HEADER LIGASE 12-JUL-99 1QE0
TITLE CRYSTAL STRUCTURE OF APO S. AUREUS HISTIDYL-TRNA SYNTHETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTIDINE--TRNA LIGASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HISTIDYL-TRNA SYNTHETASE,HISRS;
COMPND 5 EC: 6.1.1.21;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: HISS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDB575
KEYWDS CLASS II TRNA SYNTHETASE, BETA SHEET, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.QIU,C.A.JANSON,M.N.BLACKBURN,I.K.CHOHAN,M.HIBBS,S.S.ABDEL-MEGUID
REVDAT 5 28-JUN-17 1QE0 1 DBREF
REVDAT 4 24-FEB-09 1QE0 1 VERSN
REVDAT 3 01-APR-03 1QE0 1 JRNL
REVDAT 2 26-SEP-01 1QE0 3 ATOM
REVDAT 1 12-JUL-00 1QE0 0
JRNL AUTH X.QIU,C.A.JANSON,M.N.BLACKBURN,I.K.CHHOHAN,M.HIBBS,
JRNL AUTH 2 S.S.ABDEL-MEGUID
JRNL TITL COOPERATIVE STRUCTURAL DYNAMICS AND A NOVEL FIDELITY
JRNL TITL 2 MECHANISM IN HISTIDYL-TRNA SYNTHETASES.
JRNL REF BIOCHEMISTRY V. 38 12296 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10493797
JRNL DOI 10.1021/BI990482V
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 70.0
REMARK 3 NUMBER OF REFLECTIONS : 19332
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : 5% OF OBSERVED REFLECTIONS
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1010
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 : 5896
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 2.000
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THERE IS A PSEUDO 1/2 TRANSLATION ALONG Z, CAUSING NEARLY HALF OF
REMARK 3 THE
REMARK 3 REFLECTIONS BEING NEAR ZERO INTENSITY AND MEASURED AT NOISE LEVEL.
REMARK 3 R(ALL) IS NOT CALCULATED SINCE IT WOULD BE HORRIBLE.
REMARK 4
REMARK 4 1QE0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000009328.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT, SMART
REMARK 200 DATA SCALING SOFTWARE : SAINT
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28925
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 31.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.19400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.56400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CITRATE, TARTRATE, (NH4)2SO4, PH 5.6,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.32667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 38.66333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.99500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 19.33167
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 96.65833
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 52
REMARK 465 VAL A 53
REMARK 465 GLY A 54
REMARK 465 ASP A 55
REMARK 465 SER A 56
REMARK 465 THR A 57
REMARK 465 ASP A 58
REMARK 465 VAL A 59
REMARK 465 VAL A 60
REMARK 465 GLN A 61
REMARK 465 LYS A 62
REMARK 465 GLU A 114
REMARK 465 ARG A 115
REMARK 465 LYS A 116
REMARK 465 GLN A 117
REMARK 465 LYS A 118
REMARK 465 GLY A 119
REMARK 465 ARG A 120
REMARK 465 ASP A 207
REMARK 465 CYS A 208
REMARK 465 LYS A 209
REMARK 465 VAL A 210
REMARK 465 ASP A 211
REMARK 465 ARG A 212
REMARK 465 ASP A 213
REMARK 465 LYS A 214
REMARK 465 GLU A 215
REMARK 465 ALA A 216
REMARK 465 ILE A 217
REMARK 465 LYS A 218
REMARK 465 GLY B 52
REMARK 465 VAL B 53
REMARK 465 GLY B 54
REMARK 465 ASP B 55
REMARK 465 SER B 56
REMARK 465 THR B 57
REMARK 465 ASP B 58
REMARK 465 VAL B 59
REMARK 465 VAL B 60
REMARK 465 GLN B 61
REMARK 465 LYS B 62
REMARK 465 GLU B 114
REMARK 465 ARG B 115
REMARK 465 LYS B 116
REMARK 465 GLN B 117
REMARK 465 LYS B 118
REMARK 465 GLY B 119
REMARK 465 ARG B 120
REMARK 465 ARG B 172
REMARK 465 LYS B 173
REMARK 465 GLU B 174
REMARK 465 TYR B 175
REMARK 465 ASN B 176
REMARK 465 GLU B 177
REMARK 465 ALA B 178
REMARK 465 LEU B 179
REMARK 465 VAL B 180
REMARK 465 LYS B 181
REMARK 465 HIS B 182
REMARK 465 PHE B 183
REMARK 465 GLU B 184
REMARK 465 PRO B 185
REMARK 465 VAL B 186
REMARK 465 ILE B 187
REMARK 465 HIS B 188
REMARK 465 GLU B 189
REMARK 465 PHE B 190
REMARK 465 CYS B 191
REMARK 465 SER B 192
REMARK 465 ASP B 193
REMARK 465 CYS B 194
REMARK 465 GLN B 195
REMARK 465 SER B 196
REMARK 465 ARG B 197
REMARK 465 LEU B 198
REMARK 465 HIS B 199
REMARK 465 THR B 200
REMARK 465 ASP B 201
REMARK 465 PRO B 202
REMARK 465 MET B 203
REMARK 465 ARG B 204
REMARK 465 ILE B 205
REMARK 465 LEU B 206
REMARK 465 ASP B 207
REMARK 465 CYS B 208
REMARK 465 LYS B 209
REMARK 465 VAL B 210
REMARK 465 ASP B 211
REMARK 465 ARG B 212
REMARK 465 ASP B 213
REMARK 465 LYS B 214
REMARK 465 GLU B 215
REMARK 465 ALA B 216
REMARK 465 ILE B 217
REMARK 465 LYS B 218
REMARK 465 THR B 219
REMARK 465 ALA B 220
REMARK 465 PRO B 221
REMARK 465 ARG B 222
REMARK 465 ILE B 223
REMARK 465 THR B 224
REMARK 465 ASP B 225
REMARK 465 PHE B 226
REMARK 465 LEU B 227
REMARK 465 ASN B 228
REMARK 465 GLU B 229
REMARK 465 GLU B 230
REMARK 465 LYS B 420
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 A 63 CG CD OE1 OE2
REMARK 470 GLU A 323 CG CD OE1 OE2
REMARK 470 LYS B 232 CG CD CE NZ
REMARK 470 GLU B 323 CG CD OE1 OE2
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 PRO A 274 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 PRO A 299 C - N - CA ANGL. DEV. = 10.5 DEGREES
REMARK 500 LEU A 308 CA - CB - CG ANGL. DEV. = 18.5 DEGREES
REMARK 500 PRO B 274 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 PRO B 299 C - N - CA ANGL. DEV. = 10.5 DEGREES
REMARK 500 LEU B 308 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 13 -26.34 -38.84
REMARK 500 ASN A 34 33.66 75.59
REMARK 500 ASP A 47 -8.06 -59.83
REMARK 500 LYS A 68 57.21 -69.36
REMARK 500 ASP A 69 -152.54 -99.12
REMARK 500 ASP A 72 -7.74 67.74
REMARK 500 ASN A 107 111.28 -169.72
REMARK 500 ALA A 134 72.50 -168.00
REMARK 500 HIS A 158 48.93 -102.79
REMARK 500 HIS A 182 -78.60 -63.79
REMARK 500 VAL A 186 26.42 -141.89
REMARK 500 ASP A 193 -78.72 -54.67
REMARK 500 ASP A 201 92.33 -173.72
REMARK 500 PRO A 221 152.10 -48.22
REMARK 500 THR A 224 1.88 -65.02
REMARK 500 ASN A 228 -150.44 -78.77
REMARK 500 ASP A 260 -5.95 -56.27
REMARK 500 HIS A 264 -124.18 30.27
REMARK 500 ASP A 277 98.39 -64.86
REMARK 500 ALA A 279 -19.19 68.26
REMARK 500 PRO A 299 172.62 -54.92
REMARK 500 ASP A 325 54.26 -68.17
REMARK 500 GLU A 328 67.82 5.18
REMARK 500 LYS A 361 -168.88 -121.62
REMARK 500 LEU A 364 -6.21 62.33
REMARK 500 GLN A 365 83.73 34.09
REMARK 500 ALA A 380 109.59 -50.05
REMARK 500 ASN B 34 35.76 75.76
REMARK 500 ASP B 69 -151.29 -98.34
REMARK 500 ASP B 72 -4.16 60.07
REMARK 500 ASN B 107 113.12 -163.98
REMARK 500 ALA B 134 75.93 -170.28
REMARK 500 HIS B 158 48.90 -101.88
REMARK 500 LYS B 160 96.02 -160.42
REMARK 500 ASP B 260 -6.22 -57.90
REMARK 500 THR B 263 -73.66 -60.51
REMARK 500 HIS B 264 -99.66 -105.69
REMARK 500 PRO B 299 170.27 -54.73
REMARK 500 ILE B 326 -97.59 -86.89
REMARK 500 GLU B 327 83.76 48.35
REMARK 500 LYS B 361 -164.77 -122.13
REMARK 500 LEU B 364 -4.49 60.37
REMARK 500 GLN B 365 84.52 36.18
REMARK 500 LEU B 414 -64.27 -22.71
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 33 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QE0 A 1 420 UNP P60911 SYH_STAAU 1 420
DBREF 1QE0 B 1 420 UNP P60911 SYH_STAAU 1 420
SEQADV 1QE0 ASP A 201 UNP P60911 ASN 201 CONFLICT
SEQADV 1QE0 THR A 250 UNP P60911 ILE 250 CONFLICT
SEQADV 1QE0 ASP B 201 UNP P60911 ASN 201 CONFLICT
SEQADV 1QE0 THR B 250 UNP P60911 ILE 250 CONFLICT
SEQRES 1 A 420 MET ILE LYS ILE PRO ARG GLY THR GLN ASP ILE LEU PRO
SEQRES 2 A 420 GLU ASP SER LYS LYS TRP ARG TYR ILE GLU ASN GLN LEU
SEQRES 3 A 420 ASP GLU LEU MET THR PHE TYR ASN TYR LYS GLU ILE ARG
SEQRES 4 A 420 THR PRO ILE PHE GLU SER THR ASP LEU PHE ALA ARG GLY
SEQRES 5 A 420 VAL GLY ASP SER THR ASP VAL VAL GLN LYS GLU MET TYR
SEQRES 6 A 420 THR PHE LYS ASP LYS GLY ASP ARG SER ILE THR LEU ARG
SEQRES 7 A 420 PRO GLU GLY THR ALA ALA VAL VAL ARG SER TYR ILE GLU
SEQRES 8 A 420 HIS LYS MET GLN GLY ASN PRO ASN GLN PRO ILE LYS LEU
SEQRES 9 A 420 TYR TYR ASN GLY PRO MET PHE ARG TYR GLU ARG LYS GLN
SEQRES 10 A 420 LYS GLY ARG TYR ARG GLN PHE ASN GLN PHE GLY VAL GLU
SEQRES 11 A 420 ALA ILE GLY ALA GLU ASN PRO SER VAL ASP ALA GLU VAL
SEQRES 12 A 420 LEU ALA MET VAL MET HIS ILE TYR GLN SER PHE GLY LEU
SEQRES 13 A 420 LYS HIS LEU LYS LEU VAL ILE ASN SER VAL GLY ASP MET
SEQRES 14 A 420 ALA SER ARG LYS GLU TYR ASN GLU ALA LEU VAL LYS HIS
SEQRES 15 A 420 PHE GLU PRO VAL ILE HIS GLU PHE CYS SER ASP CYS GLN
SEQRES 16 A 420 SER ARG LEU HIS THR ASP PRO MET ARG ILE LEU ASP CYS
SEQRES 17 A 420 LYS VAL ASP ARG ASP LYS GLU ALA ILE LYS THR ALA PRO
SEQRES 18 A 420 ARG ILE THR ASP PHE LEU ASN GLU GLU SER LYS ALA TYR
SEQRES 19 A 420 TYR GLU GLN VAL LYS ALA TYR LEU ASP ASP LEU GLY ILE
SEQRES 20 A 420 PRO TYR THR GLU ASP PRO ASN LEU VAL ARG GLY LEU ASP
SEQRES 21 A 420 TYR TYR THR HIS THR ALA PHE GLU LEU MET MET ASP ASN
SEQRES 22 A 420 PRO ASN TYR ASP GLY ALA ILE THR THR LEU CYS GLY GLY
SEQRES 23 A 420 GLY ARG TYR ASN GLY LEU LEU GLU LEU LEU ASP GLY PRO
SEQRES 24 A 420 SER GLU THR GLY ILE GLY PHE ALA LEU SER ILE GLU ARG
SEQRES 25 A 420 LEU LEU LEU ALA LEU GLU GLU GLU GLY ILE GLU LEU ASP
SEQRES 26 A 420 ILE GLU GLU ASN LEU ASP LEU PHE ILE VAL THR MET GLY
SEQRES 27 A 420 ASP GLN ALA ASP ARG TYR ALA VAL LYS LEU LEU ASN HIS
SEQRES 28 A 420 LEU ARG HIS ASN GLY ILE LYS ALA ASP LYS ASP TYR LEU
SEQRES 29 A 420 GLN ARG LYS ILE LYS GLY GLN MET LYS GLN ALA ASP ARG
SEQRES 30 A 420 LEU GLY ALA LYS PHE THR ILE VAL ILE GLY ASP GLN GLU
SEQRES 31 A 420 LEU GLU ASN ASN LYS ILE ASP VAL LYS ASN MET THR THR
SEQRES 32 A 420 GLY GLU SER GLU THR ILE GLU LEU ASP ALA LEU VAL GLU
SEQRES 33 A 420 TYR PHE LYS LYS
SEQRES 1 B 420 MET ILE LYS ILE PRO ARG GLY THR GLN ASP ILE LEU PRO
SEQRES 2 B 420 GLU ASP SER LYS LYS TRP ARG TYR ILE GLU ASN GLN LEU
SEQRES 3 B 420 ASP GLU LEU MET THR PHE TYR ASN TYR LYS GLU ILE ARG
SEQRES 4 B 420 THR PRO ILE PHE GLU SER THR ASP LEU PHE ALA ARG GLY
SEQRES 5 B 420 VAL GLY ASP SER THR ASP VAL VAL GLN LYS GLU MET TYR
SEQRES 6 B 420 THR PHE LYS ASP LYS GLY ASP ARG SER ILE THR LEU ARG
SEQRES 7 B 420 PRO GLU GLY THR ALA ALA VAL VAL ARG SER TYR ILE GLU
SEQRES 8 B 420 HIS LYS MET GLN GLY ASN PRO ASN GLN PRO ILE LYS LEU
SEQRES 9 B 420 TYR TYR ASN GLY PRO MET PHE ARG TYR GLU ARG LYS GLN
SEQRES 10 B 420 LYS GLY ARG TYR ARG GLN PHE ASN GLN PHE GLY VAL GLU
SEQRES 11 B 420 ALA ILE GLY ALA GLU ASN PRO SER VAL ASP ALA GLU VAL
SEQRES 12 B 420 LEU ALA MET VAL MET HIS ILE TYR GLN SER PHE GLY LEU
SEQRES 13 B 420 LYS HIS LEU LYS LEU VAL ILE ASN SER VAL GLY ASP MET
SEQRES 14 B 420 ALA SER ARG LYS GLU TYR ASN GLU ALA LEU VAL LYS HIS
SEQRES 15 B 420 PHE GLU PRO VAL ILE HIS GLU PHE CYS SER ASP CYS GLN
SEQRES 16 B 420 SER ARG LEU HIS THR ASP PRO MET ARG ILE LEU ASP CYS
SEQRES 17 B 420 LYS VAL ASP ARG ASP LYS GLU ALA ILE LYS THR ALA PRO
SEQRES 18 B 420 ARG ILE THR ASP PHE LEU ASN GLU GLU SER LYS ALA TYR
SEQRES 19 B 420 TYR GLU GLN VAL LYS ALA TYR LEU ASP ASP LEU GLY ILE
SEQRES 20 B 420 PRO TYR THR GLU ASP PRO ASN LEU VAL ARG GLY LEU ASP
SEQRES 21 B 420 TYR TYR THR HIS THR ALA PHE GLU LEU MET MET ASP ASN
SEQRES 22 B 420 PRO ASN TYR ASP GLY ALA ILE THR THR LEU CYS GLY GLY
SEQRES 23 B 420 GLY ARG TYR ASN GLY LEU LEU GLU LEU LEU ASP GLY PRO
SEQRES 24 B 420 SER GLU THR GLY ILE GLY PHE ALA LEU SER ILE GLU ARG
SEQRES 25 B 420 LEU LEU LEU ALA LEU GLU GLU GLU GLY ILE GLU LEU ASP
SEQRES 26 B 420 ILE GLU GLU ASN LEU ASP LEU PHE ILE VAL THR MET GLY
SEQRES 27 B 420 ASP GLN ALA ASP ARG TYR ALA VAL LYS LEU LEU ASN HIS
SEQRES 28 B 420 LEU ARG HIS ASN GLY ILE LYS ALA ASP LYS ASP TYR LEU
SEQRES 29 B 420 GLN ARG LYS ILE LYS GLY GLN MET LYS GLN ALA ASP ARG
SEQRES 30 B 420 LEU GLY ALA LYS PHE THR ILE VAL ILE GLY ASP GLN GLU
SEQRES 31 B 420 LEU GLU ASN ASN LYS ILE ASP VAL LYS ASN MET THR THR
SEQRES 32 B 420 GLY GLU SER GLU THR ILE GLU LEU ASP ALA LEU VAL GLU
SEQRES 33 B 420 TYR PHE LYS LYS
FORMUL 3 HOH *100(H2 O)
HELIX 1 1 LEU A 12 ASN A 34 1 23
HELIX 2 2 THR A 46 ALA A 50 1 5
HELIX 3 3 LYS A 68 ARG A 73 1 6
HELIX 4 4 GLY A 81 HIS A 92 1 12
HELIX 5 5 LYS A 93 ASN A 97 5 5
HELIX 6 6 ASN A 136 PHE A 154 1 19
HELIX 7 7 ASP A 168 GLU A 184 1 17
HELIX 8 8 PRO A 185 PHE A 190 5 6
HELIX 9 9 CYS A 191 ARG A 197 1 7
HELIX 10 10 ASP A 201 LEU A 206 5 6
HELIX 11 11 ARG A 222 PHE A 226 5 5
HELIX 12 12 GLU A 230 GLY A 246 1 17
HELIX 13 13 GLY A 291 LEU A 296 1 6
HELIX 14 14 ILE A 310 GLU A 320 1 11
HELIX 15 15 MET A 337 HIS A 354 1 18
HELIX 16 16 LYS A 367 LEU A 378 1 12
HELIX 17 17 GLY A 387 ASN A 394 1 8
HELIX 18 18 ASP A 412 LYS A 420 1 9
HELIX 19 19 LEU B 12 ASN B 34 1 23
HELIX 20 20 THR B 46 ARG B 51 1 6
HELIX 21 21 LYS B 68 ARG B 73 1 6
HELIX 22 22 GLY B 81 HIS B 92 1 12
HELIX 23 23 LYS B 93 ASN B 97 5 5
HELIX 24 24 ASN B 136 SER B 153 1 18
HELIX 25 25 SER B 231 GLY B 246 1 16
HELIX 26 26 GLY B 291 LEU B 296 1 6
HELIX 27 27 ILE B 310 GLU B 320 1 11
HELIX 28 28 MET B 337 HIS B 354 1 18
HELIX 29 29 LYS B 367 LEU B 378 1 12
HELIX 30 30 GLY B 387 ASN B 394 1 8
HELIX 31 31 ASP B 412 LYS B 419 1 8
SHEET 1 A 8 LYS A 36 GLU A 37 0
SHEET 2 A 8 ILE A 102 PHE A 111 1 O LYS A 103 N LYS A 36
SHEET 3 A 8 GLN A 123 ILE A 132 -1 O PHE A 124 N MET A 110
SHEET 4 A 8 THR A 302 SER A 309 -1 O ILE A 304 N ALA A 131
SHEET 5 A 8 ILE A 280 ASN A 290 -1 O LEU A 283 N SER A 309
SHEET 6 A 8 TYR A 262 ASP A 272 -1 N THR A 263 O ARG A 288
SHEET 7 A 8 LEU A 159 SER A 165 -1 O LYS A 160 N MET A 270
SHEET 8 A 8 THR A 250 GLU A 251 1 N THR A 250 O LEU A 161
SHEET 1 B 3 PHE A 43 SER A 45 0
SHEET 2 B 3 ILE A 75 LEU A 77 -1 N THR A 76 O GLU A 44
SHEET 3 B 3 TYR A 65 PHE A 67 -1 O TYR A 65 N LEU A 77
SHEET 1 C 5 ALA A 359 LYS A 361 0
SHEET 2 C 5 LEU A 332 THR A 336 1 O LEU A 332 N ASP A 360
SHEET 3 C 5 PHE A 382 ILE A 386 1 O PHE A 382 N PHE A 333
SHEET 4 C 5 ILE A 396 ASN A 400 -1 O LYS A 399 N THR A 383
SHEET 5 C 5 SER A 406 ILE A 409 -1 O GLU A 407 N VAL A 398
SHEET 1 D 8 LYS B 36 GLU B 37 0
SHEET 2 D 8 ILE B 102 PHE B 111 1 O LYS B 103 N LYS B 36
SHEET 3 D 8 GLN B 123 ILE B 132 -1 O PHE B 124 N MET B 110
SHEET 4 D 8 THR B 302 SER B 309 -1 O ILE B 304 N ALA B 131
SHEET 5 D 8 ILE B 280 ASN B 290 -1 O LEU B 283 N SER B 309
SHEET 6 D 8 THR B 265 ASP B 272 -1 O THR B 265 N ARG B 288
SHEET 7 D 8 LEU B 159 SER B 165 -1 O LYS B 160 N MET B 270
SHEET 8 D 8 TYR B 249 GLU B 251 1 N THR B 250 O LEU B 161
SHEET 1 E 3 PHE B 43 SER B 45 0
SHEET 2 E 3 ILE B 75 LEU B 77 -1 N THR B 76 O GLU B 44
SHEET 3 E 3 THR B 66 PHE B 67 -1 O PHE B 67 N ILE B 75
SHEET 1 F 5 ALA B 359 LYS B 361 0
SHEET 2 F 5 LEU B 332 THR B 336 1 O LEU B 332 N ASP B 360
SHEET 3 F 5 PHE B 382 ILE B 386 1 O PHE B 382 N PHE B 333
SHEET 4 F 5 LYS B 395 ASN B 400 -1 O LYS B 399 N THR B 383
SHEET 5 F 5 SER B 406 GLU B 410 -1 O GLU B 407 N VAL B 398
SSBOND 1 CYS A 191 CYS A 194 1555 1555 2.86
CISPEP 1 GLN A 100 PRO A 101 0 -0.04
CISPEP 2 GLN B 100 PRO B 101 0 -0.75
CRYST1 125.650 125.650 115.990 90.00 90.00 120.00 P 65 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 0.007960 0.004590 0.000000 0.00000
SCALE2 0.000000 0.009190 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008620 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
