HEADER LIGASE 03-SEP-01 1JWA
TITLE STRUCTURE OF THE ATP-BOUND MOEB-MOAD PROTEIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MOLYBDOPTERIN BIOSYNTHESIS MOEB PROTEIN;
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: MOLYBDOPTERIN [MPT] CONVERTING FACTOR, SUBUNIT 1;
COMPND 7 CHAIN: D;
COMPND 8 SYNONYM: MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN D;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: MOEB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 12 ORGANISM_TAXID: 562;
SOURCE 13 GENE: MOAD;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS MOEB: MODIFIED ROSSMANN FOLD; MOAD: UBIQUITIN-LIKE FOLD, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.W.LAKE,M.M.WUEBBENS,K.V.RAJAGOPALAN,H.SCHINDELIN
REVDAT 5 07-FEB-24 1JWA 1 REMARK
REVDAT 4 04-OCT-17 1JWA 1 REMARK
REVDAT 3 13-JUL-11 1JWA 1 VERSN
REVDAT 2 24-FEB-09 1JWA 1 VERSN
REVDAT 1 21-NOV-01 1JWA 0
JRNL AUTH M.W.LAKE,M.M.WUEBBENS,K.V.RAJAGOPALAN,H.SCHINDELIN
JRNL TITL MECHANISM OF UBIQUITIN ACTIVATION REVEALED BY THE STRUCTURE
JRNL TITL 2 OF A BACTERIAL MOEB-MOAD COMPLEX.
JRNL REF NATURE V. 414 325 2001
JRNL REFN ISSN 0028-0836
JRNL PMID 11713534
JRNL DOI 10.1038/35104586
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 6696
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.100
REMARK 3 FREE R VALUE TEST SET COUNT : 288
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2237
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
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) : 49.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.24000
REMARK 3 B22 (A**2) : -0.24000
REMARK 3 B33 (A**2) : 0.48000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.019 ; 0.022
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.022 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.551 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.341 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.432 ; 4.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JWA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014258.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7355
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.14300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: DIFFERENCE FOURIER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE, HEPES, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 51.59200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.36150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.36150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 25.79600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.36150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.36150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 77.38800
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.36150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.36150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 25.79600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.36150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.36150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 77.38800
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 51.59200
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 ASYMMETRIC UNIT CONTAINS A HETERODIMER COMPRISED OF (1)
REMARK 300 MOLECULE OF MOEB AND (1) MOLECULE OF MOAD. THE HETEROTETRAMER IS
REMARK 300 GENERATED BY APPLYING: -Y+1,-X+1,1/2-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: 10810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350 BIOMT1 2 0.000000 -1.000000 0.000000 78.72300
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 78.72300
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 51.59200
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B 1
REMARK 465 GLN B 167
REMARK 465 ASP B 168
REMARK 465 GLY B 169
REMARK 465 GLU B 170
REMARK 465 PRO B 171
REMARK 465 CYS B 172
REMARK 465 TYR B 173
REMARK 465 ARG B 174
REMARK 465 CYS B 175
REMARK 465 LEU B 176
REMARK 465 SER B 177
REMARK 465 ARG B 178
REMARK 465 LEU B 179
REMARK 465 PHE B 180
REMARK 465 GLY B 181
REMARK 465 GLU B 182
REMARK 465 ASN B 183
REMARK 465 ALA B 184
REMARK 465 LEU B 185
REMARK 465 THR B 186
REMARK 465 CYS B 187
REMARK 465 VAL B 188
REMARK 465 ASN B 241
REMARK 465 PRO B 242
REMARK 465 GLY B 243
REMARK 465 CYS B 244
REMARK 465 GLU B 245
REMARK 465 VAL B 246
REMARK 465 CYS B 247
REMARK 465 GLY B 248
REMARK 465 GLN B 249
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 B 189 CG CD OE1 OE2
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 96 NH2 ARG B 96 8665 1.87
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 B 62 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 92 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ARG B 96 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP B 123 CB - CG - OD2 ANGL. DEV. = 6.3 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 GLU B 3 91.87 75.06
REMARK 500 PHE B 21 -70.97 -98.53
REMARK 500 ASP B 22 -178.44 56.64
REMARK 500 LEU B 39 48.32 -88.39
REMARK 500 ARG B 73 -25.68 -149.59
REMARK 500 ASN B 107 86.94 -69.50
REMARK 500 ALA B 120 -8.11 -59.99
REMARK 500 ARG B 156 -102.40 55.11
REMARK 500 VAL B 192 117.55 -174.22
REMARK 500 ALA B 219 38.27 -95.14
REMARK 500 LYS D 3 89.50 -67.90
REMARK 500 ALA D 8 -142.88 55.98
REMARK 500 ASP D 24 30.90 178.36
REMARK 500 GLN D 57 -4.66 78.72
REMARK 500 PHE D 62 34.25 -69.60
REMARK 500 HIS D 64 143.83 -33.76
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 ATP B 250
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FMO RELATED DB: PDB
REMARK 900 STRUCTURE OF MOLYBDOPTERIN SYNTHASE (MOAD IN COMPLEX WITH MOAE)
REMARK 900 RELATED ID: 1JW9 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE NATIVE MOEB-MOAD PROTEIN COMPLEX
REMARK 900 RELATED ID: 1JWB RELATED DB: PDB
REMARK 900 STRUCTURE OF THE COVALENT ACYL-ADENYLATE FORM OF THE MOEB-MOAD
REMARK 900 PROTEIN COMPLEX
DBREF 1JWA B 1 249 UNP P12282 MOEB_ECOLI 1 249
DBREF 1JWA D 1 81 UNP P30748 MOAD_ECOLI 1 81
SEQRES 1 B 249 MET ALA GLU LEU SER ASP GLN GLU MET LEU ARG TYR ASN
SEQRES 2 B 249 ARG GLN ILE ILE LEU ARG GLY PHE ASP PHE ASP GLY GLN
SEQRES 3 B 249 GLU ALA LEU LYS ASP SER ARG VAL LEU ILE VAL GLY LEU
SEQRES 4 B 249 GLY GLY LEU GLY CYS ALA ALA SER GLN TYR LEU ALA SER
SEQRES 5 B 249 ALA GLY VAL GLY ASN LEU THR LEU LEU ASP PHE ASP THR
SEQRES 6 B 249 VAL SER LEU SER ASN LEU GLN ARG GLN THR LEU HIS SER
SEQRES 7 B 249 ASP ALA THR VAL GLY GLN PRO LYS VAL GLU SER ALA ARG
SEQRES 8 B 249 ASP ALA LEU THR ARG ILE ASN PRO HIS ILE ALA ILE THR
SEQRES 9 B 249 PRO VAL ASN ALA LEU LEU ASP ASP ALA GLU LEU ALA ALA
SEQRES 10 B 249 LEU ILE ALA GLU HIS ASP LEU VAL LEU ASP CYS THR ASP
SEQRES 11 B 249 ASN VAL ALA VAL ARG ASN GLN LEU ASN ALA GLY CYS PHE
SEQRES 12 B 249 ALA ALA LYS VAL PRO LEU VAL SER GLY ALA ALA ILE ARG
SEQRES 13 B 249 MET GLU GLY GLN ILE THR VAL PHE THR TYR GLN ASP GLY
SEQRES 14 B 249 GLU PRO CYS TYR ARG CYS LEU SER ARG LEU PHE GLY GLU
SEQRES 15 B 249 ASN ALA LEU THR CYS VAL GLU ALA GLY VAL MET ALA PRO
SEQRES 16 B 249 LEU ILE GLY VAL ILE GLY SER LEU GLN ALA MET GLU ALA
SEQRES 17 B 249 ILE LYS MET LEU ALA GLY TYR GLY LYS PRO ALA SER GLY
SEQRES 18 B 249 LYS ILE VAL MET TYR ASP ALA MET THR CYS GLN PHE ARG
SEQRES 19 B 249 GLU MET LYS LEU MET ARG ASN PRO GLY CYS GLU VAL CYS
SEQRES 20 B 249 GLY GLN
SEQRES 1 D 81 MET ILE LYS VAL LEU PHE PHE ALA GLN VAL ARG GLU LEU
SEQRES 2 D 81 VAL GLY THR ASP ALA THR GLU VAL ALA ALA ASP PHE PRO
SEQRES 3 D 81 THR VAL GLU ALA LEU ARG GLN HIS MET ALA ALA GLN SER
SEQRES 4 D 81 ASP ARG TRP ALA LEU ALA LEU GLU ASP GLY LYS LEU LEU
SEQRES 5 D 81 ALA ALA VAL ASN GLN THR LEU VAL SER PHE ASP HIS PRO
SEQRES 6 D 81 LEU THR ASP GLY ASP GLU VAL ALA PHE PHE PRO PRO VAL
SEQRES 7 D 81 THR GLY GLY
HET ATP B 250 31
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 ATP C10 H16 N5 O13 P3
HELIX 1 1 SER B 5 TYR B 12 1 8
HELIX 2 2 TYR B 12 ILE B 17 1 6
HELIX 3 3 PHE B 21 ASP B 31 1 11
HELIX 4 4 GLY B 40 GLY B 54 1 15
HELIX 5 5 LEU B 68 ARG B 73 5 6
HELIX 6 6 SER B 78 VAL B 82 5 5
HELIX 7 7 PRO B 85 ASN B 98 1 14
HELIX 8 8 ASP B 111 ALA B 120 1 10
HELIX 9 9 ASN B 131 LYS B 146 1 16
HELIX 10 10 MET B 193 GLY B 214 1 22
HELIX 11 11 PHE D 7 GLY D 15 1 9
HELIX 12 12 THR D 27 ALA D 37 1 11
HELIX 13 13 SER D 39 LEU D 46 1 8
SHEET 1 A 8 ALA B 102 ASN B 107 0
SHEET 2 A 8 ASN B 57 ASP B 62 1 N LEU B 58 O THR B 104
SHEET 3 A 8 ARG B 33 VAL B 37 1 N ILE B 36 O THR B 59
SHEET 4 A 8 LEU B 124 ASP B 127 1 O LEU B 126 N LEU B 35
SHEET 5 A 8 LEU B 149 ILE B 155 1 O VAL B 150 N VAL B 125
SHEET 6 A 8 GLU B 158 PHE B 164 -1 O THR B 162 N SER B 151
SHEET 7 A 8 LYS B 222 ASP B 227 -1 O TYR B 226 N GLY B 159
SHEET 8 A 8 GLN B 232 LYS B 237 -1 O GLN B 232 N ASP B 227
SHEET 1 B 5 ALA D 18 GLU D 20 0
SHEET 2 B 5 LYS D 3 PHE D 6 -1 N VAL D 4 O THR D 19
SHEET 3 B 5 GLU D 71 PHE D 75 1 O PHE D 74 N LEU D 5
SHEET 4 B 5 LEU D 52 VAL D 55 -1 N ALA D 54 O ALA D 73
SHEET 5 B 5 THR D 58 LEU D 59 -1 O THR D 58 N VAL D 55
SITE 1 AC1 17 ARG B 14 GLY B 40 GLY B 41 LEU B 61
SITE 2 AC1 17 ASP B 62 PHE B 63 ASP B 64 SER B 69
SITE 3 AC1 17 ASN B 70 ARG B 73 GLN B 74 LYS B 86
SITE 4 AC1 17 LEU B 109 ASP B 130 ASN B 131 VAL B 134
SITE 5 AC1 17 GLY D 81
CRYST1 78.723 78.723 103.184 90.00 90.00 90.00 P 41 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 0.012703 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012703 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009691 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
