HEADER TRANSFERASE 10-JAN-96 1MXB
TITLE S-ADENOSYLMETHIONINE SYNTHETASE WITH ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-ADENOSYLMETHIONINE SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAT, ATP\:L-METHIONINE S-ADENOSYLTRANSFERASE;
COMPND 5 EC: 2.5.1.6
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS TRANSFERASE, ONE-CARBON METABOLISM, ATP-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR F.TAKUSAGAWA,S.KAMITORI,G.D.MARKHAM
REVDAT 7 03-APR-24 1MXB 1 REMARK
REVDAT 6 14-FEB-24 1MXB 1 REMARK LINK
REVDAT 5 16-NOV-11 1MXB 1 HETATM
REVDAT 4 13-JUL-11 1MXB 1 VERSN
REVDAT 3 24-FEB-09 1MXB 1 VERSN
REVDAT 2 01-APR-03 1MXB 1 JRNL
REVDAT 1 11-JUL-96 1MXB 0
JRNL AUTH F.TAKUSAGAWA,S.KAMITORI,G.D.MARKHAM
JRNL TITL STRUCTURE AND FUNCTION OF S-ADENOSYLMETHIONINE SYNTHETASE:
JRNL TITL 2 CRYSTAL STRUCTURES OF S-ADENOSYLMETHIONINE SYNTHETASE WITH
JRNL TITL 3 ADP, BRADP, AND PPI AT 28 ANGSTROMS RESOLUTION.
JRNL REF BIOCHEMISTRY V. 35 2586 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8611562
JRNL DOI 10.1021/BI952604Z
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
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) (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 16033
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2899
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.80
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 3.040
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.460
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 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:
REMARK 3 RESIDUES 102 - 107 WERE NOT FOUND DUE TO HIGH
REMARK 3 TEMPERATURE FACTORS.
REMARK 4
REMARK 4 1MXB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175183.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 6
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN MULTIWIRE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : KUAVST, KUMDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16033
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.05300
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) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.22000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: MAT ITSELF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2
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 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 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 93.20000
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 46.60000
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 93.20000
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 46.60000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 93.20000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 46.60000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 93.20000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 46.60000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 46.60000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -200.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 -64.45000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 111.63067
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 46.60000
REMARK 350 BIOMT1 4 0.500000 0.866025 0.000000 -64.45000
REMARK 350 BIOMT2 4 0.866025 -0.500000 0.000000 111.63067
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 46.60000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 K K A 414 LIES ON A SPECIAL POSITION.
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 ASN A 103
REMARK 465 GLN A 104
REMARK 465 GLY A 105
REMARK 465 VAL A 106
REMARK 465 ASP A 107
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 ILE A 102 CA C O CB CG1 CG2 CD1
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 HIS A 3 NE2 HIS A 3 CD2 -0.068
REMARK 500 HIS A 79 NE2 HIS A 79 CD2 -0.070
REMARK 500 HIS A 142 NE2 HIS A 142 CD2 -0.068
REMARK 500 HIS A 189 NE2 HIS A 189 CD2 -0.075
REMARK 500 HIS A 257 NE2 HIS A 257 CD2 -0.081
REMARK 500 HIS A 348 NE2 HIS A 348 CD2 -0.076
REMARK 500 HIS A 359 NE2 HIS A 359 CD2 -0.068
REMARK 500 HIS A 364 NE2 HIS A 364 CD2 -0.079
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 16 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP A 61 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 61 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP A 159 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 159 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP A 215 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 215 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 THR A 250 N - CA - CB ANGL. DEV. = -14.6 DEGREES
REMARK 500 THR A 250 CA - CB - CG2 ANGL. DEV. = 11.3 DEGREES
REMARK 500 ASP A 271 CB - CG - OD1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG A 336 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 LEU A 340 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 ARG A 362 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 362 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 TRP A 367 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP A 367 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 377 NE - CZ - NH2 ANGL. DEV. = -3.7 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 ALA A 60 158.85 -49.34
REMARK 500 ASP A 118 147.30 71.88
REMARK 500 ILE A 206 -63.22 -102.63
REMARK 500 ASN A 225 56.63 34.28
REMARK 500 ASP A 238 -158.81 -123.66
REMARK 500 LYS A 245 42.50 -89.63
REMARK 500 THR A 250 -90.17 -66.45
REMARK 500 TYR A 251 20.44 -158.13
REMARK 500 GLU A 331 -60.53 -101.57
REMARK 500 ASP A 345 72.21 35.71
REMARK 500 PRO A 349 81.47 -65.13
REMARK 500 TYR A 357 4.14 81.25
REMARK 500 GLU A 363 -24.59 -30.21
REMARK 500 ASP A 378 -70.99 -55.67
REMARK 500 LEU A 382 137.12 -39.18
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 48 MET A 49 -147.39
REMARK 500 ASP A 173 ASP A 174 -121.97
REMARK 500 THR A 227 GLY A 228 -120.16
REMARK 500 GLY A 228 ARG A 229 128.66
REMARK 500 GLY A 259 GLY A 260 -128.05
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 TYR A 140 0.15 SIDE CHAIN
REMARK 500 ARG A 244 0.12 SIDE CHAIN
REMARK 500 TYR A 276 0.08 SIDE CHAIN
REMARK 500 TYR A 280 0.06 SIDE CHAIN
REMARK 500 ARG A 336 0.10 SIDE CHAIN
REMARK 500 TYR A 357 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
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 MG A 412 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 16 OD2
REMARK 620 2 ASP A 16 OD1 55.6
REMARK 620 3 PO4 A 384 O2 97.7 129.9
REMARK 620 4 ADP A 385 O1A 120.3 154.9 73.7
REMARK 620 5 ADP A 385 O3B 63.3 117.1 68.8 58.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 413 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 42 OE1
REMARK 620 2 GLU A 42 OE2 43.0
REMARK 620 3 SER A 263 O 130.0 172.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 414 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 243 O
REMARK 620 2 GLY A 243 O 110.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 411 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 271 OD1
REMARK 620 2 ASP A 271 OD2 56.3
REMARK 620 3 PO4 A 384 O4 113.5 100.6
REMARK 620 4 ADP A 385 O2B 171.5 127.5 74.2
REMARK 620 5 ADP A 385 O2A 123.8 69.1 62.5 62.3
REMARK 620 N 1 2 3 4
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 384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 385
DBREF 1MXB A 1 383 UNP P0A817 METK_ECOLI 2 384
SEQRES 1 A 383 ALA LYS HIS LEU PHE THR SER GLU SER VAL SER GLU GLY
SEQRES 2 A 383 HIS PRO ASP LYS ILE ALA ASP GLN ILE SER ASP ALA VAL
SEQRES 3 A 383 LEU ASP ALA ILE LEU GLU GLN ASP PRO LYS ALA ARG VAL
SEQRES 4 A 383 ALA CYS GLU THR TYR VAL LYS THR GLY MET VAL LEU VAL
SEQRES 5 A 383 GLY GLY GLU ILE THR THR SER ALA TRP VAL ASP ILE GLU
SEQRES 6 A 383 GLU ILE THR ARG ASN THR VAL ARG GLU ILE GLY TYR VAL
SEQRES 7 A 383 HIS SER ASP MET GLY PHE ASP ALA ASN SER CYS ALA VAL
SEQRES 8 A 383 LEU SER ALA ILE GLY LYS GLN SER PRO ASP ILE ASN GLN
SEQRES 9 A 383 GLY VAL ASP ARG ALA ASP PRO LEU GLU GLN GLY ALA GLY
SEQRES 10 A 383 ASP GLN GLY LEU MET PHE GLY TYR ALA THR ASN GLU THR
SEQRES 11 A 383 ASP VAL LEU MET PRO ALA PRO ILE THR TYR ALA HIS ARG
SEQRES 12 A 383 LEU VAL GLN ARG GLN ALA GLU VAL ARG LYS ASN GLY THR
SEQRES 13 A 383 LEU PRO TRP LEU ARG PRO ASP ALA LYS SER GLN VAL THR
SEQRES 14 A 383 PHE GLN TYR ASP ASP GLY LYS ILE VAL GLY ILE ASP ALA
SEQRES 15 A 383 VAL VAL LEU SER THR GLN HIS SER GLU GLU ILE ASP GLN
SEQRES 16 A 383 LYS SER LEU GLN GLU ALA VAL MET GLU GLU ILE ILE LYS
SEQRES 17 A 383 PRO ILE LEU PRO ALA GLU TRP LEU THR SER ALA THR LYS
SEQRES 18 A 383 PHE PHE ILE ASN PRO THR GLY ARG PHE VAL ILE GLY GLY
SEQRES 19 A 383 PRO MET GLY ASP CYS GLY LEU THR GLY ARG LYS ILE ILE
SEQRES 20 A 383 VAL ASP THR TYR GLY GLY MET ALA ARG HIS GLY GLY GLY
SEQRES 21 A 383 ALA PHE SER GLY LYS ASP PRO SER LYS VAL ASP ARG SER
SEQRES 22 A 383 ALA ALA TYR ALA ALA ARG TYR VAL ALA LYS ASN ILE VAL
SEQRES 23 A 383 ALA ALA GLY LEU ALA ASP ARG CYS GLU ILE GLN VAL SER
SEQRES 24 A 383 TYR ALA ILE GLY VAL ALA GLU PRO THR SER ILE MET VAL
SEQRES 25 A 383 GLU THR PHE GLY THR GLU LYS VAL PRO SER GLU GLN LEU
SEQRES 26 A 383 THR LEU LEU VAL ARG GLU PHE PHE ASP LEU ARG PRO TYR
SEQRES 27 A 383 GLY LEU ILE GLN MET LEU ASP LEU LEU HIS PRO ILE TYR
SEQRES 28 A 383 LYS GLU THR ALA ALA TYR GLY HIS PHE GLY ARG GLU HIS
SEQRES 29 A 383 PHE PRO TRP GLU LYS THR ASP LYS ALA GLN LEU LEU ARG
SEQRES 30 A 383 ASP ALA ALA GLY LEU LYS
HET PO4 A 384 5
HET MG A 411 1
HET MG A 412 1
HET K A 413 1
HET K A 414 1
HET ADP A 385 31
HETNAM PO4 PHOSPHATE ION
HETNAM MG MAGNESIUM ION
HETNAM K POTASSIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 2 PO4 O4 P 3-
FORMUL 3 MG 2(MG 2+)
FORMUL 5 K 2(K 1+)
FORMUL 7 ADP C10 H15 N5 O10 P2
HELIX 1 1 PRO A 15 GLN A 33 1 19
HELIX 2 2 ILE A 64 ILE A 75 1 12
HELIX 3 3 SER A 80 MET A 82 5 3
HELIX 4 4 PRO A 111 GLU A 113 5 3
HELIX 5 5 ALA A 136 LYS A 153 1 18
HELIX 6 6 GLN A 195 GLU A 205 1 11
HELIX 7 7 ALA A 213 TRP A 215 5 3
HELIX 8 8 ILE A 246 THR A 250 1 5
HELIX 9 9 VAL A 270 ALA A 287 1 18
HELIX 10 10 SER A 322 PHE A 332 1 11
HELIX 11 11 PRO A 337 MET A 343 1 7
HELIX 12 12 LYS A 352 ALA A 355 5 4
HELIX 13 13 PRO A 366 GLU A 368 5 3
HELIX 14 14 ALA A 373 ALA A 379 1 7
SHEET 1 A 4 HIS A 3 VAL A 10 0
SHEET 2 A 4 ALA A 164 TYR A 172 -1 N TYR A 172 O HIS A 3
SHEET 3 A 4 ALA A 182 THR A 187 -1 N SER A 186 O LYS A 165
SHEET 4 A 4 LYS A 221 ILE A 224 1 N LYS A 221 O VAL A 183
SHEET 1 B 3 ARG A 38 LYS A 46 0
SHEET 2 B 3 MET A 49 THR A 57 -1 N THR A 57 O ARG A 38
SHEET 3 B 3 ALA A 90 GLN A 98 1 N ALA A 90 O VAL A 50
SHEET 1 C 3 GLY A 120 THR A 127 0
SHEET 2 C 3 ARG A 293 TYR A 300 -1 N TYR A 300 O GLY A 120
SHEET 3 C 3 SER A 309 THR A 314 -1 N GLU A 313 O GLU A 295
SHEET 1 D 2 PHE A 170 ASP A 173 0
SHEET 2 D 2 LYS A 176 ILE A 180 -1 N GLY A 179 O GLN A 171
LINK OD2 ASP A 16 MG MG A 412 9555 1555 2.19
LINK OD1 ASP A 16 MG MG A 412 9555 1555 2.22
LINK OE1 GLU A 42 K K A 413 1555 1555 2.65
LINK OE2 GLU A 42 K K A 413 1555 1555 3.00
LINK O GLY A 243 K K A 414 1555 1555 2.51
LINK O GLY A 243 K K A 414 9555 1555 2.52
LINK O SER A 263 K K A 413 1555 1555 2.62
LINK OD1 ASP A 271 MG MG A 411 1555 1555 2.19
LINK OD2 ASP A 271 MG MG A 411 1555 1555 2.15
LINK O4 PO4 A 384 MG MG A 411 1555 1555 2.25
LINK O2 PO4 A 384 MG MG A 412 1555 1555 2.01
LINK O2B ADP A 385 MG MG A 411 1555 1555 2.12
LINK O2A ADP A 385 MG MG A 411 1555 1555 2.99
LINK O1A ADP A 385 MG MG A 412 1555 1555 2.14
LINK O3B ADP A 385 MG MG A 412 1555 1555 2.90
SITE 1 AC1 10 ASP A 16 ARG A 244 LYS A 245 GLY A 260
SITE 2 AC1 10 ALA A 261 LYS A 265 ASP A 271 ADP A 385
SITE 3 AC1 10 MG A 411 MG A 412
SITE 1 AC2 3 ASP A 271 PO4 A 384 ADP A 385
SITE 1 AC3 3 ASP A 16 PO4 A 384 ADP A 385
SITE 1 AC4 3 GLU A 42 SER A 263 LYS A 265
SITE 1 AC5 2 GLY A 243 ILE A 246
SITE 1 AC6 16 HIS A 14 ASP A 16 ARG A 38 ALA A 40
SITE 2 AC6 16 GLU A 55 GLN A 98 ASP A 118 LYS A 165
SITE 3 AC6 16 GLY A 237 LYS A 245 LYS A 265 LYS A 269
SITE 4 AC6 16 ASP A 271 PO4 A 384 MG A 411 MG A 412
CRYST1 128.900 128.900 139.800 90.00 90.00 120.00 P 62 2 2 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 0.007758 0.004479 0.000000 0.00000
SCALE2 0.000000 0.008958 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007153 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
