HEADER TRANSFERASE 17-OCT-03 1R74
TITLE CRYSTAL STRUCTURE OF HUMAN GLYCINE N-METHYLTRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCINE N-METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.1.1.20;
COMPND 5 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: GNMT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET17B;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PGE3
KEYWDS GLYCINE N-METHYLTRANSFERASE, HUMAN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.PAKHOMOVA,Z.LUKA,C.WAGNER,M.E.NEWCOMER
REVDAT 5 23-AUG-23 1R74 1 REMARK LINK
REVDAT 4 11-OCT-17 1R74 1 REMARK
REVDAT 3 13-JUL-11 1R74 1 VERSN
REVDAT 2 24-FEB-09 1R74 1 VERSN
REVDAT 1 21-SEP-04 1R74 0
JRNL AUTH S.PAKHOMOVA,Z.LUKA,S.GROHMANN,C.WAGNER,M.E.NEWCOMER
JRNL TITL GLYCINE N-METHYLTRANSFERASES: A COMPARISON OF THE CRYSTAL
JRNL TITL 2 STRUCTURES AND KINETIC PROPERTIES OF RECOMBINANT HUMAN,
JRNL TITL 3 MOUSE AND RAT ENZYMES.
JRNL REF PROTEINS V. 57 331 2004
JRNL REFN ISSN 0887-3585
JRNL PMID 15340920
JRNL DOI 10.1002/PROT.20209
REMARK 2
REMARK 2 RESOLUTION. 2.55 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) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 22070
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1623
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1487
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 135
REMARK 3 BIN FREE R VALUE : 0.3970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4240
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 60
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : 0.48000
REMARK 3 B33 (A**2) : -0.35000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.560
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.310
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.245
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.270
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4381 ; 0.027 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3904 ; 0.010 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5945 ; 2.167 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9038 ; 1.605 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 549 ; 7.843 ; 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): 656 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4929 ; 0.017 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 917 ; 0.033 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 952 ; 0.242 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4270 ; 0.252 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2666 ; 0.100 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 94 ; 0.158 ; 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): 13 ; 0.119 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 40 ; 0.345 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.438 ; 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): 2741 ; 0.862 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4355 ; 1.568 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1640 ; 2.588 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1590 ; 4.003 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 6 A 125 1
REMARK 3 1 B 6 B 126 1
REMARK 3 2 A 133 A 224 1
REMARK 3 2 B 133 B 225 1
REMARK 3 3 A 237 A 293 1
REMARK 3 3 B 237 B 293 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 3729 ; 0.14 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 3729 ; 0.21 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1R74 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020518.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-02; NULL
REMARK 200 TEMPERATURE (KELVIN) : 103; NULL
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N; NULL
REMARK 200 RADIATION SOURCE : ROTATING ANODE; NULL
REMARK 200 BEAMLINE : NULL; NULL
REMARK 200 X-RAY GENERATOR MODEL : ENRAF-NONIUS FR591; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; NULL
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : MIRRORS; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; NULL
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23864
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 12.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
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) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.38900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1XVA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, NA CITRATE, PH 5.6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 273K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 37.92000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.61500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.92000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.61500
REMARK 290 SMTRY3 4 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER
REMARK 300 GENERATED FROM THE DIMER IN THE ASYMMETRIC UNIT BY THE OPERATION:
REMARK 300 -X+2,-Y-1,Z
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 15370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 151.68000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -83.23000
REMARK 350 BIOMT3 2 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 2
REMARK 465 SER A 3
REMARK 465 VAL A 4
REMARK 465 GLN A 126
REMARK 465 SER A 127
REMARK 465 ALA A 128
REMARK 465 GLN A 225
REMARK 465 VAL A 226
REMARK 465 PRO A 227
REMARK 465 GLY A 228
REMARK 465 ALA A 229
REMARK 465 GLY A 230
REMARK 465 GLN A 231
REMARK 465 ASP A 232
REMARK 465 GLY A 233
REMARK 465 SER A 234
REMARK 465 PRO A 235
REMARK 465 ASP A 294
REMARK 465 VAL B 1
REMARK 465 ASP B 2
REMARK 465 SER B 3
REMARK 465 VAL B 4
REMARK 465 VAL B 226
REMARK 465 PRO B 227
REMARK 465 GLY B 228
REMARK 465 ALA B 229
REMARK 465 GLY B 230
REMARK 465 GLN B 231
REMARK 465 ASP B 232
REMARK 465 GLY B 233
REMARK 465 SER B 234
REMARK 465 PRO B 235
REMARK 465 ASP B 294
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 GLN A 31 CG CD OE1 NE2
REMARK 470 ILE A 34 CG1 CG2 CD1
REMARK 470 ASP A 36 CG OD1 OD2
REMARK 470 THR A 37 OG1 CG2
REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2
REMARK 470 SER A 39 OG
REMARK 470 ARG A 40 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 43 CG CD OE1 OE2
REMARK 470 ARG A 53 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 59 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 75 CG1 CG2
REMARK 470 LYS A 89 CG CD CE NZ
REMARK 470 GLU A 129 CG CD OE1 OE2
REMARK 470 LYS A 149 CG CD CE NZ
REMARK 470 SER A 153 OG
REMARK 470 LYS A 160 CG CD CE NZ
REMARK 470 LYS A 192 CG CD CE NZ
REMARK 470 LYS A 197 CG CD CE NZ
REMARK 470 SER A 238 OG
REMARK 470 LYS A 239 CG CD CE NZ
REMARK 470 LYS A 263 CG CD CE NZ
REMARK 470 GLN A 265 CG CD OE1 NE2
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 ILE A 282 CG1 CG2 CD1
REMARK 470 ARG B 28 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 38 CG CD NE CZ NH1 NH2
REMARK 470 SER B 127 OG
REMARK 470 GLU B 129 CG CD OE1 OE2
REMARK 470 LYS B 149 CG CD CE NZ
REMARK 470 LYS B 160 CG CD CE NZ
REMARK 470 GLN B 225 CG CD OE1 NE2
REMARK 470 LYS B 276 CG CD CE NZ
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 O THR A 185 ND2 ASN A 213 2745 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 43 CG GLU B 43 CD 0.102
REMARK 500 TYR B 44 CD1 TYR B 44 CE1 0.107
REMARK 500 GLN B 54 CG GLN B 54 CD 0.187
REMARK 500 VAL B 63 CB VAL B 63 CG1 -0.169
REMARK 500 VAL B 69 CB VAL B 69 CG2 0.141
REMARK 500 LYS B 160 CA LYS B 160 CB 0.138
REMARK 500 SER B 184 CB SER B 184 OG -0.098
REMARK 500 TYR B 244 CD1 TYR B 244 CE1 -0.095
REMARK 500 TYR B 245 CZ TYR B 245 CE2 0.079
REMARK 500 HIS B 247 CE1 HIS B 247 NE2 -0.100
REMARK 500 CYS B 248 CB CYS B 248 SG 0.119
REMARK 500
REMARK 500 REMARK: NULL
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 A 19 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 85 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP A 133 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 151 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 180 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP B 62 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 85 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP B 88 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 98 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP B 123 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP B 151 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG B 167 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 CYS B 264 CA - CB - SG ANGL. DEV. = 8.8 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 SER A 39 73.25 -151.85
REMARK 500 ASN A 213 15.56 56.16
REMARK 500 PHE A 272 -4.37 77.53
REMARK 500 GLN A 279 150.81 -42.38
REMARK 500 ASP B 36 77.85 -110.18
REMARK 500 SER B 127 -175.68 -46.61
REMARK 500 ALA B 128 63.02 -68.85
REMARK 500 GLU B 129 -88.31 -166.21
REMARK 500 ASN B 140 32.26 71.78
REMARK 500 ASN B 213 19.60 56.16
REMARK 500 PHE B 272 -8.99 77.62
REMARK 500 GLN B 279 151.24 -44.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 HIS A 181 0.06 SIDE CHAIN
REMARK 500 HIS B 247 0.08 SIDE CHAIN
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 BME A 1187
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 2187
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 2264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 2284
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 2001
DBREF 1R74 A 1 294 UNP Q14749 GNMT_HUMAN 1 294
DBREF 1R74 B 1 294 UNP Q14749 GNMT_HUMAN 1 294
SEQRES 1 A 294 VAL ASP SER VAL TYR ARG THR ARG SER LEU GLY VAL ALA
SEQRES 2 A 294 ALA GLU GLY LEU PRO ASP GLN TYR ALA ASP GLY GLU ALA
SEQRES 3 A 294 ALA ARG VAL TRP GLN LEU TYR ILE GLY ASP THR ARG SER
SEQRES 4 A 294 ARG THR ALA GLU TYR LYS ALA TRP LEU LEU GLY LEU LEU
SEQRES 5 A 294 ARG GLN HIS GLY CYS GLN ARG VAL LEU ASP VAL ALA CYS
SEQRES 6 A 294 GLY THR GLY VAL ASP SER ILE MET LEU VAL GLU GLU GLY
SEQRES 7 A 294 PHE SER VAL THR SER VAL ASP ALA SER ASP LYS MET LEU
SEQRES 8 A 294 LYS TYR ALA LEU LYS GLU ARG TRP ASN ARG ARG HIS GLU
SEQRES 9 A 294 PRO ALA PHE ASP LYS TRP VAL ILE GLU GLU ALA ASN TRP
SEQRES 10 A 294 MET THR LEU ASP LYS ASP VAL PRO GLN SER ALA GLU GLY
SEQRES 11 A 294 GLY PHE ASP ALA VAL ILE CYS LEU GLY ASN SER PHE ALA
SEQRES 12 A 294 HIS LEU PRO ASP CYS LYS GLY ASP GLN SER GLU HIS ARG
SEQRES 13 A 294 LEU ALA LEU LYS ASN ILE ALA SER MET VAL ARG ALA GLY
SEQRES 14 A 294 GLY LEU LEU VAL ILE ASP HIS ARG ASN TYR ASP HIS ILE
SEQRES 15 A 294 LEU SER THR GLY CYS ALA PRO PRO GLY LYS ASN ILE TYR
SEQRES 16 A 294 TYR LYS SER ASP LEU THR LYS ASP VAL THR THR SER VAL
SEQRES 17 A 294 LEU ILE VAL ASN ASN LYS ALA HIS MET VAL THR LEU ASP
SEQRES 18 A 294 TYR THR VAL GLN VAL PRO GLY ALA GLY GLN ASP GLY SER
SEQRES 19 A 294 PRO GLY LEU SER LYS PHE ARG LEU SER TYR TYR PRO HIS
SEQRES 20 A 294 CYS LEU ALA SER PHE THR GLU LEU LEU GLN ALA ALA PHE
SEQRES 21 A 294 GLY GLY LYS CYS GLN HIS SER VAL LEU GLY ASP PHE LYS
SEQRES 22 A 294 PRO TYR LYS PRO GLY GLN THR TYR ILE PRO CYS TYR PHE
SEQRES 23 A 294 ILE HIS VAL LEU LYS ARG THR ASP
SEQRES 1 B 294 VAL ASP SER VAL TYR ARG THR ARG SER LEU GLY VAL ALA
SEQRES 2 B 294 ALA GLU GLY LEU PRO ASP GLN TYR ALA ASP GLY GLU ALA
SEQRES 3 B 294 ALA ARG VAL TRP GLN LEU TYR ILE GLY ASP THR ARG SER
SEQRES 4 B 294 ARG THR ALA GLU TYR LYS ALA TRP LEU LEU GLY LEU LEU
SEQRES 5 B 294 ARG GLN HIS GLY CYS GLN ARG VAL LEU ASP VAL ALA CYS
SEQRES 6 B 294 GLY THR GLY VAL ASP SER ILE MET LEU VAL GLU GLU GLY
SEQRES 7 B 294 PHE SER VAL THR SER VAL ASP ALA SER ASP LYS MET LEU
SEQRES 8 B 294 LYS TYR ALA LEU LYS GLU ARG TRP ASN ARG ARG HIS GLU
SEQRES 9 B 294 PRO ALA PHE ASP LYS TRP VAL ILE GLU GLU ALA ASN TRP
SEQRES 10 B 294 MET THR LEU ASP LYS ASP VAL PRO GLN SER ALA GLU GLY
SEQRES 11 B 294 GLY PHE ASP ALA VAL ILE CYS LEU GLY ASN SER PHE ALA
SEQRES 12 B 294 HIS LEU PRO ASP CYS LYS GLY ASP GLN SER GLU HIS ARG
SEQRES 13 B 294 LEU ALA LEU LYS ASN ILE ALA SER MET VAL ARG ALA GLY
SEQRES 14 B 294 GLY LEU LEU VAL ILE ASP HIS ARG ASN TYR ASP HIS ILE
SEQRES 15 B 294 LEU SER THR GLY CYS ALA PRO PRO GLY LYS ASN ILE TYR
SEQRES 16 B 294 TYR LYS SER ASP LEU THR LYS ASP VAL THR THR SER VAL
SEQRES 17 B 294 LEU ILE VAL ASN ASN LYS ALA HIS MET VAL THR LEU ASP
SEQRES 18 B 294 TYR THR VAL GLN VAL PRO GLY ALA GLY GLN ASP GLY SER
SEQRES 19 B 294 PRO GLY LEU SER LYS PHE ARG LEU SER TYR TYR PRO HIS
SEQRES 20 B 294 CYS LEU ALA SER PHE THR GLU LEU LEU GLN ALA ALA PHE
SEQRES 21 B 294 GLY GLY LYS CYS GLN HIS SER VAL LEU GLY ASP PHE LYS
SEQRES 22 B 294 PRO TYR LYS PRO GLY GLN THR TYR ILE PRO CYS TYR PHE
SEQRES 23 B 294 ILE HIS VAL LEU LYS ARG THR ASP
HET BME A1187 4
HET CIT A1001 13
HET BME B2187 4
HET BME B2264 4
HET BME B2284 4
HET CIT B2001 13
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM CIT CITRIC ACID
FORMUL 3 BME 4(C2 H6 O S)
FORMUL 4 CIT 2(C6 H8 O7)
FORMUL 9 HOH *60(H2 O)
HELIX 1 1 GLY A 24 GLY A 24 5 1
HELIX 2 2 ALA A 26 VAL A 29 5 4
HELIX 3 3 TYR A 44 LEU A 52 1 9
HELIX 4 4 GLY A 68 LEU A 74 1 7
HELIX 5 5 GLU A 76 GLY A 78 5 3
HELIX 6 6 MET A 90 ARG A 101 1 12
HELIX 7 7 GLU A 104 LYS A 109 1 6
HELIX 8 8 ASN A 116 MET A 118 5 3
HELIX 9 9 THR A 119 VAL A 124 1 6
HELIX 10 10 SER A 141 LEU A 145 5 5
HELIX 11 11 GLU A 154 LEU A 159 1 6
HELIX 12 12 ASN A 161 SER A 164 5 4
HELIX 13 13 ASN A 178 GLY A 186 1 9
HELIX 14 14 CYS A 248 PHE A 260 1 13
HELIX 15 15 VAL B 29 ILE B 34 1 6
HELIX 16 16 THR B 41 HIS B 55 1 15
HELIX 17 17 GLY B 68 GLU B 77 1 10
HELIX 18 18 SER B 87 ARG B 101 1 15
HELIX 19 19 GLU B 104 LYS B 109 1 6
HELIX 20 20 ASN B 116 MET B 118 5 3
HELIX 21 21 THR B 119 VAL B 124 1 6
HELIX 22 22 SER B 141 LEU B 145 5 5
HELIX 23 23 GLN B 152 LEU B 159 1 8
HELIX 24 24 ASN B 161 SER B 164 5 4
HELIX 25 25 ASN B 178 GLY B 186 1 9
HELIX 26 26 CYS B 248 PHE B 260 1 13
SHEET 1 A 8 VAL A 111 GLU A 114 0
SHEET 2 A 8 THR A 82 ASP A 85 1 N SER A 83 O VAL A 111
SHEET 3 A 8 LEU A 61 VAL A 63 1 N ASP A 62 O THR A 82
SHEET 4 A 8 PHE A 132 CYS A 137 1 O ILE A 136 N VAL A 63
SHEET 5 A 8 VAL A 166 ARG A 177 1 O ARG A 167 N PHE A 132
SHEET 6 A 8 TYR A 285 LYS A 291 -1 O HIS A 288 N ILE A 174
SHEET 7 A 8 SER A 267 GLY A 270 -1 N LEU A 269 O ILE A 287
SHEET 8 A 8 LYS A 273 PRO A 274 -1 O LYS A 273 N GLY A 270
SHEET 1 B 3 ASP A 203 VAL A 211 0
SHEET 2 B 3 LYS A 214 THR A 223 -1 O MET A 217 N LEU A 209
SHEET 3 B 3 ARG A 241 TYR A 244 -1 O LEU A 242 N LEU A 220
SHEET 1 C 8 VAL B 111 GLU B 114 0
SHEET 2 C 8 SER B 80 ASP B 85 1 N SER B 83 O VAL B 111
SHEET 3 C 8 ARG B 59 VAL B 63 1 N ASP B 62 O THR B 82
SHEET 4 C 8 PHE B 132 CYS B 137 1 O ILE B 136 N VAL B 63
SHEET 5 C 8 VAL B 166 ARG B 177 1 O VAL B 173 N CYS B 137
SHEET 6 C 8 TYR B 285 ARG B 292 -1 O LEU B 290 N LEU B 172
SHEET 7 C 8 CYS B 264 GLY B 270 -1 N LEU B 269 O ILE B 287
SHEET 8 C 8 LYS B 273 PRO B 274 -1 O LYS B 273 N GLY B 270
SHEET 1 D 3 LYS B 202 VAL B 211 0
SHEET 2 D 3 LYS B 214 VAL B 224 -1 O MET B 217 N LEU B 209
SHEET 3 D 3 SER B 238 TYR B 244 -1 O TYR B 244 N VAL B 218
LINK SG CYS A 187 S2 BME A1187 1555 1555 2.06
LINK SG CYS B 187 S2 BME B2187 1555 1555 2.02
LINK SG CYS B 264 S2 BME B2264 1555 1555 2.02
LINK SG CYS B 284 S2 BME B2284 1555 1555 2.07
SITE 1 AC1 6 GLN A 54 GLY A 186 CYS A 187 VAL A 204
SITE 2 AC1 6 THR A 206 ASN A 212
SITE 1 AC2 8 TYR A 33 GLY A 139 ASN A 140 HIS A 144
SITE 2 AC2 8 ASN A 193 TYR A 244 TYR A 285 GLU B 15
SITE 1 AC3 8 ARG B 53 GLN B 54 GLY B 56 GLY B 186
SITE 2 AC3 8 CYS B 187 VAL B 204 THR B 206 ASN B 212
SITE 1 AC4 4 GLN B 257 CYS B 264 GLN B 265 HIS B 266
SITE 1 AC5 2 LYS B 192 CYS B 284
SITE 1 AC6 10 TYR B 33 GLY B 139 ASN B 140 HIS B 144
SITE 2 AC6 10 ASN B 193 TYR B 222 TYR B 244 TYR B 285
SITE 3 AC6 10 HOH B2286 HOH B2320
CRYST1 75.840 83.230 114.880 90.00 90.00 90.00 P 21 21 2 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 0.013186 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012015 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008705 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
