HEADER AMINOACYL-TRNA SYNTHASE 20-JUL-94 1GLN
TITLE ARCHITECTURES OF CLASS-DEFINING AND SPECIFIC DOMAINS OF GLUTAMYL-TRNA
TITLE 2 SYNTHETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8
KEYWDS RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL
KEYWDS 2 GENOMICS, AMINOACYL-TRNA SYNTHASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.NUREKI,D.G.VASSYLYEV,K.KATAYANAGI,T.SHIMIZU,S.SEKINE,T.KIGAWA,
AUTHOR 2 T.MIYAZAWA,S.YOKOYAMA,K.MORIKAWA,RIKEN STRUCTURAL
AUTHOR 3 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 5 07-FEB-24 1GLN 1 REMARK
REVDAT 4 29-NOV-17 1GLN 1 HELIX
REVDAT 3 13-JUL-11 1GLN 1 VERSN
REVDAT 2 24-FEB-09 1GLN 1 VERSN
REVDAT 1 15-OCT-95 1GLN 0
JRNL AUTH O.NUREKI,D.G.VASSYLYEV,K.KATAYANAGI,T.SHIMIZU,S.SEKINE,
JRNL AUTH 2 T.KIGAWA,T.MIYAZAWA,S.YOKOYAMA,K.MORIKAWA
JRNL TITL ARCHITECTURES OF CLASS-DEFINING AND SPECIFIC DOMAINS OF
JRNL TITL 2 GLUTAMYL-TRNA SYNTHETASE.
JRNL REF SCIENCE V. 267 1958 1995
JRNL REFN ISSN 0036-8075
JRNL PMID 7701318
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 3813
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : NULL
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: NULL
REMARK 4
REMARK 4 1GLN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173608.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13867
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 6.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 37.87500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.78000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.04500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.78000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.87500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.04500
REMARK 290 SMTRY3 4 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: MONOMERIC
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 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 NH2 ARG A 311 OE2 GLU A 364 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ILE A 6 N - CA - CB ANGL. DEV. = 19.8 DEGREES
REMARK 500 ALA A 7 CB - CA - C ANGL. DEV. = 11.1 DEGREES
REMARK 500 TRP A 28 CB - CA - C ANGL. DEV. = 12.2 DEGREES
REMARK 500 ARG A 31 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A 42 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 44 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 PRO A 50 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 55 CD - NE - CZ ANGL. DEV. = 17.6 DEGREES
REMARK 500 ARG A 55 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 55 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 VAL A 73 N - CA - CB ANGL. DEV. = -14.0 DEGREES
REMARK 500 ALA A 74 N - CA - CB ANGL. DEV. = 8.5 DEGREES
REMARK 500 GLU A 84 CA - CB - CG ANGL. DEV. = 17.1 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 GLU A 95 CA - CB - CG ANGL. DEV. = 13.7 DEGREES
REMARK 500 ARG A 99 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 ARG A 99 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 99 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 104 CD - NE - CZ ANGL. DEV. = 12.6 DEGREES
REMARK 500 ARG A 104 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 GLU A 136 CG - CD - OE2 ANGL. DEV. = 12.6 DEGREES
REMARK 500 ARG A 140 CD - NE - CZ ANGL. DEV. = 39.8 DEGREES
REMARK 500 ARG A 140 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 152 NH1 - CZ - NH2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG A 152 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 152 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP A 175 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 VAL A 177 CB - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 LEU A 197 CB - CA - C ANGL. DEV. = 11.9 DEGREES
REMARK 500 ARG A 205 CB - CG - CD ANGL. DEV. = 18.5 DEGREES
REMARK 500 ARG A 221 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 TRP A 225 CB - CA - C ANGL. DEV. = 14.1 DEGREES
REMARK 500 TRP A 225 CA - CB - CG ANGL. DEV. = 21.5 DEGREES
REMARK 500 ARG A 229 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 247 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 LEU A 262 CA - CB - CG ANGL. DEV. = 18.6 DEGREES
REMARK 500 ARG A 267 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 CYS A 271 N - CA - CB ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 281 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 PHE A 284 C - N - CA ANGL. DEV. = 27.9 DEGREES
REMARK 500 PHE A 284 N - CA - CB ANGL. DEV. = 16.6 DEGREES
REMARK 500 ARG A 297 CD - NE - CZ ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG A 311 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG A 311 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG A 319 CD - NE - CZ ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 319 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 319 NE - CZ - NH2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 GLU A 325 OE1 - CD - OE2 ANGL. DEV. = -10.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 63 ANGLE DEVIATIONS.
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 10 46.64 -66.74
REMARK 500 ALA A 29 -80.39 -50.26
REMARK 500 ASP A 72 -14.80 -48.83
REMARK 500 ALA A 74 -147.66 46.80
REMARK 500 ALA A 75 -172.28 152.36
REMARK 500 ARG A 81 111.10 -179.14
REMARK 500 ARG A 99 3.47 165.51
REMARK 500 ARG A 116 -70.87 -48.03
REMARK 500 LYS A 117 -11.95 -46.92
REMARK 500 PRO A 151 92.82 -65.60
REMARK 500 PRO A 228 -169.52 -76.47
REMARK 500 PRO A 234 -18.87 -40.76
REMARK 500 LEU A 235 136.69 74.96
REMARK 500 LYS A 241 162.89 -17.90
REMARK 500 THR A 242 123.90 150.80
REMARK 500 LYS A 243 118.19 -38.52
REMARK 500 ILE A 244 149.60 -35.94
REMARK 500 LYS A 248 61.87 90.53
REMARK 500 SER A 249 136.66 129.05
REMARK 500 PHE A 275 113.70 152.08
REMARK 500 PHE A 284 96.94 128.95
REMARK 500 THR A 285 -162.07 -63.41
REMARK 500 LEU A 286 -101.97 14.68
REMARK 500 GLU A 287 -52.91 -29.97
REMARK 500 GLN A 291 -29.55 -164.15
REMARK 500 PHE A 293 115.24 -39.41
REMARK 500 VAL A 321 -72.90 -140.41
REMARK 500 ALA A 369 31.00 -94.99
REMARK 500 TYR A 371 -17.93 -46.43
REMARK 500 LEU A 442 -8.95 96.51
REMARK 500 LEU A 453 -67.65 -28.67
REMARK 500 LEU A 467 -67.92 -92.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003000897.1 RELATED DB: TARGETDB
DBREF 1GLN A 1 468 UNP P27000 SYE_THET8 1 468
SEQRES 1 A 468 MET VAL VAL THR ARG ILE ALA PRO SER PRO THR GLY ASP
SEQRES 2 A 468 PRO HIS VAL GLY THR ALA TYR ILE ALA LEU PHE ASN TYR
SEQRES 3 A 468 ALA TRP ALA ARG ARG ASN GLY GLY ARG PHE ILE VAL ARG
SEQRES 4 A 468 ILE GLU ASP THR ASP ARG ALA ARG TYR VAL PRO GLY ALA
SEQRES 5 A 468 GLU GLU ARG ILE LEU ALA ALA LEU LYS TRP LEU GLY LEU
SEQRES 6 A 468 SER TYR ASP GLU GLY PRO ASP VAL ALA ALA PRO THR GLY
SEQRES 7 A 468 PRO TYR ARG GLN SER GLU ARG LEU PRO LEU TYR GLN LYS
SEQRES 8 A 468 TYR ALA GLU GLU LEU LEU LYS ARG GLY TRP ALA TYR ARG
SEQRES 9 A 468 ALA PHE GLU THR PRO GLU GLU LEU GLU GLN ILE ARG LYS
SEQRES 10 A 468 GLU LYS GLY GLY TYR ASP GLY ARG ALA ARG ASN ILE PRO
SEQRES 11 A 468 PRO GLU GLU ALA GLU GLU ARG ALA ARG ARG GLY GLU PRO
SEQRES 12 A 468 HIS VAL ILE ARG LEU LYS VAL PRO ARG PRO GLY THR THR
SEQRES 13 A 468 GLU VAL LYS ASP GLU LEU ARG GLY VAL VAL VAL TYR ASP
SEQRES 14 A 468 ASN GLN GLU ILE PRO ASP VAL VAL LEU LEU LYS SER ASP
SEQRES 15 A 468 GLY TYR PRO THR TYR HIS LEU ALA ASN VAL VAL ASP ASP
SEQRES 16 A 468 HIS LEU MET GLY VAL THR ASP VAL ILE ARG ALA GLU GLU
SEQRES 17 A 468 TRP LEU VAL SER THR PRO ILE HIS VAL LEU LEU TYR ARG
SEQRES 18 A 468 ALA PHE GLY TRP GLU ALA PRO ARG PHE TYR HIS MET PRO
SEQRES 19 A 468 LEU LEU ARG ASN PRO ASP LYS THR LYS ILE SER LYS ARG
SEQRES 20 A 468 LYS SER HIS THR SER LEU ASP TRP TYR LYS ALA GLU GLY
SEQRES 21 A 468 PHE LEU PRO GLU ALA LEU ARG ASN TYR LEU CYS LEU MET
SEQRES 22 A 468 GLY PHE SER MET PRO ASP GLY ARG GLU ILE PHE THR LEU
SEQRES 23 A 468 GLU GLU PHE ILE GLN ALA PHE THR TRP GLU ARG VAL SER
SEQRES 24 A 468 LEU GLY GLY PRO VAL PHE ASP LEU GLU LYS LEU ARG TRP
SEQRES 25 A 468 MET ASN GLY LYS TYR ILE ARG GLU VAL LEU SER LEU GLU
SEQRES 26 A 468 GLU VAL ALA GLU ARG VAL LYS PRO PHE LEU ARG GLU ALA
SEQRES 27 A 468 GLY LEU SER TRP GLU SER GLU ALA TYR LEU ARG ARG ALA
SEQRES 28 A 468 VAL GLU LEU MET ARG PRO ARG PHE ASP THR LEU LYS GLU
SEQRES 29 A 468 PHE PRO GLU LYS ALA ARG TYR LEU PHE THR GLU ASP TYR
SEQRES 30 A 468 PRO VAL SER GLU LYS ALA GLN ARG LYS LEU GLU GLU GLY
SEQRES 31 A 468 LEU PRO LEU LEU LYS GLU LEU TYR PRO ARG LEU ARG ALA
SEQRES 32 A 468 GLN GLU GLU TRP THR GLU ALA ALA LEU GLU ALA LEU LEU
SEQRES 33 A 468 ARG GLY PHE ALA ALA GLU LYS GLY VAL LYS LEU GLY GLN
SEQRES 34 A 468 VAL ALA GLN PRO LEU ARG ALA ALA LEU THR GLY SER LEU
SEQRES 35 A 468 GLU THR PRO GLY LEU PHE GLU ILE LEU ALA LEU LEU GLY
SEQRES 36 A 468 LYS GLU ARG ALA LEU ARG ARG LEU GLU ARG ALA LEU ALA
FORMUL 2 HOH *160(H2 O)
HELIX 1 AA HIS A 15 GLY A 33 1 19
HELIX 2 AB GLY A 51 GLY A 64 1 14
HELIX 3 AC ARG A 85 LYS A 98 1 14
HELIX 4 AD THR A 108 GLY A 120 1 13
HELIX 5 AE GLY A 124 ILE A 129 53/10 HELIX 6
HELIX 6 AF PRO A 131 ARG A 140 1 10
HELIX 7 AG THR A 186 GLY A 199 1 14
HELIX 8 AH SER A 212 GLY A 224 1 13
HELIX 9 AI SER A 252 GLY A 260 1 9
HELIX 10 AJ LEU A 262 MET A 273 1 12
HELIX 11 AK LEU A 286 PHE A 293 1 8
HELIX 12 AL ASP A 306 VAL A 321 1 16
HELIX 13 AM SER A 323 GLY A 339 1 17
HELIX 14 AN SER A 344 ARG A 356 1 13
HELIX 15 AO LYS A 363 ARG A 370 1 8
HELIX 16 AP SER A 380 LEU A 391 1 12
HELIX 17 AQ GLY A 390 GLN A 404 1 15
HELIX 18 AR THR A 408 GLY A 424 1 17
HELIX 19 AS LEU A 427 GLY A 440 1 14
HELIX 20 AT GLY A 446 LEU A 454 1 9
HELIX 21 AU GLY A 455 ALA A 468 1 14
SHEET 1 S1 5 ASP A 68 GLY A 70 0
SHEET 2 S1 5 ARG A 35 GLU A 41 1 O PHE A 36 N ASP A 68
SHEET 3 S1 5 VAL A 2 PRO A 8 1 O VAL A 2 N ARG A 35
SHEET 4 S1 5 THR A 201 GLU A 207 1 N THR A 201 O VAL A 3
SHEET 5 S1 5 ARG A 229 MET A 233 1 N ARG A 229 O THR A 201
SHEET 1 S2 4 TRP A 101 ALA A 105 0
SHEET 2 S2 4 HIS A 144 LYS A 149 -1 N LYS A 149 O TRP A 101
SHEET 3 S2 4 VAL A 176 SER A 181 1 O VAL A 176 N LEU A 148
SHEET 4 S2 4 TYR A 184 THR A 186 -1 N THR A 186 O LEU A 178
SHEET 1 S3 2 GLY A 154 ASP A 160 0
SHEET 2 S3 2 GLY A 164 ASN A 170 -1 N ASN A 170 O GLY A 154
CRYST1 75.750 110.090 67.560 90.00 90.00 90.00 P 21 21 21 4
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 0.013201 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014802 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
