HEADER TRANSFERASE 25-OCT-02 1N3B
TITLE CRYSTAL STRUCTURE OF DEPHOSPHOCOENZYME A KINASE FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEPHOSPHO-COA KINASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: DEPHOSPHOCOENZYME A KINASE;
COMPND 5 EC: 2.7.1.24;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: COAE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DL41(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET20B DERIVATIVE
KEYWDS TRIMER, P-LOOP, ALPHA/BETA, MONTREAL-KINGSTON BACTERIAL STRUCTURAL
KEYWDS 2 GENOMICS INITIATIVE, BSGI, STRUCTURAL GENOMICS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.O'TOOLE,J.A.R.G.BARBOSA,Y.LI,L.-W.HUNG,A.MATTE,M.CYGLER,MONTREAL-
AUTHOR 2 KINGSTON BACTERIAL STRUCTURAL GENOMICS INITIATIVE (BSGI)
REVDAT 4 01-FEB-17 1N3B 1 AUTHOR
REVDAT 3 16-APR-14 1N3B 1 REMARK VERSN
REVDAT 2 24-FEB-09 1N3B 1 VERSN
REVDAT 1 28-JAN-03 1N3B 0
JRNL AUTH N.O'TOOLE,J.A.R.G.BARBOSA,Y.LI,L.-W.HUNG,A.MATTE,M.CYGLER
JRNL TITL CRYSTAL STRUCTURE OF A TRIMERIC FORM OF DEPHOSPHOCOENZYME A
JRNL TITL 2 KINASE FROM ESCHERICHIA COLI
JRNL REF PROTEIN SCI. V. 12 327 2003
JRNL REFN ISSN 0961-8368
JRNL PMID 12538896
JRNL DOI 10.1110/PS.0227803
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.OBLOMOVA,A.TEPLYAKOV,N.BONANDER,E.EISENSTEIN,A.HOWARD,
REMARK 1 AUTH 2 G.GILLILAND
REMARK 1 TITL CRYSTAL STRUCTURE OF DEPHOSPHO-COENZYME A KINASE FROM
REMARK 1 TITL 2 HAEMOPHILUS INFLUENZAE
REMARK 1 REF J.STRUCT.BIOL. V. 136 119 2001
REMARK 1 REFN ISSN 1047-8477
REMARK 1 DOI 10.1006/JSBI.2001.4428
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.K.MISHRA,P.K.PARK,D.G.DRUECKHAMMER
REMARK 1 TITL IDENTIFICATION OF YACE (COAE) AS THE STRUCTURAL GENE FOR
REMARK 1 TITL 2 DEPHOSPHOCOENZYME A KINASE IN ESCHERICHIA COLI K-12
REMARK 1 REF J.BACTERIOL. V. 183 2774 2001
REMARK 1 REFN ISSN 0021-9193
REMARK 1 DOI 10.1128/JB.183.9.2774-2778.2001
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.VORHEIN,H.BONISCH,G.SCHAFER,G.E.SCHULZ
REMARK 1 TITL THE STRUCTURE OF A TRIMERIC ARCHAEL ADENYLATE KINASE
REMARK 1 REF J.MOL.BIOL. V. 282 167 1998
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1998.2003
REMARK 1 REFERENCE 4
REMARK 1 AUTH D.M.WORRAL,P.K.TUBBS
REMARK 1 TITL A BIFUNCTIONAL ENZYME COMPLEX IN COENZYME A BIOSYNTHESIS:
REMARK 1 TITL 2 PURIFICATION OF PANTETHEINE PHOSPHATE ADENYLYLTRANSFERASE
REMARK 1 TITL 3 AND DEPHOSPHO-COA KINASE
REMARK 1 REF BIOCHEM.J. V. 215 153 1983
REMARK 1 REFN ISSN 0264-6021
REMARK 1 REFERENCE 5
REMARK 1 AUTH S.AGHAJANIAN,D.M.WORRAL
REMARK 1 TITL IDENTIFICATION AND CHARACTERIZATION OF THE GENE ENCODING THE
REMARK 1 TITL 2 HUMAN ADENYLYLTRANSFERASE AND DEPHOSPHOCOENZYME A KINASE
REMARK 1 TITL 3 BIFUNCTIONAL ENZYME
REMARK 1 REF BIOCHEM.J. V. 365 13 2002
REMARK 1 REFN ISSN 0264-6021
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
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) (%) : 86.8
REMARK 3 NUMBER OF REFLECTIONS : 107923
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE-R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.400
REMARK 3 FREE R VALUE TEST SET COUNT : 5518
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 : 4547
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 449
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.46
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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.260
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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:
REMARK 3 BULK SOLVENT CORRECTION EMPLOYED.
REMARK 3 THE STRUCTURE WAS REFINED USING FRIEDEL'S PAIRS.
REMARK 4
REMARK 4 1N3B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-02.
REMARK 100 THE RCSB ID CODE IS RCSB017465.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97957, 0.97941
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MONOCHROMATING CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59512
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.3
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.43900
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CACODYLATE BUFFER, AMMONIUM
REMARK 280 SULFATE, GLYCEROL, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 41.20500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -165.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 ILE A 50
REMARK 465 ALA A 51
REMARK 465 ASP A 52
REMARK 465 HIS A 53
REMARK 465 PHE A 54
REMARK 465 GLY A 55
REMARK 465 ALA A 56
REMARK 465 ASN A 57
REMARK 465 MSE A 58
REMARK 465 ILE A 59
REMARK 465 ALA A 60
REMARK 465 ALA A 61
REMARK 465 ASP A 62
REMARK 465 GLY A 63
REMARK 465 THR A 64
REMARK 465 LEU A 65
REMARK 465 GLN A 66
REMARK 465 ARG A 67
REMARK 465 ARG A 68
REMARK 465 ALA A 69
REMARK 465 LEU A 70
REMARK 465 ARG A 71
REMARK 465 GLU A 72
REMARK 465 ARG A 73
REMARK 465 ILE A 74
REMARK 465 PHE A 75
REMARK 465 ALA A 76
REMARK 465 ASN A 77
REMARK 465 LYS A 205
REMARK 465 PRO A 206
REMARK 465 GLY A 207
REMARK 465 SER A 208
REMARK 465 HIS A 209
REMARK 465 HIS A 210
REMARK 465 HIS A 211
REMARK 465 HIS A 212
REMARK 465 HIS A 213
REMARK 465 HIS A 214
REMARK 465 HIS A 215
REMARK 465 HIS A 216
REMARK 465 GLY B 207
REMARK 465 SER B 208
REMARK 465 HIS B 209
REMARK 465 HIS B 210
REMARK 465 HIS B 211
REMARK 465 HIS B 212
REMARK 465 HIS B 213
REMARK 465 HIS B 214
REMARK 465 HIS B 215
REMARK 465 HIS B 216
REMARK 465 GLY C 207
REMARK 465 SER C 208
REMARK 465 HIS C 209
REMARK 465 HIS C 210
REMARK 465 HIS C 211
REMARK 465 HIS C 212
REMARK 465 HIS C 213
REMARK 465 HIS C 214
REMARK 465 HIS C 215
REMARK 465 HIS C 216
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 O HOH B 627 O HOH B 657 2.11
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 A 79 -69.14 73.83
REMARK 500 ASP A 146 70.93 43.06
REMARK 500 ALA B 76 -39.57 75.06
REMARK 500 LEU B 114 30.19 -96.92
REMARK 500 ASN C 77 70.71 168.87
REMARK 500 ASP C 145 -119.83 -137.35
REMARK 500 ASP C 146 -156.64 -155.50
REMARK 500 VAL C 147 65.82 38.57
REMARK 500 THR C 148 -135.48 11.90
REMARK 500 HIS C 151 -54.99 69.94
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 SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 510
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: COAE_ECOLI RELATED DB: TARGETDB
DBREF 1N3B A 1 206 UNP P0A6I9 COAE_ECOLI 1 206
DBREF 1N3B B 1 206 UNP P0A6I9 COAE_ECOLI 1 206
DBREF 1N3B C 1 206 UNP P0A6I9 COAE_ECOLI 1 206
SEQADV 1N3B MSE A 1 UNP P0A6I9 MET 1 MODIFIED RESIDUE
SEQADV 1N3B MSE A 58 UNP P0A6I9 MET 58 MODIFIED RESIDUE
SEQADV 1N3B MSE A 142 UNP P0A6I9 MET 142 MODIFIED RESIDUE
SEQADV 1N3B GLY A 207 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B SER A 208 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS A 209 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS A 210 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS A 211 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS A 212 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS A 213 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS A 214 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS A 215 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS A 216 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B MSE B 1 UNP P0A6I9 MET 1 MODIFIED RESIDUE
SEQADV 1N3B MSE B 58 UNP P0A6I9 MET 58 MODIFIED RESIDUE
SEQADV 1N3B MSE B 142 UNP P0A6I9 MET 142 MODIFIED RESIDUE
SEQADV 1N3B GLY B 207 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B SER B 208 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS B 209 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS B 210 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS B 211 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS B 212 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS B 213 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS B 214 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS B 215 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS B 216 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B MSE C 1 UNP P0A6I9 MET 1 MODIFIED RESIDUE
SEQADV 1N3B MSE C 58 UNP P0A6I9 MET 58 MODIFIED RESIDUE
SEQADV 1N3B MSE C 142 UNP P0A6I9 MET 142 MODIFIED RESIDUE
SEQADV 1N3B GLY C 207 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B SER C 208 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS C 209 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS C 210 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS C 211 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS C 212 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS C 213 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS C 214 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS C 215 UNP P0A6I9 EXPRESSION TAG
SEQADV 1N3B HIS C 216 UNP P0A6I9 EXPRESSION TAG
SEQRES 1 A 216 MSE ARG TYR ILE VAL ALA LEU THR GLY GLY ILE GLY SER
SEQRES 2 A 216 GLY LYS SER THR VAL ALA ASN ALA PHE ALA ASP LEU GLY
SEQRES 3 A 216 ILE ASN VAL ILE ASP ALA ASP ILE ILE ALA ARG GLN VAL
SEQRES 4 A 216 VAL GLU PRO GLY ALA PRO ALA LEU HIS ALA ILE ALA ASP
SEQRES 5 A 216 HIS PHE GLY ALA ASN MSE ILE ALA ALA ASP GLY THR LEU
SEQRES 6 A 216 GLN ARG ARG ALA LEU ARG GLU ARG ILE PHE ALA ASN PRO
SEQRES 7 A 216 GLU GLU LYS ASN TRP LEU ASN ALA LEU LEU HIS PRO LEU
SEQRES 8 A 216 ILE GLN GLN GLU THR GLN HIS GLN ILE GLN GLN ALA THR
SEQRES 9 A 216 SER PRO TYR VAL LEU TRP VAL VAL PRO LEU LEU VAL GLU
SEQRES 10 A 216 ASN SER LEU TYR LYS LYS ALA ASN ARG VAL LEU VAL VAL
SEQRES 11 A 216 ASP VAL SER PRO GLU THR GLN LEU LYS ARG THR MSE GLN
SEQRES 12 A 216 ARG ASP ASP VAL THR ARG GLU HIS VAL GLU GLN ILE LEU
SEQRES 13 A 216 ALA ALA GLN ALA THR ARG GLU ALA ARG LEU ALA VAL ALA
SEQRES 14 A 216 ASP ASP VAL ILE ASP ASN ASN GLY ALA PRO ASP ALA ILE
SEQRES 15 A 216 ALA SER ASP VAL ALA ARG LEU HIS ALA HIS TYR LEU GLN
SEQRES 16 A 216 LEU ALA SER GLN PHE VAL SER GLN GLU LYS PRO GLY SER
SEQRES 17 A 216 HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 216 MSE ARG TYR ILE VAL ALA LEU THR GLY GLY ILE GLY SER
SEQRES 2 B 216 GLY LYS SER THR VAL ALA ASN ALA PHE ALA ASP LEU GLY
SEQRES 3 B 216 ILE ASN VAL ILE ASP ALA ASP ILE ILE ALA ARG GLN VAL
SEQRES 4 B 216 VAL GLU PRO GLY ALA PRO ALA LEU HIS ALA ILE ALA ASP
SEQRES 5 B 216 HIS PHE GLY ALA ASN MSE ILE ALA ALA ASP GLY THR LEU
SEQRES 6 B 216 GLN ARG ARG ALA LEU ARG GLU ARG ILE PHE ALA ASN PRO
SEQRES 7 B 216 GLU GLU LYS ASN TRP LEU ASN ALA LEU LEU HIS PRO LEU
SEQRES 8 B 216 ILE GLN GLN GLU THR GLN HIS GLN ILE GLN GLN ALA THR
SEQRES 9 B 216 SER PRO TYR VAL LEU TRP VAL VAL PRO LEU LEU VAL GLU
SEQRES 10 B 216 ASN SER LEU TYR LYS LYS ALA ASN ARG VAL LEU VAL VAL
SEQRES 11 B 216 ASP VAL SER PRO GLU THR GLN LEU LYS ARG THR MSE GLN
SEQRES 12 B 216 ARG ASP ASP VAL THR ARG GLU HIS VAL GLU GLN ILE LEU
SEQRES 13 B 216 ALA ALA GLN ALA THR ARG GLU ALA ARG LEU ALA VAL ALA
SEQRES 14 B 216 ASP ASP VAL ILE ASP ASN ASN GLY ALA PRO ASP ALA ILE
SEQRES 15 B 216 ALA SER ASP VAL ALA ARG LEU HIS ALA HIS TYR LEU GLN
SEQRES 16 B 216 LEU ALA SER GLN PHE VAL SER GLN GLU LYS PRO GLY SER
SEQRES 17 B 216 HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 216 MSE ARG TYR ILE VAL ALA LEU THR GLY GLY ILE GLY SER
SEQRES 2 C 216 GLY LYS SER THR VAL ALA ASN ALA PHE ALA ASP LEU GLY
SEQRES 3 C 216 ILE ASN VAL ILE ASP ALA ASP ILE ILE ALA ARG GLN VAL
SEQRES 4 C 216 VAL GLU PRO GLY ALA PRO ALA LEU HIS ALA ILE ALA ASP
SEQRES 5 C 216 HIS PHE GLY ALA ASN MSE ILE ALA ALA ASP GLY THR LEU
SEQRES 6 C 216 GLN ARG ARG ALA LEU ARG GLU ARG ILE PHE ALA ASN PRO
SEQRES 7 C 216 GLU GLU LYS ASN TRP LEU ASN ALA LEU LEU HIS PRO LEU
SEQRES 8 C 216 ILE GLN GLN GLU THR GLN HIS GLN ILE GLN GLN ALA THR
SEQRES 9 C 216 SER PRO TYR VAL LEU TRP VAL VAL PRO LEU LEU VAL GLU
SEQRES 10 C 216 ASN SER LEU TYR LYS LYS ALA ASN ARG VAL LEU VAL VAL
SEQRES 11 C 216 ASP VAL SER PRO GLU THR GLN LEU LYS ARG THR MSE GLN
SEQRES 12 C 216 ARG ASP ASP VAL THR ARG GLU HIS VAL GLU GLN ILE LEU
SEQRES 13 C 216 ALA ALA GLN ALA THR ARG GLU ALA ARG LEU ALA VAL ALA
SEQRES 14 C 216 ASP ASP VAL ILE ASP ASN ASN GLY ALA PRO ASP ALA ILE
SEQRES 15 C 216 ALA SER ASP VAL ALA ARG LEU HIS ALA HIS TYR LEU GLN
SEQRES 16 C 216 LEU ALA SER GLN PHE VAL SER GLN GLU LYS PRO GLY SER
SEQRES 17 C 216 HIS HIS HIS HIS HIS HIS HIS HIS
MODRES 1N3B MSE A 1 MET SELENOMETHIONINE
MODRES 1N3B MSE A 142 MET SELENOMETHIONINE
MODRES 1N3B MSE B 1 MET SELENOMETHIONINE
MODRES 1N3B MSE B 58 MET SELENOMETHIONINE
MODRES 1N3B MSE B 142 MET SELENOMETHIONINE
MODRES 1N3B MSE C 1 MET SELENOMETHIONINE
MODRES 1N3B MSE C 58 MET SELENOMETHIONINE
MODRES 1N3B MSE C 142 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 142 8
HET MSE B 1 8
HET MSE B 58 8
HET MSE B 142 8
HET MSE C 1 8
HET MSE C 58 8
HET MSE C 142 8
HET SO4 A 501 5
HET SO4 B 502 5
HET SO4 C 503 5
HET SO4 C 504 5
HET SO4 A 505 5
HET SO4 B 506 5
HET SO4 C 507 5
HET SO4 C 508 5
HET SO4 B 509 5
HET SO4 A 510 5
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 4 SO4 10(O4 S 2-)
FORMUL 14 HOH *449(H2 O)
HELIX 1 1 GLY A 14 LEU A 25 1 12
HELIX 2 2 ALA A 32 VAL A 39 1 8
HELIX 3 3 ALA A 44 ALA A 49 1 6
HELIX 4 4 GLU A 79 ALA A 103 1 25
HELIX 5 5 SER A 119 ALA A 124 5 6
HELIX 6 6 SER A 133 ASP A 146 1 14
HELIX 7 7 THR A 148 GLN A 159 1 12
HELIX 8 8 THR A 161 ALA A 169 1 9
HELIX 9 9 ALA A 178 ALA A 181 5 4
HELIX 10 10 ILE A 182 PHE A 200 1 19
HELIX 11 11 GLY B 14 LEU B 25 1 12
HELIX 12 12 ALA B 32 VAL B 39 1 8
HELIX 13 13 ALA B 44 GLY B 55 1 12
HELIX 14 14 ALA B 56 ILE B 59 5 4
HELIX 15 15 GLN B 66 PHE B 75 1 10
HELIX 16 16 ASN B 77 ALA B 103 1 27
HELIX 17 17 SER B 119 ALA B 124 5 6
HELIX 18 18 SER B 133 ASP B 145 1 13
HELIX 19 19 THR B 148 GLN B 159 1 12
HELIX 20 20 THR B 161 ALA B 169 1 9
HELIX 21 21 ALA B 178 ALA B 181 5 4
HELIX 22 22 ILE B 182 PHE B 200 1 19
HELIX 23 23 GLY C 14 ASP C 24 1 11
HELIX 24 24 ALA C 32 VAL C 39 1 8
HELIX 25 25 ALA C 44 GLY C 55 1 12
HELIX 26 26 ALA C 56 ILE C 59 5 4
HELIX 27 27 GLN C 66 ALA C 76 1 11
HELIX 28 28 ASN C 77 ALA C 103 1 27
HELIX 29 29 SER C 119 ALA C 124 5 6
HELIX 30 30 SER C 133 ASP C 145 1 13
HELIX 31 31 HIS C 151 GLN C 159 1 9
HELIX 32 32 THR C 161 ALA C 169 1 9
HELIX 33 33 ALA C 181 PHE C 200 1 20
SHEET 1 A 5 ASN A 28 ASP A 31 0
SHEET 2 A 5 TYR A 107 VAL A 111 1 O LEU A 109 N ILE A 30
SHEET 3 A 5 TYR A 3 THR A 8 1 N LEU A 7 O TRP A 110
SHEET 4 A 5 ARG A 126 ASP A 131 1 O LEU A 128 N ALA A 6
SHEET 5 A 5 ASP A 171 ASP A 174 1 O ILE A 173 N ASP A 131
SHEET 1 B 5 ASN B 28 ASP B 31 0
SHEET 2 B 5 TYR B 107 VAL B 111 1 O LEU B 109 N ILE B 30
SHEET 3 B 5 TYR B 3 THR B 8 1 N LEU B 7 O TRP B 110
SHEET 4 B 5 ARG B 126 ASP B 131 1 O LEU B 128 N ALA B 6
SHEET 5 B 5 ASP B 171 ASP B 174 1 O ILE B 173 N ASP B 131
SHEET 1 C 5 ASN C 28 ASP C 31 0
SHEET 2 C 5 TYR C 107 VAL C 111 1 O LEU C 109 N ILE C 30
SHEET 3 C 5 TYR C 3 THR C 8 1 N VAL C 5 O TRP C 110
SHEET 4 C 5 ARG C 126 ASP C 131 1 O LEU C 128 N ALA C 6
SHEET 5 C 5 ASP C 171 ASP C 174 1 O ILE C 173 N VAL C 129
LINK C MSE A 1 N ARG A 2 1555 1555 1.33
LINK C THR A 141 N MSE A 142 1555 1555 1.33
LINK C MSE A 142 N GLN A 143 1555 1555 1.33
LINK C MSE B 1 N ARG B 2 1555 1555 1.33
LINK C ASN B 57 N MSE B 58 1555 1555 1.34
LINK C MSE B 58 N ILE B 59 1555 1555 1.33
LINK C THR B 141 N MSE B 142 1555 1555 1.33
LINK C MSE B 142 N GLN B 143 1555 1555 1.33
LINK C MSE C 1 N ARG C 2 1555 1555 1.33
LINK C ASN C 57 N MSE C 58 1555 1555 1.33
LINK C MSE C 58 N ILE C 59 1555 1555 1.33
LINK C THR C 141 N MSE C 142 1555 1555 1.33
LINK C MSE C 142 N GLN C 143 1555 1555 1.33
CISPEP 1 ALA C 178 PRO C 179 0 0.35
SITE 1 AC1 8 ILE A 11 GLY A 12 SER A 13 GLY A 14
SITE 2 AC1 8 LYS A 15 ARG A 144 HOH A 528 HOH A 604
SITE 1 AC2 8 ILE B 11 GLY B 12 SER B 13 GLY B 14
SITE 2 AC2 8 LYS B 15 ARG B 144 HOH B 563 HOH B 587
SITE 1 AC3 6 GLY C 12 SER C 13 GLY C 14 LYS C 15
SITE 2 AC3 6 ARG C 144 HOH C 596
SITE 1 AC4 10 SER A 119 TYR A 121 LYS A 122 SER B 119
SITE 2 AC4 10 TYR B 121 LYS B 122 HOH B 554 SER C 119
SITE 3 AC4 10 TYR C 121 LYS C 122
SITE 1 AC5 3 ARG A 126 HIS A 192 HOH A 576
SITE 1 AC6 2 ARG B 126 HIS B 192
SITE 1 AC7 3 ARG C 126 HIS C 192 HOH C 653
SITE 1 AC8 5 HOH B 680 GLN C 93 THR C 96 GLN C 97
SITE 2 AC8 5 TRP C 110
SITE 1 AC9 4 ALA A 157 GLN B 93 GLN B 97 TRP B 110
SITE 1 BC1 6 GLN A 93 THR A 96 GLN A 97 TRP A 110
SITE 2 BC1 6 LYS A 123 HOH C 650
CRYST1 55.500 82.410 76.000 90.00 94.77 90.00 P 1 21 1 6
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 0.018018 0.000000 0.001504 0.00000
SCALE2 0.000000 0.012134 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013204 0.00000
HETATM 1 N MSE A 1 15.279 50.586 45.803 1.00 46.10 N
HETATM 2 CA MSE A 1 15.268 49.091 45.836 1.00 46.36 C
HETATM 3 C MSE A 1 14.501 48.547 44.656 1.00 42.93 C
HETATM 4 O MSE A 1 13.650 49.239 44.087 1.00 43.92 O
HETATM 5 CB MSE A 1 14.583 48.579 47.089 1.00 51.37 C
HETATM 6 CG MSE A 1 15.160 49.063 48.379 1.00 58.22 C
HETATM 7 SE MSE A 1 14.135 48.235 49.752 1.00 68.21 SE
HETATM 8 CE MSE A 1 15.133 46.578 49.871 1.00 63.53 C
(ATOM LINES ARE NOT SHOWN.)
END