SEQRES 5 A 292 ARG GLN HIS GLY CYS HIS ARG VAL LEU ASP VAL ALA CYS
SEQRES 6 A 292 GLY THR GLY VAL ASP SER ILE MET LEU VAL GLU GLU GLY
SEQRES 7 A 292 PHE SER VAL THR SER VAL ASP ALA SER ASP LYS MET LEU
SEQRES 8 A 292 LYS TYR ALA LEU LYS GLU ARG TRP ASN ARG ARG LYS GLU
SEQRES 9 A 292 PRO ALA PHE ASP LYS TRP VAL ILE GLU GLU ALA ASN TRP
SEQRES 10 A 292 LEU THR LEU ASP LYS ASP VAL PRO ALA GLY ASP GLY PHE
SEQRES 11 A 292 ASP ALA VAL ILE CYS LEU GLY ASN SER PHE ALA HIS LEU
SEQRES 12 A 292 PRO ASP SER LYS GLY ASP GLN SER GLU HIS ARG LEU ALA
SEQRES 13 A 292 LEU LYS ASN ILE ALA SER MET VAL ARG PRO GLY GLY LEU
SEQRES 14 A 292 LEU VAL ILE ASP HIS ARG ASN TYR ASP TYR ILE LEU SER
SEQRES 15 A 292 THR GLY CYS ALA PRO PRO GLY LYS ASN ILE TYR TYR LYS
SEQRES 16 A 292 SER ASP LEU THR LYS ASP ILE THR THR SER VAL LEU THR
SEQRES 17 A 292 VAL ASN ASN LYS ALA HIS MET VAL THR LEU ASP TYR THR
SEQRES 18 A 292 VAL GLN VAL PRO GLY ALA GLY ARG ASP GLY ALA PRO GLY
SEQRES 19 A 292 PHE SER LYS PHE ARG LEU SER TYR TYR PRO HIS CYS LEU
SEQRES 20 A 292 ALA SER PHE THR GLU LEU VAL GLN GLU ALA PHE GLY GLY
SEQRES 21 A 292 ARG CYS GLN HIS SER VAL LEU GLY ASP PHE LYS PRO TYR
SEQRES 22 A 292 ARG PRO GLY GLN ALA TYR VAL PRO CYS TYR PHE ILE HIS
SEQRES 23 A 292 VAL LEU LYS LYS THR GLY
SEQRES 1 B 292 VAL ASP SER VAL TYR ARG THR ARG SER LEU GLY VAL ALA
SEQRES 2 B 292 ALA GLU GLY ILE PRO ASP GLN TYR ALA ASP GLY GLU ALA
SEQRES 3 B 292 ALA ARG VAL TRP GLN LEU TYR ILE GLY ASP THR ARG SER
SEQRES 4 B 292 ARG THR ALA GLU TYR LYS ALA TRP LEU LEU GLY LEU LEU
SEQRES 5 B 292 ARG GLN HIS GLY CYS HIS ARG VAL LEU ASP VAL ALA CYS
SEQRES 6 B 292 GLY THR GLY VAL ASP SER ILE MET LEU VAL GLU GLU GLY
SEQRES 7 B 292 PHE SER VAL THR SER VAL ASP ALA SER ASP LYS MET LEU
SEQRES 8 B 292 LYS TYR ALA LEU LYS GLU ARG TRP ASN ARG ARG LYS GLU
SEQRES 9 B 292 PRO ALA PHE ASP LYS TRP VAL ILE GLU GLU ALA ASN TRP
SEQRES 10 B 292 LEU THR LEU ASP LYS ASP VAL PRO ALA GLY ASP GLY PHE
SEQRES 11 B 292 ASP ALA VAL ILE CYS LEU GLY ASN SER PHE ALA HIS LEU
SEQRES 12 B 292 PRO ASP SER LYS GLY ASP GLN SER GLU HIS ARG LEU ALA
SEQRES 13 B 292 LEU LYS ASN ILE ALA SER MET VAL ARG PRO GLY GLY LEU
SEQRES 14 B 292 LEU VAL ILE ASP HIS ARG ASN TYR ASP TYR ILE LEU SER
SEQRES 15 B 292 THR GLY CYS ALA PRO PRO GLY LYS ASN ILE TYR TYR LYS
SEQRES 16 B 292 SER ASP LEU THR LYS ASP ILE THR THR SER VAL LEU THR
SEQRES 17 B 292 VAL ASN ASN LYS ALA HIS MET VAL THR LEU ASP TYR THR
SEQRES 18 B 292 VAL GLN VAL PRO GLY ALA GLY ARG ASP GLY ALA PRO GLY
SEQRES 19 B 292 PHE SER LYS PHE ARG LEU SER TYR TYR PRO HIS CYS LEU
SEQRES 20 B 292 ALA SER PHE THR GLU LEU VAL GLN GLU ALA PHE GLY GLY
SEQRES 21 B 292 ARG CYS GLN HIS SER VAL LEU GLY ASP PHE LYS PRO TYR
SEQRES 22 B 292 ARG PRO GLY GLN ALA TYR VAL PRO CYS TYR PHE ILE HIS
SEQRES 23 B 292 VAL LEU LYS LYS THR GLY
SEQRES 1 C 292 VAL ASP SER VAL TYR ARG THR ARG SER LEU GLY VAL ALA
SEQRES 2 C 292 ALA GLU GLY ILE PRO ASP GLN TYR ALA ASP GLY GLU ALA
SEQRES 3 C 292 ALA ARG VAL TRP GLN LEU TYR ILE GLY ASP THR ARG SER
SEQRES 4 C 292 ARG THR ALA GLU TYR LYS ALA TRP LEU LEU GLY LEU LEU
SEQRES 5 C 292 ARG GLN HIS GLY CYS HIS ARG VAL LEU ASP VAL ALA CYS
SEQRES 6 C 292 GLY THR GLY VAL ASP SER ILE MET LEU VAL GLU GLU GLY
SEQRES 7 C 292 PHE SER VAL THR SER VAL ASP ALA SER ASP LYS MET LEU
SEQRES 8 C 292 LYS TYR ALA LEU LYS GLU ARG TRP ASN ARG ARG LYS GLU
SEQRES 9 C 292 PRO ALA PHE ASP LYS TRP VAL ILE GLU GLU ALA ASN TRP
SEQRES 10 C 292 LEU THR LEU ASP LYS ASP VAL PRO ALA GLY ASP GLY PHE
SEQRES 11 C 292 ASP ALA VAL ILE CYS LEU GLY ASN SER PHE ALA HIS LEU
SEQRES 12 C 292 PRO ASP SER LYS GLY ASP GLN SER GLU HIS ARG LEU ALA
SEQRES 13 C 292 LEU LYS ASN ILE ALA SER MET VAL ARG PRO GLY GLY LEU
SEQRES 14 C 292 LEU VAL ILE ASP HIS ARG ASN TYR ASP TYR ILE LEU SER
SEQRES 15 C 292 THR GLY CYS ALA PRO PRO GLY LYS ASN ILE TYR TYR LYS
SEQRES 16 C 292 SER ASP LEU THR LYS ASP ILE THR THR SER VAL LEU THR
SEQRES 17 C 292 VAL ASN ASN LYS ALA HIS MET VAL THR LEU ASP TYR THR
SEQRES 18 C 292 VAL GLN VAL PRO GLY ALA GLY ARG ASP GLY ALA PRO GLY
SEQRES 19 C 292 PHE SER LYS PHE ARG LEU SER TYR TYR PRO HIS CYS LEU
SEQRES 20 C 292 ALA SER PHE THR GLU LEU VAL GLN GLU ALA PHE GLY GLY
SEQRES 21 C 292 ARG CYS GLN HIS SER VAL LEU GLY ASP PHE LYS PRO TYR
SEQRES 22 C 292 ARG PRO GLY GLN ALA TYR VAL PRO CYS TYR PHE ILE HIS
SEQRES 23 C 292 VAL LEU LYS LYS THR GLY
SEQRES 1 D 292 VAL ASP SER VAL TYR ARG THR ARG SER LEU GLY VAL ALA
SEQRES 2 D 292 ALA GLU GLY ILE PRO ASP GLN TYR ALA ASP GLY GLU ALA
SEQRES 3 D 292 ALA ARG VAL TRP GLN LEU TYR ILE GLY ASP THR ARG SER
SEQRES 4 D 292 ARG THR ALA GLU TYR LYS ALA TRP LEU LEU GLY LEU LEU
SEQRES 5 D 292 ARG GLN HIS GLY CYS HIS ARG VAL LEU ASP VAL ALA CYS
SEQRES 6 D 292 GLY THR GLY VAL ASP SER ILE MET LEU VAL GLU GLU GLY
SEQRES 7 D 292 PHE SER VAL THR SER VAL ASP ALA SER ASP LYS MET LEU
SEQRES 8 D 292 LYS TYR ALA LEU LYS GLU ARG TRP ASN ARG ARG LYS GLU
SEQRES 9 D 292 PRO ALA PHE ASP LYS TRP VAL ILE GLU GLU ALA ASN TRP
SEQRES 10 D 292 LEU THR LEU ASP LYS ASP VAL PRO ALA GLY ASP GLY PHE
SEQRES 11 D 292 ASP ALA VAL ILE CYS LEU GLY ASN SER PHE ALA HIS LEU
SEQRES 12 D 292 PRO ASP SER LYS GLY ASP GLN SER GLU HIS ARG LEU ALA
SEQRES 13 D 292 LEU LYS ASN ILE ALA SER MET VAL ARG PRO GLY GLY LEU
SEQRES 14 D 292 LEU VAL ILE ASP HIS ARG ASN TYR ASP TYR ILE LEU SER
SEQRES 15 D 292 THR GLY CYS ALA PRO PRO GLY LYS ASN ILE TYR TYR LYS
SEQRES 16 D 292 SER ASP LEU THR LYS ASP ILE THR THR SER VAL LEU THR
SEQRES 17 D 292 VAL ASN ASN LYS ALA HIS MET VAL THR LEU ASP TYR THR
SEQRES 18 D 292 VAL GLN VAL PRO GLY ALA GLY ARG ASP GLY ALA PRO GLY
SEQRES 19 D 292 PHE SER LYS PHE ARG LEU SER TYR TYR PRO HIS CYS LEU
SEQRES 20 D 292 ALA SER PHE THR GLU LEU VAL GLN GLU ALA PHE GLY GLY
SEQRES 21 D 292 ARG CYS GLN HIS SER VAL LEU GLY ASP PHE LYS PRO TYR
SEQRES 22 D 292 ARG PRO GLY GLN ALA TYR VAL PRO CYS TYR PHE ILE HIS
SEQRES 23 D 292 VAL LEU LYS LYS THR GLY
HET C2F A1410 33
HET C2F B1420 33
HETNAM C2F 5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID
FORMUL 5 C2F 2(C20 H25 N7 O6)
FORMUL 7 HOH *14(H2 O)
HELIX 1 1 GLY A 24 ILE A 34 1 11
HELIX 2 2 THR A 41 GLN A 54 1 14
HELIX 3 3 GLY A 68 GLU A 77 1 10
HELIX 4 4 SER A 87 ARG A 101 1 15
HELIX 5 5 GLU A 104 LYS A 109 1 6
HELIX 6 6 ASN A 116 LEU A 118 5 3
HELIX 7 7 THR A 119 VAL A 124 1 6
HELIX 8 8 ASN A 138 LEU A 143 5 6
HELIX 9 9 GLN A 150 SER A 162 1 13
HELIX 10 10 ASN A 176 GLY A 184 1 9
HELIX 11 11 CYS A 246 ALA A 257 1 12
HELIX 12 12 GLY B 24 GLY B 35 1 12
HELIX 13 13 THR B 41 GLN B 54 1 14
HELIX 14 14 GLY B 68 GLU B 77 1 10
HELIX 15 15 SER B 87 ARG B 101 1 15
HELIX 16 16 GLU B 104 LYS B 109 1 6
HELIX 17 17 ASN B 116 LEU B 118 5 3
HELIX 18 18 THR B 119 VAL B 124 1 6
HELIX 19 19 SER B 139 LEU B 143 5 5
HELIX 20 20 GLN B 150 MET B 163 1 14
HELIX 21 21 ASN B 176 GLY B 184 1 9
HELIX 22 22 CYS B 246 PHE B 258 1 13
HELIX 23 23 GLY C 24 ILE C 34 1 11
HELIX 24 24 THR C 41 GLN C 54 1 14
HELIX 25 25 GLY C 68 GLU C 77 1 10
HELIX 26 26 SER C 87 ARG C 101 1 15
HELIX 27 27 GLU C 104 LYS C 109 1 6
HELIX 28 28 ASN C 116 LEU C 118 5 3
HELIX 29 29 THR C 119 VAL C 124 1 6
HELIX 30 30 SER C 139 LEU C 143 5 5
HELIX 31 31 GLN C 150 SER C 162 1 13
HELIX 32 32 ASN C 176 GLY C 184 1 9
HELIX 33 33 CYS C 246 ALA C 257 1 12
HELIX 34 34 GLY D 24 GLY D 35 1 12
HELIX 35 35 THR D 41 GLN D 54 1 14
HELIX 36 36 GLY D 68 GLU D 77 1 10
HELIX 37 37 SER D 87 ARG D 101 1 15
HELIX 38 38 GLU D 104 LYS D 109 1 6
HELIX 39 39 ASN D 116 LEU D 118 5 3
HELIX 40 40 THR D 119 VAL D 124 1 6
HELIX 41 41 SER D 139 LEU D 143 5 5
HELIX 42 42 GLN D 150 MET D 163 1 14
HELIX 43 43 ASN D 176 GLY D 184 1 9
HELIX 44 44 CYS D 246 ALA D 257 1 12
SHEET 1 A 2 VAL A 4 ARG A 6 0
SHEET 2 A 2 VAL C 4 ARG C 6 -1 O TYR C 5 N TYR A 5
SHEET 1 B 7 VAL A 111 GLU A 114 0
SHEET 2 B 7 SER A 80 ASP A 85 1 N SER A 83 O VAL A 111
SHEET 3 B 7 ARG A 59 ASP A 62 1 N ASP A 62 O VAL A 84
SHEET 4 B 7 PHE A 130 CYS A 135 1 O ALA A 132 N LEU A 61
SHEET 5 B 7 VAL A 164 ARG A 175 1 O LEU A 169 N ASP A 131
SHEET 6 B 7 TYR A 283 LYS A 289 -1 O PHE A 284 N HIS A 174
SHEET 7 B 7 SER A 265 VAL A 266 -1 N SER A 265 O VAL A 287
SHEET 1 C 6 SER A 236 TYR A 242 0
SHEET 2 C 6 LYS A 212 VAL A 222 -1 N VAL A 216 O TYR A 242
SHEET 3 C 6 ASP A 201 VAL A 209 -1 N LEU A 207 O MET A 215
SHEET 4 C 6 ASP C 201 VAL C 209 -1 O THR C 208 N VAL A 206
SHEET 5 C 6 LYS C 212 VAL C 222 -1 O MET C 215 N LEU C 207
SHEET 6 C 6 SER C 236 TYR C 242 -1 O TYR C 242 N VAL C 216
SHEET 1 D 7 VAL B 111 GLU B 114 0
SHEET 2 D 7 SER B 80 ASP B 85 1 N SER B 83 O VAL B 111
SHEET 3 D 7 ARG B 59 ASP B 62 1 N VAL B 60 O SER B 80
SHEET 4 D 7 PHE B 130 CYS B 135 1 O ILE B 134 N LEU B 61
SHEET 5 D 7 VAL B 164 ARG B 175 1 O VAL B 171 N VAL B 133
SHEET 6 D 7 TYR B 283 LYS B 290 -1 O LYS B 290 N GLY B 167
SHEET 7 D 7 CYS B 262 GLY B 268 -1 N LEU B 267 O ILE B 285
SHEET 1 E 6 SER B 236 TYR B 242 0
SHEET 2 E 6 LYS B 212 VAL B 222 -1 N LEU B 218 O LEU B 240
SHEET 3 E 6 LYS B 200 VAL B 209 -1 N SER B 205 O THR B 217
SHEET 4 E 6 LYS D 200 VAL D 209 -1 O VAL D 206 N THR B 208
SHEET 5 E 6 LYS D 212 VAL D 224 -1 O THR D 217 N SER D 205
SHEET 6 E 6 GLY D 234 TYR D 242 -1 O LEU D 240 N LEU D 218
SHEET 1 F 8 VAL C 111 GLU C 114 0
SHEET 2 F 8 SER C 80 ASP C 85 1 N SER C 83 O VAL C 111
SHEET 3 F 8 ARG C 59 ASP C 62 1 N ASP C 62 O VAL C 84
SHEET 4 F 8 PHE C 130 CYS C 135 1 O ALA C 132 N LEU C 61
SHEET 5 F 8 VAL C 164 ARG C 175 1 O LEU C 169 N ASP C 131
SHEET 6 F 8 TYR C 283 LYS C 289 -1 O PHE C 284 N HIS C 174
SHEET 7 F 8 VAL C 266 GLY C 268 -1 N LEU C 267 O ILE C 285
SHEET 8 F 8 LYS C 271 PRO C 272 -1 O LYS C 271 N GLY C 268
SHEET 1 G 7 VAL D 111 GLU D 114 0
SHEET 2 G 7 SER D 80 ASP D 85 1 N SER D 83 O VAL D 111
SHEET 3 G 7 ARG D 59 ASP D 62 1 N VAL D 60 O SER D 80
SHEET 4 G 7 PHE D 130 CYS D 135 1 O ILE D 134 N LEU D 61
SHEET 5 G 7 VAL D 164 ARG D 175 1 O VAL D 171 N VAL D 133
SHEET 6 G 7 TYR D 283 LYS D 290 -1 O LYS D 290 N GLY D 167
SHEET 7 G 7 CYS D 262 GLY D 268 -1 N LEU D 267 O ILE D 285
SITE 1 AC1 12 TYR A 5 THR A 7 LEU B 207 HIS B 214
SITE 2 AC1 12 MET B 215 ARG B 239 SER C 3 VAL C 4
SITE 3 AC1 12 TYR C 5 LEU D 207 HIS D 214 MET D 215
SITE 1 AC2 10 LEU A 207 MET A 215 SER B 3 TYR B 5
SITE 2 AC2 10 LEU C 207 HIS C 214 MET C 215 ARG C 239
SITE 3 AC2 10 TYR D 5 THR D 7
CRYST1 57.427 84.751 132.245 90.00 91.61 90.00 P 1 21 1 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 0.017413 0.000000 0.000489 0.00000
SCALE2 0.000000 0.011799 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007565 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
