HEADER TRANSFERASE 19-SEP-06 2IF2
TITLE CRYSTAL STRUCTURE OF THE PUTATIVE DEPHOSPHO-COA KINASE FROM AQUIFEX
TITLE 2 AEOLICUS, NORTHEAST STRUCTURAL GENOMICS TARGET QR72.
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: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 224324;
SOURCE 4 STRAIN: VF5;
SOURCE 5 GENE: COAE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21,JM109
KEYWDS ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FOROUHAR,M.HUSSAIN,J.SEETHARAMAN,A.HUSSAIN,M.WU,Y.FANG,
AUTHOR 2 K.CUNNINGHAM,L.C.MA,R.XIAO,J.LIU,M.BARAN,B.ROST,T.B.ACTON,
AUTHOR 3 G.T.MONTELIONE,J.F.HUNT,L.TONG,NORTHEAST STRUCTURAL GENOMICS
AUTHOR 4 CONSORTIUM (NESG)
REVDAT 3 13-JUL-11 2IF2 1 VERSN
REVDAT 2 24-FEB-09 2IF2 1 VERSN
REVDAT 1 03-OCT-06 2IF2 0
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, XTALVIEW
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 78145.850
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.2
REMARK 3 NUMBER OF REFLECTIONS : 28597
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700
REMARK 3 FREE R VALUE TEST SET COUNT : 2780
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3068
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE : 0.3960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 358
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4541
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 7
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 68.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 23.68000
REMARK 3 B22 (A**2) : -29.21000
REMARK 3 B33 (A**2) : 5.54000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.51
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.50
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.68
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.73
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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 : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 20.98
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2IF2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-06.
REMARK 100 THE RCSB ID CODE IS RCSB039502.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.15
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32628
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 37.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.65300
REMARK 200 R SYM FOR SHELL (I) : 0.44500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 57.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM CACODYLATE, 30% PEG8K, 210MM
REMARK 280 AMMONIUM SULFATE, AND 5MM DTT., PH 6.15, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 35.81600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.81250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.50650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.81250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.81600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.50650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ASP A 195
REMARK 465 PRO A 196
REMARK 465 LEU A 197
REMARK 465 GLU A 198
REMARK 465 HIS A 199
REMARK 465 HIS A 200
REMARK 465 HIS A 201
REMARK 465 HIS A 202
REMARK 465 HIS A 203
REMARK 465 HIS A 204
REMARK 465 ASP B 195
REMARK 465 PRO B 196
REMARK 465 LEU B 197
REMARK 465 GLU B 198
REMARK 465 HIS B 199
REMARK 465 HIS B 200
REMARK 465 HIS B 201
REMARK 465 HIS B 202
REMARK 465 HIS B 203
REMARK 465 HIS B 204
REMARK 465 LYS C 51
REMARK 465 THR C 52
REMARK 465 PHE C 53
REMARK 465 GLY C 54
REMARK 465 LYS C 55
REMARK 465 GLY C 56
REMARK 465 ILE C 57
REMARK 465 LEU C 58
REMARK 465 ASP C 59
REMARK 465 GLU C 60
REMARK 465 GLU C 61
REMARK 465 GLY C 62
REMARK 465 ASN C 63
REMARK 465 ILE C 64
REMARK 465 ASP C 65
REMARK 465 ARG C 66
REMARK 465 LYS C 67
REMARK 465 LYS C 68
REMARK 465 LEU C 69
REMARK 465 ALA C 70
REMARK 465 ASP C 71
REMARK 465 ILE C 72
REMARK 465 VAL C 73
REMARK 465 PHE C 74
REMARK 465 LYS C 75
REMARK 465 ASP C 76
REMARK 465 GLU C 77
REMARK 465 GLU C 78
REMARK 465 LYS C 79
REMARK 465 LEU C 80
REMARK 465 ARG C 81
REMARK 465 ASP C 195
REMARK 465 PRO C 196
REMARK 465 LEU C 197
REMARK 465 GLU C 198
REMARK 465 HIS C 199
REMARK 465 HIS C 200
REMARK 465 HIS C 201
REMARK 465 HIS C 202
REMARK 465 HIS C 203
REMARK 465 HIS C 204
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 ARG A 40 -81.61 -70.61
REMARK 500 LYS A 41 -83.30 -164.92
REMARK 500 LYS A 55 -11.19 -40.01
REMARK 500 GLU A 61 90.16 46.70
REMARK 500 ASN A 63 -163.78 -104.29
REMARK 500 ILE A 72 14.91 -65.01
REMARK 500 LYS A 75 -61.67 -95.36
REMARK 500 GLU A 77 4.91 -62.95
REMARK 500 THR A 87 -70.05 -57.51
REMARK 500 ASP A 105 -1.16 61.21
REMARK 500 SER A 113 -0.54 61.36
REMARK 500 VAL A 116 -76.42 -92.25
REMARK 500 ASP A 125 -82.11 -39.11
REMARK 500 ALA A 132 120.64 -176.15
REMARK 500 MSE A 146 -2.58 -169.53
REMARK 500 SER A 147 129.98 69.24
REMARK 500 LYS A 166 22.08 -78.99
REMARK 500 LYS B 2 91.31 88.30
REMARK 500 ARG B 40 -92.44 -58.25
REMARK 500 LYS B 41 -62.98 -178.95
REMARK 500 THR B 52 -36.66 -137.36
REMARK 500 LYS B 55 65.07 -119.93
REMARK 500 ASP B 59 105.83 -163.16
REMARK 500 GLU B 61 33.76 37.13
REMARK 500 LYS B 75 20.54 -78.53
REMARK 500 ASP B 76 102.59 -173.21
REMARK 500 THR B 106 136.55 -26.18
REMARK 500 LEU B 114 25.04 -74.67
REMARK 500 ALA B 132 106.04 177.33
REMARK 500 GLU B 139 -71.21 -52.02
REMARK 500 GLU C 23 -18.98 -46.19
REMARK 500 TYR C 39 71.72 -119.15
REMARK 500 ARG C 40 -84.98 -134.15
REMARK 500 LYS C 41 41.90 -143.35
REMARK 500 VAL C 45 25.46 -76.36
REMARK 500 VAL C 49 -44.51 -131.94
REMARK 500 HIS C 88 11.79 -69.14
REMARK 500 TYR C 92 -17.09 -47.41
REMARK 500 GLU C 104 9.61 48.23
REMARK 500 THR C 106 -124.13 -112.75
REMARK 500 THR C 120 31.51 -72.42
REMARK 500 ASN C 123 -3.08 -59.89
REMARK 500 MSE C 146 -10.88 -163.27
REMARK 500 GLU C 148 -0.78 61.05
REMARK 500 PRO C 160 136.60 -38.42
REMARK 500 LEU C 192 -4.82 -166.41
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 B 124 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 SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: QR72 RELATED DB: TARGETDB
DBREF 2IF2 A 1 196 UNP O67792 COAE_AQUAE 1 196
DBREF 2IF2 B 1 196 UNP O67792 COAE_AQUAE 1 196
DBREF 2IF2 C 1 196 UNP O67792 COAE_AQUAE 1 196
SEQADV 2IF2 MSE A 1 UNP O67792 MET 1 MODIFIED RESIDUE
SEQADV 2IF2 MSE A 20 UNP O67792 MET 20 MODIFIED RESIDUE
SEQADV 2IF2 MSE A 146 UNP O67792 MET 146 MODIFIED RESIDUE
SEQADV 2IF2 MSE A 159 UNP O67792 MET 159 MODIFIED RESIDUE
SEQADV 2IF2 LEU A 197 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 GLU A 198 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS A 199 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS A 200 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS A 201 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS A 202 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS A 203 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS A 204 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 MSE B 1 UNP O67792 MET 1 MODIFIED RESIDUE
SEQADV 2IF2 MSE B 20 UNP O67792 MET 20 MODIFIED RESIDUE
SEQADV 2IF2 MSE B 146 UNP O67792 MET 146 MODIFIED RESIDUE
SEQADV 2IF2 MSE B 159 UNP O67792 MET 159 MODIFIED RESIDUE
SEQADV 2IF2 LEU B 197 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 GLU B 198 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS B 199 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS B 200 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS B 201 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS B 202 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS B 203 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS B 204 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 MSE C 1 UNP O67792 MET 1 MODIFIED RESIDUE
SEQADV 2IF2 MSE C 20 UNP O67792 MET 20 MODIFIED RESIDUE
SEQADV 2IF2 MSE C 146 UNP O67792 MET 146 MODIFIED RESIDUE
SEQADV 2IF2 MSE C 159 UNP O67792 MET 159 MODIFIED RESIDUE
SEQADV 2IF2 LEU C 197 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 GLU C 198 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS C 199 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS C 200 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS C 201 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS C 202 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS C 203 UNP O67792 EXPRESSION TAG
SEQADV 2IF2 HIS C 204 UNP O67792 EXPRESSION TAG
SEQRES 1 A 204 MSE LYS ARG ILE GLY LEU THR GLY ASN ILE GLY CYS GLY
SEQRES 2 A 204 LYS SER THR VAL ALA GLN MSE PHE ARG GLU LEU GLY ALA
SEQRES 3 A 204 TYR VAL LEU ASP ALA ASP LYS LEU ILE HIS SER PHE TYR
SEQRES 4 A 204 ARG LYS GLY HIS PRO VAL TYR GLU GLU VAL VAL LYS THR
SEQRES 5 A 204 PHE GLY LYS GLY ILE LEU ASP GLU GLU GLY ASN ILE ASP
SEQRES 6 A 204 ARG LYS LYS LEU ALA ASP ILE VAL PHE LYS ASP GLU GLU
SEQRES 7 A 204 LYS LEU ARG LYS LEU GLU GLU ILE THR HIS ARG ALA LEU
SEQRES 8 A 204 TYR LYS GLU ILE GLU LYS ILE THR LYS ASN LEU SER GLU
SEQRES 9 A 204 ASP THR LEU PHE ILE LEU GLU ALA SER LEU LEU VAL GLU
SEQRES 10 A 204 LYS GLY THR TYR LYS ASN TYR ASP LYS LEU ILE VAL VAL
SEQRES 11 A 204 TYR ALA PRO TYR GLU VAL CYS LYS GLU ARG ALA ILE LYS
SEQRES 12 A 204 ARG GLY MSE SER GLU GLU ASP PHE GLU ARG ARG TRP LYS
SEQRES 13 A 204 LYS GLN MSE PRO ILE GLU GLU LYS VAL LYS TYR ALA ASP
SEQRES 14 A 204 TYR VAL ILE ASP ASN SER GLY SER ILE GLU GLU THR TYR
SEQRES 15 A 204 LYS GLN VAL LYS LYS VAL TYR GLU GLU LEU THR ARG ASP
SEQRES 16 A 204 PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 204 MSE LYS ARG ILE GLY LEU THR GLY ASN ILE GLY CYS GLY
SEQRES 2 B 204 LYS SER THR VAL ALA GLN MSE PHE ARG GLU LEU GLY ALA
SEQRES 3 B 204 TYR VAL LEU ASP ALA ASP LYS LEU ILE HIS SER PHE TYR
SEQRES 4 B 204 ARG LYS GLY HIS PRO VAL TYR GLU GLU VAL VAL LYS THR
SEQRES 5 B 204 PHE GLY LYS GLY ILE LEU ASP GLU GLU GLY ASN ILE ASP
SEQRES 6 B 204 ARG LYS LYS LEU ALA ASP ILE VAL PHE LYS ASP GLU GLU
SEQRES 7 B 204 LYS LEU ARG LYS LEU GLU GLU ILE THR HIS ARG ALA LEU
SEQRES 8 B 204 TYR LYS GLU ILE GLU LYS ILE THR LYS ASN LEU SER GLU
SEQRES 9 B 204 ASP THR LEU PHE ILE LEU GLU ALA SER LEU LEU VAL GLU
SEQRES 10 B 204 LYS GLY THR TYR LYS ASN TYR ASP LYS LEU ILE VAL VAL
SEQRES 11 B 204 TYR ALA PRO TYR GLU VAL CYS LYS GLU ARG ALA ILE LYS
SEQRES 12 B 204 ARG GLY MSE SER GLU GLU ASP PHE GLU ARG ARG TRP LYS
SEQRES 13 B 204 LYS GLN MSE PRO ILE GLU GLU LYS VAL LYS TYR ALA ASP
SEQRES 14 B 204 TYR VAL ILE ASP ASN SER GLY SER ILE GLU GLU THR TYR
SEQRES 15 B 204 LYS GLN VAL LYS LYS VAL TYR GLU GLU LEU THR ARG ASP
SEQRES 16 B 204 PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 204 MSE LYS ARG ILE GLY LEU THR GLY ASN ILE GLY CYS GLY
SEQRES 2 C 204 LYS SER THR VAL ALA GLN MSE PHE ARG GLU LEU GLY ALA
SEQRES 3 C 204 TYR VAL LEU ASP ALA ASP LYS LEU ILE HIS SER PHE TYR
SEQRES 4 C 204 ARG LYS GLY HIS PRO VAL TYR GLU GLU VAL VAL LYS THR
SEQRES 5 C 204 PHE GLY LYS GLY ILE LEU ASP GLU GLU GLY ASN ILE ASP
SEQRES 6 C 204 ARG LYS LYS LEU ALA ASP ILE VAL PHE LYS ASP GLU GLU
SEQRES 7 C 204 LYS LEU ARG LYS LEU GLU GLU ILE THR HIS ARG ALA LEU
SEQRES 8 C 204 TYR LYS GLU ILE GLU LYS ILE THR LYS ASN LEU SER GLU
SEQRES 9 C 204 ASP THR LEU PHE ILE LEU GLU ALA SER LEU LEU VAL GLU
SEQRES 10 C 204 LYS GLY THR TYR LYS ASN TYR ASP LYS LEU ILE VAL VAL
SEQRES 11 C 204 TYR ALA PRO TYR GLU VAL CYS LYS GLU ARG ALA ILE LYS
SEQRES 12 C 204 ARG GLY MSE SER GLU GLU ASP PHE GLU ARG ARG TRP LYS
SEQRES 13 C 204 LYS GLN MSE PRO ILE GLU GLU LYS VAL LYS TYR ALA ASP
SEQRES 14 C 204 TYR VAL ILE ASP ASN SER GLY SER ILE GLU GLU THR TYR
SEQRES 15 C 204 LYS GLN VAL LYS LYS VAL TYR GLU GLU LEU THR ARG ASP
SEQRES 16 C 204 PRO LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 2IF2 MSE A 1 MET SELENOMETHIONINE
MODRES 2IF2 MSE A 20 MET SELENOMETHIONINE
MODRES 2IF2 MSE A 146 MET SELENOMETHIONINE
MODRES 2IF2 MSE A 159 MET SELENOMETHIONINE
MODRES 2IF2 MSE B 1 MET SELENOMETHIONINE
MODRES 2IF2 MSE B 20 MET SELENOMETHIONINE
MODRES 2IF2 MSE B 146 MET SELENOMETHIONINE
MODRES 2IF2 MSE B 159 MET SELENOMETHIONINE
MODRES 2IF2 MSE C 1 MET SELENOMETHIONINE
MODRES 2IF2 MSE C 20 MET SELENOMETHIONINE
MODRES 2IF2 MSE C 146 MET SELENOMETHIONINE
MODRES 2IF2 MSE C 159 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 20 8
HET MSE A 146 8
HET MSE A 159 8
HET MSE B 1 8
HET MSE B 20 8
HET MSE B 146 8
HET MSE B 159 8
HET MSE C 1 8
HET MSE C 20 8
HET MSE C 146 8
HET MSE C 159 8
HET SO4 A 301 5
HET SO4 B 302 5
HET SO4 C 303 5
HET EDO B 304 4
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 4 SO4 3(O4 S 2-)
FORMUL 7 EDO C2 H6 O2
FORMUL 8 HOH *7(H2 O)
HELIX 1 1 GLY A 13 LEU A 24 1 12
HELIX 2 2 ALA A 31 SER A 37 1 7
HELIX 3 3 PHE A 38 ARG A 40 5 3
HELIX 4 4 HIS A 43 GLY A 54 1 12
HELIX 5 5 ASP A 65 ILE A 72 1 8
HELIX 6 6 ASP A 76 TYR A 92 1 17
HELIX 7 7 GLU A 94 LEU A 102 1 9
HELIX 8 8 THR A 120 TYR A 124 5 5
HELIX 9 9 PRO A 133 ARG A 144 1 12
HELIX 10 10 SER A 147 LYS A 156 1 10
HELIX 11 11 PRO A 160 VAL A 165 1 6
HELIX 12 12 LYS A 166 ALA A 168 5 3
HELIX 13 13 SER A 177 GLU A 191 1 15
HELIX 14 14 GLY B 13 GLY B 25 1 13
HELIX 15 15 ALA B 31 SER B 37 1 7
HELIX 16 16 HIS B 43 GLY B 54 1 12
HELIX 17 17 LYS B 67 LYS B 75 1 9
HELIX 18 18 ASP B 76 ASN B 101 1 26
HELIX 19 19 GLY B 119 TYR B 124 5 6
HELIX 20 20 PRO B 133 ARG B 144 1 12
HELIX 21 21 SER B 147 GLN B 158 1 12
HELIX 22 22 PRO B 160 VAL B 165 1 6
HELIX 23 23 SER B 177 ARG B 194 1 18
HELIX 24 24 GLY C 13 LEU C 24 1 12
HELIX 25 25 ALA C 31 SER C 37 1 7
HELIX 26 26 LEU C 83 LEU C 102 1 20
HELIX 27 27 LEU C 114 GLY C 119 1 6
HELIX 28 28 PRO C 133 LYS C 143 1 11
HELIX 29 29 GLU C 148 LYS C 157 1 10
HELIX 30 30 PRO C 160 VAL C 165 1 6
HELIX 31 31 LYS C 166 ALA C 168 5 3
HELIX 32 32 SER C 177 GLU C 191 1 15
SHEET 1 A 5 TYR A 27 ASP A 30 0
SHEET 2 A 5 PHE A 108 GLU A 111 1 O ILE A 109 N LEU A 29
SHEET 3 A 5 ARG A 3 GLY A 8 1 N ILE A 4 O PHE A 108
SHEET 4 A 5 LYS A 126 VAL A 130 1 O ILE A 128 N THR A 7
SHEET 5 A 5 TYR A 170 VAL A 171 1 O TYR A 170 N VAL A 129
SHEET 1 B 2 ASP A 59 GLU A 60 0
SHEET 2 B 2 ASN A 63 ILE A 64 -1 O ASN A 63 N GLU A 60
SHEET 1 C 5 TYR B 27 ASP B 30 0
SHEET 2 C 5 PHE B 108 GLU B 111 1 O ILE B 109 N TYR B 27
SHEET 3 C 5 ARG B 3 GLY B 8 1 N ILE B 4 O PHE B 108
SHEET 4 C 5 LYS B 126 TYR B 131 1 O ILE B 128 N GLY B 5
SHEET 5 C 5 TYR B 170 ASP B 173 1 O ILE B 172 N TYR B 131
SHEET 1 D 5 TYR C 27 ASP C 30 0
SHEET 2 D 5 PHE C 108 GLU C 111 1 O GLU C 111 N LEU C 29
SHEET 3 D 5 ARG C 3 GLY C 8 1 N ILE C 4 O PHE C 108
SHEET 4 D 5 LYS C 126 TYR C 131 1 O ILE C 128 N GLY C 5
SHEET 5 D 5 TYR C 170 ASP C 173 1 O ILE C 172 N TYR C 131
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C GLN A 19 N MSE A 20 1555 1555 1.32
LINK C MSE A 20 N PHE A 21 1555 1555 1.33
LINK C GLY A 145 N MSE A 146 1555 1555 1.33
LINK C MSE A 146 N SER A 147 1555 1555 1.34
LINK C GLN A 158 N MSE A 159 1555 1555 1.33
LINK C MSE A 159 N PRO A 160 1555 1555 1.34
LINK C MSE B 1 N LYS B 2 1555 1555 1.33
LINK C GLN B 19 N MSE B 20 1555 1555 1.33
LINK C MSE B 20 N PHE B 21 1555 1555 1.33
LINK C GLY B 145 N MSE B 146 1555 1555 1.33
LINK C MSE B 146 N SER B 147 1555 1555 1.33
LINK C GLN B 158 N MSE B 159 1555 1555 1.33
LINK C MSE B 159 N PRO B 160 1555 1555 1.35
LINK C MSE C 1 N LYS C 2 1555 1555 1.33
LINK C GLN C 19 N MSE C 20 1555 1555 1.33
LINK C MSE C 20 N PHE C 21 1555 1555 1.33
LINK C GLY C 145 N MSE C 146 1555 1555 1.33
LINK C MSE C 146 N SER C 147 1555 1555 1.33
LINK C GLN C 158 N MSE C 159 1555 1555 1.33
LINK C MSE C 159 N PRO C 160 1555 1555 1.34
SITE 1 AC1 8 ASN A 9 ILE A 10 GLY A 11 CYS A 12
SITE 2 AC1 8 GLY A 13 LYS A 14 SER A 15 ARG A 144
SITE 1 AC2 5 GLY B 11 CYS B 12 GLY B 13 LYS B 14
SITE 2 AC2 5 ARG B 144
SITE 1 AC3 7 ASN C 9 GLY C 11 CYS C 12 GLY C 13
SITE 2 AC3 7 LYS C 14 SER C 15 ARG C 144
SITE 1 AC4 3 ASP B 32 HIS B 88 LYS B 118
CRYST1 71.632 97.013 121.625 90.00 90.00 90.00 P 21 21 21 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 0.013960 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010308 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008222 0.00000
HETATM 1 N MSE A 1 18.316 32.286 2.441 1.00103.60 N
HETATM 2 CA MSE A 1 18.225 33.294 3.537 1.00102.84 C
HETATM 3 C MSE A 1 16.890 34.023 3.502 1.00100.93 C
HETATM 4 O MSE A 1 16.239 34.112 2.461 1.00101.14 O
HETATM 5 CB MSE A 1 19.370 34.298 3.417 1.00105.39 C
HETATM 6 CG MSE A 1 19.535 34.868 2.022 1.00107.81 C
HETATM 7 SE MSE A 1 21.100 35.989 1.844 1.00113.08 SE
HETATM 8 CE MSE A 1 20.199 37.698 1.719 1.00111.51 C
(ATOM LINES ARE NOT SHOWN.)
END
