HEADER LIGASE 17-AUG-09 3A5Z
TITLE CRYSTAL STRUCTURE OF ESCHERICHIA COLI GENX IN COMPLEX WITH ELONGATION
TITLE 2 FACTOR P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE LYSYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 SYNONYM: GENX;
COMPND 5 EC: 6.1.1.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ELONGATION FACTOR P;
COMPND 9 CHAIN: B, D, F, H;
COMPND 10 SYNONYM: EF-P;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: MC4100;
SOURCE 5 GENE: GENX, ECS5136;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28C;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 13 ORGANISM_TAXID: 562;
SOURCE 14 GENE: EFP, ECS5128;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PET28C
KEYWDS AMINOACYL-TRNA SYNTHETASE PARALOG, TRANSLATION, TRNA, LYSYL-TRNA
KEYWDS 2 SYNTHETASE, ELONGATION FACTOR, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 3 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 4 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, AMINOACYL-TRNA
KEYWDS 5 SYNTHETASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.SUMIDA,T.YANAGISAWA,R.ISHII,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 01-NOV-23 3A5Z 1 REMARK SEQADV
REVDAT 3 23-OCT-13 3A5Z 1 JRNL VERSN
REVDAT 2 08-SEP-10 3A5Z 1 JRNL
REVDAT 1 25-AUG-10 3A5Z 0
JRNL AUTH T.YANAGISAWA,T.SUMIDA,R.ISHII,C.TAKEMOTO,S.YOKOYAMA
JRNL TITL A PARALOG OF LYSYL-TRNA SYNTHETASE AMINOACYLATES A CONSERVED
JRNL TITL 2 LYSINE RESIDUE IN TRANSLATION ELONGATION FACTOR P.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 17 1136 2010
JRNL REFN ISSN 1545-9993
JRNL PMID 20729861
JRNL DOI 10.1038/NSMB.1889
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 904336.200
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 82571
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) : 0.226
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4162
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9979
REMARK 3 BIN R VALUE (WORKING SET) : 0.3670
REMARK 3 BIN FREE R VALUE : 0.4190
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 490
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14608
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 128
REMARK 3 SOLVENT ATOMS : 229
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.00000
REMARK 3 B22 (A**2) : -9.33000
REMARK 3 B33 (A**2) : 3.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -20.58000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.49
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) : 0.43
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.55
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.250 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.880 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.910 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 38.00
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : REFMACAMS.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : REFMACAMS.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3A5Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000028853.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-06
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 : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82592
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35700
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3A5Y, 1UEB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA/CACODYLATE, AMMONIUM SULFATE, PEG
REMARK 280 4000, PH 6.5, VAPOR DIFFUSION, HANGING DROP, 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 51.48000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ASP B 137
REMARK 465 THR B 138
REMARK 465 ASP B 139
REMARK 465 PRO B 140
REMARK 465 GLY B 141
REMARK 465 LEU B 142
REMARK 465 LYS B 143
REMARK 465 GLY B 144
REMARK 465 ASP B 145
REMARK 465 THR B 146
REMARK 465 ALA B 147
REMARK 465 GLY B 148
REMARK 465 THR B 149
REMARK 465 GLY B 150
REMARK 465 GLY B 151
REMARK 465 LYS B 152
REMARK 465 PRO B 153
REMARK 465 ALA B 154
REMARK 465 THR B 155
REMARK 465 LEU B 156
REMARK 465 SER B 157
REMARK 465 THR B 158
REMARK 465 GLY B 159
REMARK 465 ALA B 160
REMARK 465 VAL B 161
REMARK 465 VAL B 162
REMARK 465 LYS B 163
REMARK 465 VAL B 164
REMARK 465 PRO B 165
REMARK 465 LEU B 166
REMARK 465 PHE B 167
REMARK 465 VAL B 168
REMARK 465 GLN B 169
REMARK 465 ILE B 170
REMARK 465 GLY B 171
REMARK 465 GLU B 172
REMARK 465 VAL B 173
REMARK 465 ILE B 174
REMARK 465 LYS B 175
REMARK 465 VAL B 176
REMARK 465 ASP B 177
REMARK 465 THR B 178
REMARK 465 ARG B 179
REMARK 465 SER B 180
REMARK 465 GLY B 181
REMARK 465 GLU B 182
REMARK 465 TYR B 183
REMARK 465 VAL B 184
REMARK 465 SER B 185
REMARK 465 ARG B 186
REMARK 465 VAL B 187
REMARK 465 LYS B 188
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLY D 141
REMARK 465 LEU D 142
REMARK 465 LYS D 143
REMARK 465 GLY D 144
REMARK 465 ASP D 145
REMARK 465 THR D 146
REMARK 465 ALA D 147
REMARK 465 GLY D 148
REMARK 465 THR D 149
REMARK 465 GLY D 150
REMARK 465 LYS D 188
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 HIS E 0
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 ALA F 62
REMARK 465 GLU F 63
REMARK 465 GLY F 64
REMARK 465 ALA F 65
REMARK 465 ASP F 66
REMARK 465 VAL F 67
REMARK 465 VAL F 68
REMARK 465 ASP F 69
REMARK 465 MET F 70
REMARK 465 ASN F 71
REMARK 465 LEU F 72
REMARK 465 THR F 73
REMARK 465 TYR F 74
REMARK 465 LEU F 75
REMARK 465 TYR F 76
REMARK 465 ASN F 77
REMARK 465 ASP F 78
REMARK 465 GLY F 79
REMARK 465 GLU F 80
REMARK 465 PHE F 81
REMARK 465 TRP F 82
REMARK 465 HIS F 83
REMARK 465 PHE F 84
REMARK 465 MET F 85
REMARK 465 ASN F 86
REMARK 465 ASN F 87
REMARK 465 GLU F 88
REMARK 465 THR F 89
REMARK 465 PHE F 90
REMARK 465 GLU F 91
REMARK 465 GLN F 92
REMARK 465 LEU F 93
REMARK 465 SER F 94
REMARK 465 ALA F 95
REMARK 465 ASP F 96
REMARK 465 ALA F 97
REMARK 465 LYS F 98
REMARK 465 ALA F 99
REMARK 465 ILE F 100
REMARK 465 GLY F 101
REMARK 465 ASP F 102
REMARK 465 ASN F 103
REMARK 465 ALA F 104
REMARK 465 LYS F 105
REMARK 465 TRP F 106
REMARK 465 LEU F 107
REMARK 465 LEU F 108
REMARK 465 ASP F 109
REMARK 465 GLN F 110
REMARK 465 ALA F 111
REMARK 465 GLU F 112
REMARK 465 CYS F 113
REMARK 465 ILE F 114
REMARK 465 VAL F 115
REMARK 465 THR F 116
REMARK 465 LEU F 117
REMARK 465 TRP F 118
REMARK 465 ASN F 119
REMARK 465 GLY F 120
REMARK 465 GLN F 121
REMARK 465 PRO F 122
REMARK 465 ILE F 123
REMARK 465 SER F 124
REMARK 465 VAL F 125
REMARK 465 THR F 126
REMARK 465 PRO F 127
REMARK 465 PRO F 128
REMARK 465 ASN F 129
REMARK 465 PHE F 130
REMARK 465 VAL F 131
REMARK 465 GLU F 132
REMARK 465 LEU F 133
REMARK 465 GLU F 134
REMARK 465 ILE F 135
REMARK 465 VAL F 136
REMARK 465 ASP F 137
REMARK 465 THR F 138
REMARK 465 ASP F 139
REMARK 465 PRO F 140
REMARK 465 GLY F 141
REMARK 465 LEU F 142
REMARK 465 LYS F 143
REMARK 465 GLY F 144
REMARK 465 ASP F 145
REMARK 465 THR F 146
REMARK 465 ALA F 147
REMARK 465 GLY F 148
REMARK 465 THR F 149
REMARK 465 GLY F 150
REMARK 465 GLY F 151
REMARK 465 LYS F 152
REMARK 465 PRO F 153
REMARK 465 ALA F 154
REMARK 465 THR F 155
REMARK 465 LEU F 156
REMARK 465 SER F 157
REMARK 465 THR F 158
REMARK 465 GLY F 159
REMARK 465 ALA F 160
REMARK 465 VAL F 161
REMARK 465 VAL F 162
REMARK 465 LYS F 163
REMARK 465 VAL F 164
REMARK 465 PRO F 165
REMARK 465 LEU F 166
REMARK 465 PHE F 167
REMARK 465 VAL F 168
REMARK 465 GLN F 169
REMARK 465 ILE F 170
REMARK 465 GLY F 171
REMARK 465 GLU F 172
REMARK 465 VAL F 173
REMARK 465 ILE F 174
REMARK 465 LYS F 175
REMARK 465 VAL F 176
REMARK 465 ASP F 177
REMARK 465 THR F 178
REMARK 465 ARG F 179
REMARK 465 SER F 180
REMARK 465 GLY F 181
REMARK 465 GLU F 182
REMARK 465 TYR F 183
REMARK 465 VAL F 184
REMARK 465 SER F 185
REMARK 465 ARG F 186
REMARK 465 VAL F 187
REMARK 465 LYS F 188
REMARK 465 GLY G -2
REMARK 465 SER G -1
REMARK 465 HIS G 0
REMARK 465 HIS G 65
REMARK 465 SER G 66
REMARK 465 GLY H -2
REMARK 465 SER H -1
REMARK 465 HIS H 0
REMARK 465 MET H 1
REMARK 465 ALA H 2
REMARK 465 GLY H 141
REMARK 465 LEU H 142
REMARK 465 LYS H 143
REMARK 465 GLY H 144
REMARK 465 ASP H 145
REMARK 465 THR H 146
REMARK 465 ALA H 147
REMARK 465 GLY H 148
REMARK 465 THR H 149
REMARK 465 GLY H 150
REMARK 465 LYS H 188
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 ASP A 50 127.06 -36.55
REMARK 500 SER A 66 -80.30 -72.70
REMARK 500 GLU A 102 15.17 59.54
REMARK 500 SER A 163 -41.49 -132.98
REMARK 500 ALA A 164 156.05 -43.18
REMARK 500 ASP A 177 65.32 60.11
REMARK 500 SER A 221 -103.21 66.68
REMARK 500 GLU A 228 -74.88 -68.87
REMARK 500 HIS A 230 3.39 -66.69
REMARK 500 GLU A 234 48.12 -79.91
REMARK 500 SER B 6 -44.82 -23.39
REMARK 500 ASN B 7 66.16 -100.26
REMARK 500 ASP B 8 -7.61 -163.84
REMARK 500 PHE B 9 79.64 -63.91
REMARK 500 LEU B 47 0.12 -55.45
REMARK 500 THR B 48 5.38 -151.35
REMARK 500 ASN B 71 50.59 -92.49
REMARK 500 LEU B 75 -67.26 -97.72
REMARK 500 ASP B 78 39.12 -99.78
REMARK 500 PHE B 90 1.92 82.22
REMARK 500 GLN B 110 87.18 56.35
REMARK 500 PRO B 128 97.36 -65.09
REMARK 500 ASN B 129 63.48 -66.77
REMARK 500 PHE B 130 36.17 -147.17
REMARK 500 THR C 47 -167.00 -123.10
REMARK 500 GLU C 158 62.58 39.45
REMARK 500 ALA C 164 116.59 -21.75
REMARK 500 ASP C 177 75.89 48.28
REMARK 500 SER C 221 -112.16 63.96
REMARK 500 GLU C 228 -85.69 -66.11
REMARK 500 ARG C 272 -3.24 -57.07
REMARK 500 ALA D 11 126.67 -35.97
REMARK 500 LYS D 34 13.02 56.60
REMARK 500 ARG D 45 96.98 -69.48
REMARK 500 MET D 70 132.15 -177.74
REMARK 500 ASP D 78 29.96 -142.22
REMARK 500 ASP D 109 124.81 -26.04
REMARK 500 GLN D 110 2.28 90.27
REMARK 500 ASP D 137 128.25 -175.49
REMARK 500 ASP E 50 114.81 -38.96
REMARK 500 SER E 66 -91.33 -50.59
REMARK 500 MET E 69 115.07 -174.84
REMARK 500 SER E 221 -111.70 58.22
REMARK 500 SER F 6 -6.62 -48.00
REMARK 500 PHE F 9 79.52 -61.21
REMARK 500 ASP F 18 42.35 34.68
REMARK 500 GLU F 25 -74.35 -76.54
REMARK 500 ARG F 45 88.08 -63.05
REMARK 500 THR G 47 -162.79 -105.45
REMARK 500 MET G 124 21.76 -66.25
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
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 118 0.07 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 KAA A 990
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KAA C 991
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KAA E 992
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KAA G 993
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A5Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI GENX IN COMPLEX WITH
REMARK 900 LYSYLADENYLATE ANALOG
REMARK 900 RELATED ID: MY_001000087.2 RELATED DB: TARGETDB
DBREF 3A5Z A 1 325 UNP C3SGA2 C3SGA2_ECOLX 11 335
DBREF 3A5Z B 1 188 UNP C3SGD7 C3SGD7_ECOLX 1 188
DBREF 3A5Z C 1 325 UNP C3SGA2 C3SGA2_ECOLX 11 335
DBREF 3A5Z D 1 188 UNP C3SGD7 C3SGD7_ECOLX 1 188
DBREF 3A5Z E 1 325 UNP C3SGA2 C3SGA2_ECOLX 11 335
DBREF 3A5Z F 1 188 UNP C3SGD7 C3SGD7_ECOLX 1 188
DBREF 3A5Z G 1 325 UNP C3SGA2 C3SGA2_ECOLX 11 335
DBREF 3A5Z H 1 188 UNP C3SGD7 C3SGD7_ECOLX 1 188
SEQADV 3A5Z GLY A -2 UNP C3SGA2 EXPRESSION TAG
SEQADV 3A5Z SER A -1 UNP C3SGA2 EXPRESSION TAG
SEQADV 3A5Z HIS A 0 UNP C3SGA2 EXPRESSION TAG
SEQADV 3A5Z GLY B -2 UNP C3SGD7 EXPRESSION TAG
SEQADV 3A5Z SER B -1 UNP C3SGD7 EXPRESSION TAG
SEQADV 3A5Z HIS B 0 UNP C3SGD7 EXPRESSION TAG
SEQADV 3A5Z GLY C -2 UNP C3SGA2 EXPRESSION TAG
SEQADV 3A5Z SER C -1 UNP C3SGA2 EXPRESSION TAG
SEQADV 3A5Z HIS C 0 UNP C3SGA2 EXPRESSION TAG
SEQADV 3A5Z GLY D -2 UNP C3SGD7 EXPRESSION TAG
SEQADV 3A5Z SER D -1 UNP C3SGD7 EXPRESSION TAG
SEQADV 3A5Z HIS D 0 UNP C3SGD7 EXPRESSION TAG
SEQADV 3A5Z GLY E -2 UNP C3SGA2 EXPRESSION TAG
SEQADV 3A5Z SER E -1 UNP C3SGA2 EXPRESSION TAG
SEQADV 3A5Z HIS E 0 UNP C3SGA2 EXPRESSION TAG
SEQADV 3A5Z GLY F -2 UNP C3SGD7 EXPRESSION TAG
SEQADV 3A5Z SER F -1 UNP C3SGD7 EXPRESSION TAG
SEQADV 3A5Z HIS F 0 UNP C3SGD7 EXPRESSION TAG
SEQADV 3A5Z GLY G -2 UNP C3SGA2 EXPRESSION TAG
SEQADV 3A5Z SER G -1 UNP C3SGA2 EXPRESSION TAG
SEQADV 3A5Z HIS G 0 UNP C3SGA2 EXPRESSION TAG
SEQADV 3A5Z GLY H -2 UNP C3SGD7 EXPRESSION TAG
SEQADV 3A5Z SER H -1 UNP C3SGD7 EXPRESSION TAG
SEQADV 3A5Z HIS H 0 UNP C3SGD7 EXPRESSION TAG
SEQRES 1 A 328 GLY SER HIS MET SER GLU THR ALA SER TRP GLN PRO SER
SEQRES 2 A 328 ALA SER ILE PRO ASN LEU LEU LYS ARG ALA ALA ILE MET
SEQRES 3 A 328 ALA GLU ILE ARG ARG PHE PHE ALA ASP ARG GLY VAL LEU
SEQRES 4 A 328 GLU VAL GLU THR PRO CYS MET SER GLN ALA THR VAL THR
SEQRES 5 A 328 ASP ILE HIS LEU VAL PRO PHE GLU THR ARG PHE VAL GLY
SEQRES 6 A 328 PRO GLY HIS SER GLN GLY MET ASN LEU TRP LEU MET THR
SEQRES 7 A 328 SER PRO GLU TYR HIS MET LYS ARG LEU LEU VAL ALA GLY
SEQRES 8 A 328 CYS GLY PRO VAL PHE GLN LEU CYS ARG SER PHE ARG ASN
SEQRES 9 A 328 GLU GLU MET GLY ARG TYR HIS ASN PRO GLU PHE THR MET
SEQRES 10 A 328 LEU GLU TRP TYR ARG PRO HIS TYR ASP MET TYR ARG LEU
SEQRES 11 A 328 MET ASN GLU VAL ASP ASP LEU LEU GLN GLN VAL LEU ASP
SEQRES 12 A 328 CYS PRO ALA ALA GLU SER LEU SER TYR GLN GLN ALA PHE
SEQRES 13 A 328 LEU ARG TYR LEU GLU ILE ASP PRO LEU SER ALA ASP LYS
SEQRES 14 A 328 THR GLN LEU ARG GLU VAL ALA ALA LYS LEU ASP LEU SER
SEQRES 15 A 328 ASN VAL ALA ASP THR GLU GLU ASP ARG ASP THR LEU LEU
SEQRES 16 A 328 GLN LEU LEU PHE THR PHE GLY VAL GLU PRO ASN ILE GLY
SEQRES 17 A 328 LYS GLU LYS PRO THR PHE VAL TYR HIS PHE PRO ALA SER
SEQRES 18 A 328 GLN ALA SER LEU ALA GLN ILE SER THR GLU ASP HIS ARG
SEQRES 19 A 328 VAL ALA GLU ARG PHE GLU VAL TYR TYR LYS GLY ILE GLU
SEQRES 20 A 328 LEU ALA ASN GLY PHE HIS GLU LEU THR ASP ALA ARG GLU
SEQRES 21 A 328 GLN GLN GLN ARG PHE GLU GLN ASP ASN ARG LYS ARG ALA
SEQRES 22 A 328 ALA ARG GLY LEU PRO GLN HIS PRO ILE ASP GLN ASN LEU
SEQRES 23 A 328 ILE GLU ALA LEU LYS VAL GLY MET PRO ASP CYS SER GLY
SEQRES 24 A 328 VAL ALA LEU GLY VAL ASP ARG LEU VAL MET LEU ALA LEU
SEQRES 25 A 328 GLY ALA GLU THR LEU ALA GLU VAL ILE ALA PHE SER VAL
SEQRES 26 A 328 ASP ARG ALA
SEQRES 1 B 191 GLY SER HIS MET ALA THR TYR TYR SER ASN ASP PHE ARG
SEQRES 2 B 191 ALA GLY LEU LYS ILE MET LEU ASP GLY GLU PRO TYR ALA
SEQRES 3 B 191 VAL GLU ALA SER GLU PHE VAL LYS PRO GLY LYS GLY GLN
SEQRES 4 B 191 ALA PHE ALA ARG VAL LYS LEU ARG ARG LEU LEU THR GLY
SEQRES 5 B 191 THR ARG VAL GLU LYS THR PHE LYS SER THR ASP SER ALA
SEQRES 6 B 191 GLU GLY ALA ASP VAL VAL ASP MET ASN LEU THR TYR LEU
SEQRES 7 B 191 TYR ASN ASP GLY GLU PHE TRP HIS PHE MET ASN ASN GLU
SEQRES 8 B 191 THR PHE GLU GLN LEU SER ALA ASP ALA LYS ALA ILE GLY
SEQRES 9 B 191 ASP ASN ALA LYS TRP LEU LEU ASP GLN ALA GLU CYS ILE
SEQRES 10 B 191 VAL THR LEU TRP ASN GLY GLN PRO ILE SER VAL THR PRO
SEQRES 11 B 191 PRO ASN PHE VAL GLU LEU GLU ILE VAL ASP THR ASP PRO
SEQRES 12 B 191 GLY LEU LYS GLY ASP THR ALA GLY THR GLY GLY LYS PRO
SEQRES 13 B 191 ALA THR LEU SER THR GLY ALA VAL VAL LYS VAL PRO LEU
SEQRES 14 B 191 PHE VAL GLN ILE GLY GLU VAL ILE LYS VAL ASP THR ARG
SEQRES 15 B 191 SER GLY GLU TYR VAL SER ARG VAL LYS
SEQRES 1 C 328 GLY SER HIS MET SER GLU THR ALA SER TRP GLN PRO SER
SEQRES 2 C 328 ALA SER ILE PRO ASN LEU LEU LYS ARG ALA ALA ILE MET
SEQRES 3 C 328 ALA GLU ILE ARG ARG PHE PHE ALA ASP ARG GLY VAL LEU
SEQRES 4 C 328 GLU VAL GLU THR PRO CYS MET SER GLN ALA THR VAL THR
SEQRES 5 C 328 ASP ILE HIS LEU VAL PRO PHE GLU THR ARG PHE VAL GLY
SEQRES 6 C 328 PRO GLY HIS SER GLN GLY MET ASN LEU TRP LEU MET THR
SEQRES 7 C 328 SER PRO GLU TYR HIS MET LYS ARG LEU LEU VAL ALA GLY
SEQRES 8 C 328 CYS GLY PRO VAL PHE GLN LEU CYS ARG SER PHE ARG ASN
SEQRES 9 C 328 GLU GLU MET GLY ARG TYR HIS ASN PRO GLU PHE THR MET
SEQRES 10 C 328 LEU GLU TRP TYR ARG PRO HIS TYR ASP MET TYR ARG LEU
SEQRES 11 C 328 MET ASN GLU VAL ASP ASP LEU LEU GLN GLN VAL LEU ASP
SEQRES 12 C 328 CYS PRO ALA ALA GLU SER LEU SER TYR GLN GLN ALA PHE
SEQRES 13 C 328 LEU ARG TYR LEU GLU ILE ASP PRO LEU SER ALA ASP LYS
SEQRES 14 C 328 THR GLN LEU ARG GLU VAL ALA ALA LYS LEU ASP LEU SER
SEQRES 15 C 328 ASN VAL ALA ASP THR GLU GLU ASP ARG ASP THR LEU LEU
SEQRES 16 C 328 GLN LEU LEU PHE THR PHE GLY VAL GLU PRO ASN ILE GLY
SEQRES 17 C 328 LYS GLU LYS PRO THR PHE VAL TYR HIS PHE PRO ALA SER
SEQRES 18 C 328 GLN ALA SER LEU ALA GLN ILE SER THR GLU ASP HIS ARG
SEQRES 19 C 328 VAL ALA GLU ARG PHE GLU VAL TYR TYR LYS GLY ILE GLU
SEQRES 20 C 328 LEU ALA ASN GLY PHE HIS GLU LEU THR ASP ALA ARG GLU
SEQRES 21 C 328 GLN GLN GLN ARG PHE GLU GLN ASP ASN ARG LYS ARG ALA
SEQRES 22 C 328 ALA ARG GLY LEU PRO GLN HIS PRO ILE ASP GLN ASN LEU
SEQRES 23 C 328 ILE GLU ALA LEU LYS VAL GLY MET PRO ASP CYS SER GLY
SEQRES 24 C 328 VAL ALA LEU GLY VAL ASP ARG LEU VAL MET LEU ALA LEU
SEQRES 25 C 328 GLY ALA GLU THR LEU ALA GLU VAL ILE ALA PHE SER VAL
SEQRES 26 C 328 ASP ARG ALA
SEQRES 1 D 191 GLY SER HIS MET ALA THR TYR TYR SER ASN ASP PHE ARG
SEQRES 2 D 191 ALA GLY LEU LYS ILE MET LEU ASP GLY GLU PRO TYR ALA
SEQRES 3 D 191 VAL GLU ALA SER GLU PHE VAL LYS PRO GLY LYS GLY GLN
SEQRES 4 D 191 ALA PHE ALA ARG VAL LYS LEU ARG ARG LEU LEU THR GLY
SEQRES 5 D 191 THR ARG VAL GLU LYS THR PHE LYS SER THR ASP SER ALA
SEQRES 6 D 191 GLU GLY ALA ASP VAL VAL ASP MET ASN LEU THR TYR LEU
SEQRES 7 D 191 TYR ASN ASP GLY GLU PHE TRP HIS PHE MET ASN ASN GLU
SEQRES 8 D 191 THR PHE GLU GLN LEU SER ALA ASP ALA LYS ALA ILE GLY
SEQRES 9 D 191 ASP ASN ALA LYS TRP LEU LEU ASP GLN ALA GLU CYS ILE
SEQRES 10 D 191 VAL THR LEU TRP ASN GLY GLN PRO ILE SER VAL THR PRO
SEQRES 11 D 191 PRO ASN PHE VAL GLU LEU GLU ILE VAL ASP THR ASP PRO
SEQRES 12 D 191 GLY LEU LYS GLY ASP THR ALA GLY THR GLY GLY LYS PRO
SEQRES 13 D 191 ALA THR LEU SER THR GLY ALA VAL VAL LYS VAL PRO LEU
SEQRES 14 D 191 PHE VAL GLN ILE GLY GLU VAL ILE LYS VAL ASP THR ARG
SEQRES 15 D 191 SER GLY GLU TYR VAL SER ARG VAL LYS
SEQRES 1 E 328 GLY SER HIS MET SER GLU THR ALA SER TRP GLN PRO SER
SEQRES 2 E 328 ALA SER ILE PRO ASN LEU LEU LYS ARG ALA ALA ILE MET
SEQRES 3 E 328 ALA GLU ILE ARG ARG PHE PHE ALA ASP ARG GLY VAL LEU
SEQRES 4 E 328 GLU VAL GLU THR PRO CYS MET SER GLN ALA THR VAL THR
SEQRES 5 E 328 ASP ILE HIS LEU VAL PRO PHE GLU THR ARG PHE VAL GLY
SEQRES 6 E 328 PRO GLY HIS SER GLN GLY MET ASN LEU TRP LEU MET THR
SEQRES 7 E 328 SER PRO GLU TYR HIS MET LYS ARG LEU LEU VAL ALA GLY
SEQRES 8 E 328 CYS GLY PRO VAL PHE GLN LEU CYS ARG SER PHE ARG ASN
SEQRES 9 E 328 GLU GLU MET GLY ARG TYR HIS ASN PRO GLU PHE THR MET
SEQRES 10 E 328 LEU GLU TRP TYR ARG PRO HIS TYR ASP MET TYR ARG LEU
SEQRES 11 E 328 MET ASN GLU VAL ASP ASP LEU LEU GLN GLN VAL LEU ASP
SEQRES 12 E 328 CYS PRO ALA ALA GLU SER LEU SER TYR GLN GLN ALA PHE
SEQRES 13 E 328 LEU ARG TYR LEU GLU ILE ASP PRO LEU SER ALA ASP LYS
SEQRES 14 E 328 THR GLN LEU ARG GLU VAL ALA ALA LYS LEU ASP LEU SER
SEQRES 15 E 328 ASN VAL ALA ASP THR GLU GLU ASP ARG ASP THR LEU LEU
SEQRES 16 E 328 GLN LEU LEU PHE THR PHE GLY VAL GLU PRO ASN ILE GLY
SEQRES 17 E 328 LYS GLU LYS PRO THR PHE VAL TYR HIS PHE PRO ALA SER
SEQRES 18 E 328 GLN ALA SER LEU ALA GLN ILE SER THR GLU ASP HIS ARG
SEQRES 19 E 328 VAL ALA GLU ARG PHE GLU VAL TYR TYR LYS GLY ILE GLU
SEQRES 20 E 328 LEU ALA ASN GLY PHE HIS GLU LEU THR ASP ALA ARG GLU
SEQRES 21 E 328 GLN GLN GLN ARG PHE GLU GLN ASP ASN ARG LYS ARG ALA
SEQRES 22 E 328 ALA ARG GLY LEU PRO GLN HIS PRO ILE ASP GLN ASN LEU
SEQRES 23 E 328 ILE GLU ALA LEU LYS VAL GLY MET PRO ASP CYS SER GLY
SEQRES 24 E 328 VAL ALA LEU GLY VAL ASP ARG LEU VAL MET LEU ALA LEU
SEQRES 25 E 328 GLY ALA GLU THR LEU ALA GLU VAL ILE ALA PHE SER VAL
SEQRES 26 E 328 ASP ARG ALA
SEQRES 1 F 191 GLY SER HIS MET ALA THR TYR TYR SER ASN ASP PHE ARG
SEQRES 2 F 191 ALA GLY LEU LYS ILE MET LEU ASP GLY GLU PRO TYR ALA
SEQRES 3 F 191 VAL GLU ALA SER GLU PHE VAL LYS PRO GLY LYS GLY GLN
SEQRES 4 F 191 ALA PHE ALA ARG VAL LYS LEU ARG ARG LEU LEU THR GLY
SEQRES 5 F 191 THR ARG VAL GLU LYS THR PHE LYS SER THR ASP SER ALA
SEQRES 6 F 191 GLU GLY ALA ASP VAL VAL ASP MET ASN LEU THR TYR LEU
SEQRES 7 F 191 TYR ASN ASP GLY GLU PHE TRP HIS PHE MET ASN ASN GLU
SEQRES 8 F 191 THR PHE GLU GLN LEU SER ALA ASP ALA LYS ALA ILE GLY
SEQRES 9 F 191 ASP ASN ALA LYS TRP LEU LEU ASP GLN ALA GLU CYS ILE
SEQRES 10 F 191 VAL THR LEU TRP ASN GLY GLN PRO ILE SER VAL THR PRO
SEQRES 11 F 191 PRO ASN PHE VAL GLU LEU GLU ILE VAL ASP THR ASP PRO
SEQRES 12 F 191 GLY LEU LYS GLY ASP THR ALA GLY THR GLY GLY LYS PRO
SEQRES 13 F 191 ALA THR LEU SER THR GLY ALA VAL VAL LYS VAL PRO LEU
SEQRES 14 F 191 PHE VAL GLN ILE GLY GLU VAL ILE LYS VAL ASP THR ARG
SEQRES 15 F 191 SER GLY GLU TYR VAL SER ARG VAL LYS
SEQRES 1 G 328 GLY SER HIS MET SER GLU THR ALA SER TRP GLN PRO SER
SEQRES 2 G 328 ALA SER ILE PRO ASN LEU LEU LYS ARG ALA ALA ILE MET
SEQRES 3 G 328 ALA GLU ILE ARG ARG PHE PHE ALA ASP ARG GLY VAL LEU
SEQRES 4 G 328 GLU VAL GLU THR PRO CYS MET SER GLN ALA THR VAL THR
SEQRES 5 G 328 ASP ILE HIS LEU VAL PRO PHE GLU THR ARG PHE VAL GLY
SEQRES 6 G 328 PRO GLY HIS SER GLN GLY MET ASN LEU TRP LEU MET THR
SEQRES 7 G 328 SER PRO GLU TYR HIS MET LYS ARG LEU LEU VAL ALA GLY
SEQRES 8 G 328 CYS GLY PRO VAL PHE GLN LEU CYS ARG SER PHE ARG ASN
SEQRES 9 G 328 GLU GLU MET GLY ARG TYR HIS ASN PRO GLU PHE THR MET
SEQRES 10 G 328 LEU GLU TRP TYR ARG PRO HIS TYR ASP MET TYR ARG LEU
SEQRES 11 G 328 MET ASN GLU VAL ASP ASP LEU LEU GLN GLN VAL LEU ASP
SEQRES 12 G 328 CYS PRO ALA ALA GLU SER LEU SER TYR GLN GLN ALA PHE
SEQRES 13 G 328 LEU ARG TYR LEU GLU ILE ASP PRO LEU SER ALA ASP LYS
SEQRES 14 G 328 THR GLN LEU ARG GLU VAL ALA ALA LYS LEU ASP LEU SER
SEQRES 15 G 328 ASN VAL ALA ASP THR GLU GLU ASP ARG ASP THR LEU LEU
SEQRES 16 G 328 GLN LEU LEU PHE THR PHE GLY VAL GLU PRO ASN ILE GLY
SEQRES 17 G 328 LYS GLU LYS PRO THR PHE VAL TYR HIS PHE PRO ALA SER
SEQRES 18 G 328 GLN ALA SER LEU ALA GLN ILE SER THR GLU ASP HIS ARG
SEQRES 19 G 328 VAL ALA GLU ARG PHE GLU VAL TYR TYR LYS GLY ILE GLU
SEQRES 20 G 328 LEU ALA ASN GLY PHE HIS GLU LEU THR ASP ALA ARG GLU
SEQRES 21 G 328 GLN GLN GLN ARG PHE GLU GLN ASP ASN ARG LYS ARG ALA
SEQRES 22 G 328 ALA ARG GLY LEU PRO GLN HIS PRO ILE ASP GLN ASN LEU
SEQRES 23 G 328 ILE GLU ALA LEU LYS VAL GLY MET PRO ASP CYS SER GLY
SEQRES 24 G 328 VAL ALA LEU GLY VAL ASP ARG LEU VAL MET LEU ALA LEU
SEQRES 25 G 328 GLY ALA GLU THR LEU ALA GLU VAL ILE ALA PHE SER VAL
SEQRES 26 G 328 ASP ARG ALA
SEQRES 1 H 191 GLY SER HIS MET ALA THR TYR TYR SER ASN ASP PHE ARG
SEQRES 2 H 191 ALA GLY LEU LYS ILE MET LEU ASP GLY GLU PRO TYR ALA
SEQRES 3 H 191 VAL GLU ALA SER GLU PHE VAL LYS PRO GLY LYS GLY GLN
SEQRES 4 H 191 ALA PHE ALA ARG VAL LYS LEU ARG ARG LEU LEU THR GLY
SEQRES 5 H 191 THR ARG VAL GLU LYS THR PHE LYS SER THR ASP SER ALA
SEQRES 6 H 191 GLU GLY ALA ASP VAL VAL ASP MET ASN LEU THR TYR LEU
SEQRES 7 H 191 TYR ASN ASP GLY GLU PHE TRP HIS PHE MET ASN ASN GLU
SEQRES 8 H 191 THR PHE GLU GLN LEU SER ALA ASP ALA LYS ALA ILE GLY
SEQRES 9 H 191 ASP ASN ALA LYS TRP LEU LEU ASP GLN ALA GLU CYS ILE
SEQRES 10 H 191 VAL THR LEU TRP ASN GLY GLN PRO ILE SER VAL THR PRO
SEQRES 11 H 191 PRO ASN PHE VAL GLU LEU GLU ILE VAL ASP THR ASP PRO
SEQRES 12 H 191 GLY LEU LYS GLY ASP THR ALA GLY THR GLY GLY LYS PRO
SEQRES 13 H 191 ALA THR LEU SER THR GLY ALA VAL VAL LYS VAL PRO LEU
SEQRES 14 H 191 PHE VAL GLN ILE GLY GLU VAL ILE LYS VAL ASP THR ARG
SEQRES 15 H 191 SER GLY GLU TYR VAL SER ARG VAL LYS
HET KAA A 990 32
HET KAA C 991 32
HET KAA E 992 32
HET KAA G 993 32
HETNAM KAA 5'-O-[(L-LYSYLAMINO)SULFONYL]ADENOSINE
HETSYN KAA 5'-O-[N-(L-LYSYL)SULFAMOYL]ADENOSINE
FORMUL 9 KAA 4(C16 H26 N8 O7 S)
FORMUL 13 HOH *229(H2 O)
HELIX 1 1 SER A 12 ASP A 32 1 21
HELIX 2 2 GLY A 62 SER A 66 5 5
HELIX 3 3 PRO A 77 GLY A 88 1 12
HELIX 4 4 ASP A 123 ASP A 140 1 18
HELIX 5 5 TYR A 149 GLU A 158 1 10
HELIX 6 6 ASP A 165 LEU A 176 1 12
HELIX 7 7 LEU A 178 ASP A 183 1 6
HELIX 8 8 ASP A 187 VAL A 200 1 14
HELIX 9 9 GLU A 201 ILE A 204 5 4
HELIX 10 10 PRO A 216 ALA A 220 5 5
HELIX 11 11 ASP A 254 ARG A 272 1 19
HELIX 12 12 ASP A 280 GLY A 290 1 11
HELIX 13 13 VAL A 301 GLY A 310 1 10
HELIX 14 14 THR A 313 ILE A 318 5 6
HELIX 15 15 SER A 321 ALA A 325 5 5
HELIX 16 16 LEU B 47 GLY B 49 5 3
HELIX 17 17 ASP B 96 GLY B 101 1 6
HELIX 18 18 SER C 12 ARG C 33 1 22
HELIX 19 19 PRO C 77 ALA C 87 1 11
HELIX 20 20 ASP C 123 ASP C 140 1 18
HELIX 21 21 TYR C 149 GLU C 158 1 10
HELIX 22 22 ASP C 165 LEU C 176 1 12
HELIX 23 23 LEU C 178 ASP C 183 1 6
HELIX 24 24 ASP C 187 VAL C 200 1 14
HELIX 25 25 GLU C 201 ILE C 204 5 4
HELIX 26 26 PRO C 216 ALA C 220 5 5
HELIX 27 27 ASP C 254 GLY C 273 1 20
HELIX 28 28 ASP C 280 GLY C 290 1 11
HELIX 29 29 VAL C 301 GLY C 310 1 10
HELIX 30 30 THR C 313 VAL C 317 5 5
HELIX 31 31 ASN D 7 PHE D 9 5 3
HELIX 32 32 ASP D 96 GLY D 101 1 6
HELIX 33 33 ASN D 103 LEU D 107 5 5
HELIX 34 34 SER E 12 ARG E 33 1 22
HELIX 35 35 GLY E 62 SER E 66 5 5
HELIX 36 36 PRO E 77 GLY E 88 1 12
HELIX 37 37 ASP E 123 ASP E 140 1 18
HELIX 38 38 TYR E 149 GLU E 158 1 10
HELIX 39 39 ASP E 165 LEU E 176 1 12
HELIX 40 40 LEU E 178 ASP E 183 1 6
HELIX 41 41 ASP E 187 VAL E 200 1 14
HELIX 42 42 GLU E 201 ILE E 204 5 4
HELIX 43 43 PRO E 216 ALA E 220 5 5
HELIX 44 44 ASP E 254 ARG E 272 1 19
HELIX 45 45 ASP E 280 GLY E 290 1 11
HELIX 46 46 VAL E 301 LEU E 309 1 9
HELIX 47 47 THR E 313 ILE E 318 5 6
HELIX 48 48 SER E 321 ALA E 325 5 5
HELIX 49 49 SER G 12 ARG G 33 1 22
HELIX 50 50 PRO G 77 ALA G 87 1 11
HELIX 51 51 TYR G 125 LEU G 139 1 15
HELIX 52 52 SER G 148 GLU G 158 1 11
HELIX 53 53 ASP G 165 LEU G 176 1 12
HELIX 54 54 LEU G 178 ASP G 183 1 6
HELIX 55 55 ASP G 187 VAL G 200 1 14
HELIX 56 56 PRO G 216 ALA G 220 5 5
HELIX 57 57 ASP G 254 ARG G 272 1 19
HELIX 58 58 ASP G 280 MET G 291 1 12
HELIX 59 59 GLY G 300 GLY G 310 1 11
HELIX 60 60 LEU G 314 ILE G 318 5 5
HELIX 61 61 ASN H 7 PHE H 9 5 3
HELIX 62 62 ASP H 96 GLY H 101 1 6
HELIX 63 63 ASP H 102 LEU H 107 5 6
SHEET 1 A 8 LEU A 36 GLU A 37 0
SHEET 2 A 8 VAL A 92 PHE A 99 1 O PHE A 93 N LEU A 36
SHEET 3 A 8 GLU A 111 PRO A 120 -1 O PHE A 112 N SER A 98
SHEET 4 A 8 CYS A 294 GLY A 300 -1 O LEU A 299 N LEU A 115
SHEET 5 A 8 ILE A 243 HIS A 250 -1 N ASN A 247 O ALA A 298
SHEET 6 A 8 ARG A 235 TYR A 240 -1 N PHE A 236 O GLY A 248
SHEET 7 A 8 THR A 210 TYR A 213 -1 N THR A 210 O TYR A 239
SHEET 8 A 8 GLU A 145 SER A 148 1 N GLU A 145 O PHE A 211
SHEET 1 B 3 MET A 43 SER A 44 0
SHEET 2 B 3 MET A 69 LEU A 73 -1 O TRP A 72 N SER A 44
SHEET 3 B 3 GLU A 57 PHE A 60 -1 N PHE A 60 O MET A 69
SHEET 1 C 6 TYR B 4 TYR B 5 0
SHEET 2 C 6 SER B 61 GLY B 64 -1 O ALA B 62 N TYR B 4
SHEET 3 C 6 LYS B 14 LEU B 17 -1 N MET B 16 O GLU B 63
SHEET 4 C 6 GLU B 20 VAL B 30 -1 O GLU B 20 N LEU B 17
SHEET 5 C 6 PHE B 38 ARG B 45 -1 O PHE B 38 N VAL B 30
SHEET 6 C 6 ARG B 51 LYS B 57 -1 O LYS B 54 N VAL B 41
SHEET 1 D 3 VAL B 67 MET B 70 0
SHEET 2 D 3 ILE B 114 TRP B 118 -1 O VAL B 115 N MET B 70
SHEET 3 D 3 GLN B 121 THR B 126 -1 O THR B 126 N ILE B 114
SHEET 1 E 4 GLN B 92 ALA B 95 0
SHEET 2 E 4 TRP B 82 MET B 85 -1 N TRP B 82 O ALA B 95
SHEET 3 E 4 THR B 73 ASN B 77 -1 N LEU B 75 O HIS B 83
SHEET 4 E 4 ALA B 111 GLU B 112 -1 O ALA B 111 N TYR B 74
SHEET 1 F 8 LEU C 36 GLU C 37 0
SHEET 2 F 8 VAL C 92 PHE C 99 1 O PHE C 93 N LEU C 36
SHEET 3 F 8 GLU C 111 PRO C 120 -1 O PHE C 112 N SER C 98
SHEET 4 F 8 CYS C 294 GLY C 300 -1 O LEU C 299 N LEU C 115
SHEET 5 F 8 ILE C 243 HIS C 250 -1 N LEU C 245 O GLY C 300
SHEET 6 F 8 ARG C 235 TYR C 240 -1 N PHE C 236 O GLY C 248
SHEET 7 F 8 THR C 210 TYR C 213 -1 N THR C 210 O TYR C 239
SHEET 8 F 8 GLU C 145 SER C 148 1 N GLU C 145 O PHE C 211
SHEET 1 G 3 MET C 43 SER C 44 0
SHEET 2 G 3 MET C 69 LEU C 73 -1 O TRP C 72 N SER C 44
SHEET 3 G 3 GLU C 57 PHE C 60 -1 N THR C 58 O LEU C 71
SHEET 1 H 2 TYR D 4 TYR D 5 0
SHEET 2 H 2 SER D 61 ALA D 62 -1 O ALA D 62 N TYR D 4
SHEET 1 I 4 LYS D 14 LEU D 17 0
SHEET 2 I 4 GLU D 20 VAL D 30 -1 O TYR D 22 N ILE D 15
SHEET 3 I 4 PHE D 38 ARG D 45 -1 O PHE D 38 N VAL D 30
SHEET 4 I 4 THR D 50 LYS D 57 -1 O VAL D 52 N LEU D 43
SHEET 1 J 5 VAL D 67 VAL D 68 0
SHEET 2 J 5 GLU D 112 TRP D 118 -1 O LEU D 117 N VAL D 68
SHEET 3 J 5 ASN D 71 ASN D 77 -1 N LEU D 72 O CYS D 113
SHEET 4 J 5 TRP D 82 MET D 85 -1 O HIS D 83 N TYR D 76
SHEET 5 J 5 GLN D 92 ALA D 95 -1 O ALA D 95 N TRP D 82
SHEET 1 K 3 VAL D 67 VAL D 68 0
SHEET 2 K 3 GLU D 112 TRP D 118 -1 O LEU D 117 N VAL D 68
SHEET 3 K 3 GLN D 121 THR D 126 -1 O GLN D 121 N TRP D 118
SHEET 1 L 5 VAL D 161 VAL D 164 0
SHEET 2 L 5 LYS D 152 LEU D 156 -1 N LYS D 152 O VAL D 164
SHEET 3 L 5 PHE D 130 ASP D 137 -1 N ASP D 137 O THR D 155
SHEET 4 L 5 VAL D 173 ASP D 177 -1 O ILE D 174 N LEU D 133
SHEET 5 L 5 GLU D 182 ARG D 186 -1 O VAL D 184 N LYS D 175
SHEET 1 M 8 LEU E 36 GLU E 37 0
SHEET 2 M 8 VAL E 92 PHE E 99 1 O PHE E 93 N LEU E 36
SHEET 3 M 8 GLU E 111 PRO E 120 -1 O PHE E 112 N SER E 98
SHEET 4 M 8 CYS E 294 GLY E 300 -1 O LEU E 299 N LEU E 115
SHEET 5 M 8 ILE E 243 HIS E 250 -1 N PHE E 249 O GLY E 296
SHEET 6 M 8 ARG E 235 TYR E 240 -1 N PHE E 236 O GLY E 248
SHEET 7 M 8 THR E 210 TYR E 213 -1 N THR E 210 O TYR E 239
SHEET 8 M 8 GLU E 145 SER E 148 1 N LEU E 147 O PHE E 211
SHEET 1 N 3 MET E 43 SER E 44 0
SHEET 2 N 3 ASN E 70 LEU E 73 -1 O TRP E 72 N SER E 44
SHEET 3 N 3 GLU E 57 ARG E 59 -1 N THR E 58 O LEU E 71
SHEET 1 O 4 LYS F 14 LEU F 17 0
SHEET 2 O 4 GLU F 20 VAL F 30 -1 O TYR F 22 N ILE F 15
SHEET 3 O 4 PHE F 38 ARG F 45 -1 O PHE F 38 N VAL F 30
SHEET 4 O 4 THR F 50 LYS F 57 -1 O VAL F 52 N LEU F 43
SHEET 1 P 8 LEU G 36 GLU G 37 0
SHEET 2 P 8 VAL G 92 PHE G 99 1 O PHE G 93 N LEU G 36
SHEET 3 P 8 GLU G 111 PRO G 120 -1 O PHE G 112 N SER G 98
SHEET 4 P 8 CYS G 294 LEU G 299 -1 O LEU G 299 N LEU G 115
SHEET 5 P 8 ILE G 243 HIS G 250 -1 N PHE G 249 O GLY G 296
SHEET 6 P 8 ARG G 235 TYR G 240 -1 N PHE G 236 O GLY G 248
SHEET 7 P 8 THR G 210 TYR G 213 -1 N THR G 210 O TYR G 239
SHEET 8 P 8 GLU G 145 SER G 146 1 N GLU G 145 O PHE G 211
SHEET 1 Q 3 MET G 43 SER G 44 0
SHEET 2 Q 3 GLY G 68 LEU G 73 -1 O TRP G 72 N SER G 44
SHEET 3 Q 3 GLU G 57 VAL G 61 -1 N PHE G 60 O MET G 69
SHEET 1 R 6 TYR H 4 TYR H 5 0
SHEET 2 R 6 SER H 61 GLY H 64 -1 O ALA H 62 N TYR H 4
SHEET 3 R 6 LYS H 14 LEU H 17 -1 N MET H 16 O GLU H 63
SHEET 4 R 6 GLU H 20 VAL H 30 -1 O TYR H 22 N ILE H 15
SHEET 5 R 6 PHE H 38 ARG H 45 -1 O LYS H 42 N GLU H 25
SHEET 6 R 6 THR H 50 LYS H 57 -1 O LYS H 54 N VAL H 41
SHEET 1 S 5 GLN H 92 ALA H 95 0
SHEET 2 S 5 TRP H 82 MET H 85 -1 N PHE H 84 O LEU H 93
SHEET 3 S 5 VAL H 67 ASN H 77 -1 N TYR H 76 O HIS H 83
SHEET 4 S 5 GLU H 112 TRP H 118 -1 O CYS H 113 N LEU H 72
SHEET 5 S 5 GLN H 121 THR H 126 -1 O GLN H 121 N TRP H 118
SHEET 1 T 5 VAL H 161 VAL H 164 0
SHEET 2 T 5 LYS H 152 LEU H 156 -1 N ALA H 154 O VAL H 162
SHEET 3 T 5 PHE H 130 THR H 138 -1 N VAL H 136 O THR H 155
SHEET 4 T 5 VAL H 173 ASP H 177 -1 O ILE H 174 N LEU H 133
SHEET 5 T 5 TYR H 183 ARG H 186 -1 O VAL H 184 N LYS H 175
SITE 1 AC1 19 GLU A 78 ARG A 100 GLU A 103 TYR A 107
SITE 2 AC1 19 HIS A 108 ASN A 109 PHE A 112 MET A 114
SITE 3 AC1 19 TYR A 118 GLU A 244 LEU A 245 ASN A 247
SITE 4 AC1 19 PHE A 249 GLU A 251 ALA A 298 GLY A 300
SITE 5 AC1 19 HOH A 355 HOH A 360 GLY B 33
SITE 1 AC2 19 GLU C 78 ARG C 100 GLU C 103 TYR C 107
SITE 2 AC2 19 HIS C 108 ASN C 109 PHE C 112 MET C 114
SITE 3 AC2 19 TYR C 118 GLU C 244 LEU C 245 ASN C 247
SITE 4 AC2 19 PHE C 249 GLU C 251 GLY C 296 ALA C 298
SITE 5 AC2 19 GLY C 300 ARG C 303 GLY D 33
SITE 1 AC3 18 GLU E 78 ARG E 100 GLU E 103 TYR E 107
SITE 2 AC3 18 HIS E 108 ASN E 109 PHE E 112 MET E 114
SITE 3 AC3 18 TYR E 118 GLU E 244 LEU E 245 ASN E 247
SITE 4 AC3 18 PHE E 249 GLU E 251 GLY E 296 GLY E 300
SITE 5 AC3 18 ARG E 303 GLY F 33
SITE 1 AC4 20 GLU G 78 ARG G 100 GLU G 103 TYR G 107
SITE 2 AC4 20 HIS G 108 ASN G 109 PHE G 112 MET G 114
SITE 3 AC4 20 TYR G 118 GLU G 237 GLU G 244 LEU G 245
SITE 4 AC4 20 ASN G 247 PHE G 249 GLU G 251 GLY G 296
SITE 5 AC4 20 ALA G 298 GLY G 300 ARG G 303 HOH G 342
CRYST1 105.930 102.960 119.940 90.00 99.40 90.00 P 1 21 1 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 0.009440 0.000000 0.001563 0.00000
SCALE2 0.000000 0.009713 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008451 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
