HEADER LIGASE 13-MAR-12 4E51
TITLE CRYSTAL STRUCTURE OF A HISTIDYL-TRNA SYNTHETASE HISRS FROM
TITLE 2 BURKHOLDERIA THAILANDENSIS BOUND TO HISTIDINE
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: BURKHOLDERIA THAILANDENSIS;
SOURCE 3 ORGANISM_TAXID: 271848;
SOURCE 4 STRAIN: E264;
SOURCE 5 GENE: BTH_I2235, HISS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PAVA0421
KEYWDS SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, SSGCID,
KEYWDS 2 AMINOACYLATION, TRNA ACTIVATION, CHARGED TRNA, HISTIDYL-ADENYLATE,
KEYWDS 3 ATP-DEPENDENT, LIGASE, TRNA SYNTHETASE, AARS
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 4 13-SEP-23 4E51 1 REMARK SEQADV
REVDAT 3 29-MAR-17 4E51 1 JRNL REMARK
REVDAT 2 30-OCT-13 4E51 1 JRNL
REVDAT 1 28-MAR-12 4E51 0
JRNL AUTH S.O.MOEN,T.E.EDWARDS,D.M.DRANOW,M.C.CLIFTON,B.SANKARAN,
JRNL AUTH 2 W.C.VAN VOORHIS,A.SHARMA,C.MANOIL,B.L.STAKER,P.J.MYLER,
JRNL AUTH 3 D.D.LORIMER
JRNL TITL LIGAND CO-CRYSTALLIZATION OF AMINOACYL-TRNA SYNTHETASES FROM
JRNL TITL 2 INFECTIOUS DISEASE ORGANISMS.
JRNL REF SCI REP V. 7 223 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28303005
JRNL DOI 10.1038/S41598-017-00367-6
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.BAUGH,L.A.GALLAGHER,R.PATRAPUVICH,M.C.CLIFTON,
REMARK 1 AUTH 2 A.S.GARDBERG,T.E.EDWARDS,B.ARMOUR,D.W.BEGLEY,S.H.DIETERICH,
REMARK 1 AUTH 3 D.M.DRANOW,J.ABENDROTH,J.W.FAIRMAN,D.FOX,B.L.STAKER,I.PHAN,
REMARK 1 AUTH 4 A.GILLESPIE,R.CHOI,S.NAKAZAWA-HEWITT,M.T.NGUYEN,A.NAPULI,
REMARK 1 AUTH 5 L.BARRETT,G.W.BUCHKO,R.STACY,P.J.MYLER,L.J.STEWART,C.MANOIL,
REMARK 1 AUTH 6 W.C.VAN VOORHIS
REMARK 1 TITL COMBINING FUNCTIONAL AND STRUCTURAL GENOMICS TO SAMPLE THE
REMARK 1 TITL 2 ESSENTIAL BURKHOLDERIA STRUCTOME.
REMARK 1 REF PLOS ONE V. 8 53851 2013
REMARK 1 REFN ESSN 1932-6203
REMARK 1 PMID 23382856
REMARK 1 DOI 10.1371/JOURNAL.PONE.0053851
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 34582
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 + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1742
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2212
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.3300
REMARK 3 BIN FREE R VALUE SET COUNT : 129
REMARK 3 BIN FREE R VALUE : 0.4070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6041
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 64
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.91000
REMARK 3 B22 (A**2) : 5.78000
REMARK 3 B33 (A**2) : -1.87000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.477
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.280
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.214
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.915
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6182 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3941 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8419 ; 1.464 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9602 ; 1.130 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 801 ; 6.374 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 271 ;33.258 ;24.207
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 899 ;15.453 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;25.247 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 967 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7060 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1263 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 A 9 A 501 0
REMARK 3 0 B 9 B 501 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 9 A 439
REMARK 3 RESIDUE RANGE : A 501 A 501
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2705 0.3547 44.3262
REMARK 3 T TENSOR
REMARK 3 T11: 0.1200 T22: 0.1474
REMARK 3 T33: 0.1012 T12: 0.0441
REMARK 3 T13: -0.0306 T23: 0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 0.1155 L22: 0.6080
REMARK 3 L33: 0.4291 L12: 0.1666
REMARK 3 L13: 0.0507 L23: -0.2984
REMARK 3 S TENSOR
REMARK 3 S11: 0.0581 S12: 0.0087 S13: -0.0097
REMARK 3 S21: 0.0180 S22: -0.0598 S23: 0.0236
REMARK 3 S31: 0.0376 S32: 0.1150 S33: 0.0017
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 8 B 439
REMARK 3 RESIDUE RANGE : B 501 B 501
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4767 19.5742 36.0078
REMARK 3 T TENSOR
REMARK 3 T11: 0.0825 T22: 0.1883
REMARK 3 T33: 0.1480 T12: -0.0135
REMARK 3 T13: -0.0207 T23: -0.0348
REMARK 3 L TENSOR
REMARK 3 L11: 0.1497 L22: 0.5943
REMARK 3 L33: 0.3406 L12: 0.1759
REMARK 3 L13: -0.1358 L23: -0.3926
REMARK 3 S TENSOR
REMARK 3 S11: -0.0325 S12: -0.1186 S13: 0.0678
REMARK 3 S21: -0.0255 S22: -0.0010 S23: 0.0068
REMARK 3 S31: -0.0421 S32: 0.0845 S33: 0.0335
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES: WITH TLS ADDED HYDROGENS HAVE
REMARK 3 BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 4E51 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071177.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976484
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34582
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.3400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.52400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.220
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.3.0
REMARK 200 STARTING MODEL: PDB ENTRY 1HTT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BUTHA.00063.A.A1 PS01164 AT 31 MG/ML
REMARK 280 WITH 5 MM L-HISTIDINE AGAINST WIZARD III A3 FOCUS SCREEN, 350 MM
REMARK 280 MAGNESIUM FORMATE, 12% PEG 3350 WITH 20% GLYCEROL AS CRYO-
REMARK 280 PROTECTANT, CRYSTAL TRACKING ID 230808G3, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289K
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 35.08000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.49500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.18000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.49500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.08000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.18000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 MET A -20
REMARK 465 ALA A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 MET A -12
REMARK 465 GLY A -11
REMARK 465 THR A -10
REMARK 465 LEU A -9
REMARK 465 GLU A -8
REMARK 465 ALA A -7
REMARK 465 GLN A -6
REMARK 465 THR A -5
REMARK 465 GLN A -4
REMARK 465 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 GLU A 3
REMARK 465 GLN A 4
REMARK 465 LYS A 5
REMARK 465 ARG A 6
REMARK 465 LYS A 7
REMARK 465 LEU A 8
REMARK 465 GLN A 125
REMARK 465 ARG A 126
REMARK 465 GLY A 127
REMARK 465 LEU A 282
REMARK 465 GLY A 283
REMARK 465 ALA A 284
REMARK 465 GLN A 285
REMARK 465 ARG A 410
REMARK 465 GLY A 411
REMARK 465 THR A 412
REMARK 465 GLY A 413
REMARK 465 ASP A 414
REMARK 465 ASP A 415
REMARK 465 GLY A 416
REMARK 465 GLU A 417
REMARK 465 LYS A 418
REMARK 465 THR A 440
REMARK 465 ALA A 441
REMARK 465 GLU A 442
REMARK 465 ASP A 443
REMARK 465 GLY A 444
REMARK 465 ASP A 445
REMARK 465 ASP A 446
REMARK 465 MET B -20
REMARK 465 ALA B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 MET B -12
REMARK 465 GLY B -11
REMARK 465 THR B -10
REMARK 465 LEU B -9
REMARK 465 GLU B -8
REMARK 465 ALA B -7
REMARK 465 GLN B -6
REMARK 465 THR B -5
REMARK 465 GLN B -4
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 GLU B 3
REMARK 465 GLN B 4
REMARK 465 LYS B 5
REMARK 465 ARG B 6
REMARK 465 LYS B 7
REMARK 465 GLY B 61
REMARK 465 ILE B 62
REMARK 465 GLY B 63
REMARK 465 GLU B 64
REMARK 465 VAL B 65
REMARK 465 THR B 66
REMARK 465 ARG B 123
REMARK 465 PRO B 124
REMARK 465 GLN B 125
REMARK 465 ARG B 126
REMARK 465 GLY B 127
REMARK 465 LYS B 197
REMARK 465 LEU B 198
REMARK 465 ASP B 199
REMARK 465 ASP B 200
REMARK 465 ASP B 201
REMARK 465 ALA B 202
REMARK 465 ASP B 215
REMARK 465 THR B 216
REMARK 465 LYS B 217
REMARK 465 ASN B 218
REMARK 465 LYS B 281
REMARK 465 LEU B 282
REMARK 465 GLY B 283
REMARK 465 ALA B 284
REMARK 465 GLN B 285
REMARK 465 ARG B 410
REMARK 465 GLY B 411
REMARK 465 THR B 412
REMARK 465 GLY B 413
REMARK 465 ASP B 414
REMARK 465 ASP B 415
REMARK 465 GLY B 416
REMARK 465 GLU B 417
REMARK 465 LYS B 418
REMARK 465 THR B 440
REMARK 465 ALA B 441
REMARK 465 GLU B 442
REMARK 465 ASP B 443
REMARK 465 GLY B 444
REMARK 465 ASP B 445
REMARK 465 ASP B 446
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 9 CG CD OE1 OE2
REMARK 470 LYS A 15 CG CD CE NZ
REMARK 470 VAL A 65 CG1 CG2
REMARK 470 LYS A 71 CG CD CE NZ
REMARK 470 LEU A 80 CG CD1 CD2
REMARK 470 ASN A 81 CG OD1 ND2
REMARK 470 TYR A 106 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 123 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 128 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 130 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 184 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 189 CG CD CE NZ
REMARK 470 LYS A 197 CG CD CE NZ
REMARK 470 ASP A 201 CG OD1 OD2
REMARK 470 ARG A 204 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 212 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 217 CG CD CE NZ
REMARK 470 LYS A 281 CG CD CE NZ
REMARK 470 LYS A 304 CG CD CE NZ
REMARK 470 ARG A 317 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 324 CG CD OE1 OE2
REMARK 470 GLU A 325 CG CD OE1 OE2
REMARK 470 GLU A 330 CG CD OE1 OE2
REMARK 470 GLN A 331 CG CD OE1 NE2
REMARK 470 GLU A 332 CG CD OE1 OE2
REMARK 470 ARG A 355 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 377 CG CD CE NZ
REMARK 470 LYS A 381 CG CD CE NZ
REMARK 470 GLU A 396 CG CD OE1 OE2
REMARK 470 SER A 419 OG
REMARK 470 VAL A 420 CG1 CG2
REMARK 470 GLU A 431 CG CD OE1 OE2
REMARK 470 VAL A 438 CG1 CG2
REMARK 470 LEU B 8 CG CD1 CD2
REMARK 470 LYS B 15 CG CD CE NZ
REMARK 470 ASP B 67 CG OD1 OD2
REMARK 470 ILE B 68 CG1 CG2 CD1
REMARK 470 VAL B 69 CG1 CG2
REMARK 470 LYS B 71 CG CD CE NZ
REMARK 470 VAL B 77 CG1 CG2
REMARK 470 LEU B 80 CG CD1 CD2
REMARK 470 ASN B 81 CG OD1 ND2
REMARK 470 GLU B 83 CG CD OE1 OE2
REMARK 470 ARG B 120 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 122 CG CD OE1 OE2
REMARK 470 ARG B 128 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 186 CG CD OE1 OE2
REMARK 470 LEU B 187 CG CD1 CD2
REMARK 470 LYS B 189 CG CD CE NZ
REMARK 470 LEU B 191 CG CD1 CD2
REMARK 470 GLU B 192 CG CD OE1 OE2
REMARK 470 GLN B 193 CG CD OE1 NE2
REMARK 470 ASP B 196 CG OD1 OD2
REMARK 470 GLN B 203 CG CD OE1 NE2
REMARK 470 ARG B 204 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 205 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 206 CG CD1 CD2
REMARK 470 ASN B 209 CG OD1 ND2
REMARK 470 ARG B 212 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 213 CG1 CG2
REMARK 470 LEU B 214 CG CD1 CD2
REMARK 470 LEU B 221 CG CD1 CD2
REMARK 470 GLU B 223 CG CD OE1 OE2
REMARK 470 ILE B 224 CG1 CG2 CD1
REMARK 470 VAL B 225 CG1 CG2
REMARK 470 ARG B 226 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 230 CG CD CE NZ
REMARK 470 ARG B 240 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 265 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 267 CG CD1 CD2
REMARK 470 ASP B 280 CG OD1 OD2
REMARK 470 GLU B 320 CG CD OE1 OE2
REMARK 470 GLU B 324 CG CD OE1 OE2
REMARK 470 GLU B 325 CG CD OE1 OE2
REMARK 470 GLU B 330 CG CD OE1 OE2
REMARK 470 GLN B 331 CG CD OE1 NE2
REMARK 470 GLU B 332 CG CD OE1 OE2
REMARK 470 ARG B 346 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 355 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 377 CG CD CE NZ
REMARK 470 LYS B 381 CG CD CE NZ
REMARK 470 LYS B 407 CG CD CE NZ
REMARK 470 SER B 419 OG
REMARK 470 VAL B 420 CG1 CG2
REMARK 470 GLU B 431 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS A 251 NE2 GLN B 247 3545 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS B 133 CG HIS B 133 CD2 0.056
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 VAL A 14 129.61 -36.10
REMARK 500 ALA A 79 -70.64 -52.33
REMARK 500 GLU A 90 162.22 179.88
REMARK 500 LEU A 272 -125.75 56.31
REMARK 500 ASP A 280 60.17 -100.00
REMARK 500 TYR A 294 49.39 -155.23
REMARK 500 GLU B 70 -71.86 -67.03
REMARK 500 LEU B 272 -127.96 61.74
REMARK 500 TYR B 294 48.14 -156.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS B 71 GLU B 72 -146.66
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 HIS A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HIS B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: BUTHA.00063.A RELATED DB: TARGETTRACK
DBREF 4E51 A 1 446 UNP Q2SWE3 SYH_BURTA 1 446
DBREF 4E51 B 1 446 UNP Q2SWE3 SYH_BURTA 1 446
SEQADV 4E51 MET A -20 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 ALA A -19 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 HIS A -18 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 HIS A -17 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 HIS A -16 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 HIS A -15 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 HIS A -14 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 HIS A -13 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 MET A -12 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 GLY A -11 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 THR A -10 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 LEU A -9 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 GLU A -8 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 ALA A -7 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 GLN A -6 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 THR A -5 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 GLN A -4 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 GLY A -3 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 PRO A -2 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 GLY A -1 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 SER A 0 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 MET B -20 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 ALA B -19 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 HIS B -18 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 HIS B -17 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 HIS B -16 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 HIS B -15 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 HIS B -14 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 HIS B -13 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 MET B -12 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 GLY B -11 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 THR B -10 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 LEU B -9 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 GLU B -8 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 ALA B -7 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 GLN B -6 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 THR B -5 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 GLN B -4 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 GLY B -3 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 PRO B -2 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 GLY B -1 UNP Q2SWE3 EXPRESSION TAG
SEQADV 4E51 SER B 0 UNP Q2SWE3 EXPRESSION TAG
SEQRES 1 A 467 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 A 467 ALA GLN THR GLN GLY PRO GLY SER MET THR GLU GLN LYS
SEQRES 3 A 467 ARG LYS LEU GLU LYS LEU THR GLY VAL LYS GLY MET ASN
SEQRES 4 A 467 ASP ILE LEU PRO GLN ASP ALA GLY LEU TRP GLU PHE PHE
SEQRES 5 A 467 GLU ALA THR VAL LYS SER LEU LEU ARG ALA TYR GLY TYR
SEQRES 6 A 467 GLN ASN ILE ARG THR PRO ILE VAL GLU HIS THR PRO LEU
SEQRES 7 A 467 PHE THR ARG GLY ILE GLY GLU VAL THR ASP ILE VAL GLU
SEQRES 8 A 467 LYS GLU MET TYR SER PHE VAL ASP ALA LEU ASN GLY GLU
SEQRES 9 A 467 ASN LEU THR LEU ARG PRO GLU ASN THR ALA ALA VAL VAL
SEQRES 10 A 467 ARG ALA ALA ILE GLU HIS ASN MET LEU TYR ASP GLY PRO
SEQRES 11 A 467 LYS ARG LEU TRP TYR ILE GLY PRO MET PHE ARG HIS GLU
SEQRES 12 A 467 ARG PRO GLN ARG GLY ARG TYR ARG GLN PHE HIS GLN VAL
SEQRES 13 A 467 GLY VAL GLU ALA LEU GLY PHE ALA GLY PRO ASP ALA ASP
SEQRES 14 A 467 ALA GLU ILE VAL MET MET CYS GLN ARG LEU TRP GLU ASP
SEQRES 15 A 467 LEU GLY LEU THR GLY ILE LYS LEU GLU ILE ASN SER LEU
SEQRES 16 A 467 GLY LEU ALA GLU GLU ARG ALA ALA HIS ARG VAL GLU LEU
SEQRES 17 A 467 ILE LYS TYR LEU GLU GLN HIS ALA ASP LYS LEU ASP ASP
SEQRES 18 A 467 ASP ALA GLN ARG ARG LEU TYR THR ASN PRO LEU ARG VAL
SEQRES 19 A 467 LEU ASP THR LYS ASN PRO ALA LEU GLN GLU ILE VAL ARG
SEQRES 20 A 467 ASN ALA PRO LYS LEU ILE ASP PHE LEU GLY ASP VAL SER
SEQRES 21 A 467 ARG ALA HIS PHE GLU GLY LEU GLN ARG LEU LEU LYS ALA
SEQRES 22 A 467 ASN ASN VAL PRO PHE THR ILE ASN PRO ARG LEU VAL ARG
SEQRES 23 A 467 GLY LEU ASP TYR TYR ASN LEU THR VAL PHE GLU TRP VAL
SEQRES 24 A 467 THR ASP LYS LEU GLY ALA GLN GLY THR VAL ALA ALA GLY
SEQRES 25 A 467 GLY ARG TYR ASP PRO LEU ILE GLU GLN LEU GLY GLY LYS
SEQRES 26 A 467 PRO THR ALA ALA CYS GLY TRP ALA MET GLY ILE GLU ARG
SEQRES 27 A 467 ILE LEU GLU LEU LEU LYS GLU GLU HIS LEU VAL PRO GLU
SEQRES 28 A 467 GLN GLU GLY VAL ASP VAL TYR VAL VAL HIS GLN GLY ASP
SEQRES 29 A 467 ALA ALA ARG GLU GLN ALA PHE ILE VAL ALA GLU ARG LEU
SEQRES 30 A 467 ARG ASP THR GLY LEU ASP VAL ILE LEU HIS CYS SER ALA
SEQRES 31 A 467 ASP GLY ALA GLY ALA SER PHE LYS SER GLN MET LYS ARG
SEQRES 32 A 467 ALA ASP ALA SER GLY ALA ALA PHE ALA VAL ILE PHE GLY
SEQRES 33 A 467 GLU ASP GLU VAL THR ASN GLY THR ALA SER VAL LYS PRO
SEQRES 34 A 467 LEU ARG GLY THR GLY ASP ASP GLY GLU LYS SER VAL GLN
SEQRES 35 A 467 GLN SER VAL PRO VAL GLU SER LEU THR GLU PHE LEU ILE
SEQRES 36 A 467 ASN ALA MET VAL ALA THR ALA GLU ASP GLY ASP ASP
SEQRES 1 B 467 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 B 467 ALA GLN THR GLN GLY PRO GLY SER MET THR GLU GLN LYS
SEQRES 3 B 467 ARG LYS LEU GLU LYS LEU THR GLY VAL LYS GLY MET ASN
SEQRES 4 B 467 ASP ILE LEU PRO GLN ASP ALA GLY LEU TRP GLU PHE PHE
SEQRES 5 B 467 GLU ALA THR VAL LYS SER LEU LEU ARG ALA TYR GLY TYR
SEQRES 6 B 467 GLN ASN ILE ARG THR PRO ILE VAL GLU HIS THR PRO LEU
SEQRES 7 B 467 PHE THR ARG GLY ILE GLY GLU VAL THR ASP ILE VAL GLU
SEQRES 8 B 467 LYS GLU MET TYR SER PHE VAL ASP ALA LEU ASN GLY GLU
SEQRES 9 B 467 ASN LEU THR LEU ARG PRO GLU ASN THR ALA ALA VAL VAL
SEQRES 10 B 467 ARG ALA ALA ILE GLU HIS ASN MET LEU TYR ASP GLY PRO
SEQRES 11 B 467 LYS ARG LEU TRP TYR ILE GLY PRO MET PHE ARG HIS GLU
SEQRES 12 B 467 ARG PRO GLN ARG GLY ARG TYR ARG GLN PHE HIS GLN VAL
SEQRES 13 B 467 GLY VAL GLU ALA LEU GLY PHE ALA GLY PRO ASP ALA ASP
SEQRES 14 B 467 ALA GLU ILE VAL MET MET CYS GLN ARG LEU TRP GLU ASP
SEQRES 15 B 467 LEU GLY LEU THR GLY ILE LYS LEU GLU ILE ASN SER LEU
SEQRES 16 B 467 GLY LEU ALA GLU GLU ARG ALA ALA HIS ARG VAL GLU LEU
SEQRES 17 B 467 ILE LYS TYR LEU GLU GLN HIS ALA ASP LYS LEU ASP ASP
SEQRES 18 B 467 ASP ALA GLN ARG ARG LEU TYR THR ASN PRO LEU ARG VAL
SEQRES 19 B 467 LEU ASP THR LYS ASN PRO ALA LEU GLN GLU ILE VAL ARG
SEQRES 20 B 467 ASN ALA PRO LYS LEU ILE ASP PHE LEU GLY ASP VAL SER
SEQRES 21 B 467 ARG ALA HIS PHE GLU GLY LEU GLN ARG LEU LEU LYS ALA
SEQRES 22 B 467 ASN ASN VAL PRO PHE THR ILE ASN PRO ARG LEU VAL ARG
SEQRES 23 B 467 GLY LEU ASP TYR TYR ASN LEU THR VAL PHE GLU TRP VAL
SEQRES 24 B 467 THR ASP LYS LEU GLY ALA GLN GLY THR VAL ALA ALA GLY
SEQRES 25 B 467 GLY ARG TYR ASP PRO LEU ILE GLU GLN LEU GLY GLY LYS
SEQRES 26 B 467 PRO THR ALA ALA CYS GLY TRP ALA MET GLY ILE GLU ARG
SEQRES 27 B 467 ILE LEU GLU LEU LEU LYS GLU GLU HIS LEU VAL PRO GLU
SEQRES 28 B 467 GLN GLU GLY VAL ASP VAL TYR VAL VAL HIS GLN GLY ASP
SEQRES 29 B 467 ALA ALA ARG GLU GLN ALA PHE ILE VAL ALA GLU ARG LEU
SEQRES 30 B 467 ARG ASP THR GLY LEU ASP VAL ILE LEU HIS CYS SER ALA
SEQRES 31 B 467 ASP GLY ALA GLY ALA SER PHE LYS SER GLN MET LYS ARG
SEQRES 32 B 467 ALA ASP ALA SER GLY ALA ALA PHE ALA VAL ILE PHE GLY
SEQRES 33 B 467 GLU ASP GLU VAL THR ASN GLY THR ALA SER VAL LYS PRO
SEQRES 34 B 467 LEU ARG GLY THR GLY ASP ASP GLY GLU LYS SER VAL GLN
SEQRES 35 B 467 GLN SER VAL PRO VAL GLU SER LEU THR GLU PHE LEU ILE
SEQRES 36 B 467 ASN ALA MET VAL ALA THR ALA GLU ASP GLY ASP ASP
HET HIS A 501 11
HET HIS B 501 11
HETNAM HIS HISTIDINE
FORMUL 3 HIS 2(C6 H10 N3 O2 1+)
FORMUL 5 HOH *64(H2 O)
HELIX 1 1 LEU A 21 TYR A 42 1 22
HELIX 2 2 THR A 55 ILE A 62 1 8
HELIX 3 3 THR A 66 GLU A 72 1 7
HELIX 4 4 ASN A 91 HIS A 102 1 12
HELIX 5 5 PRO A 145 GLY A 163 1 19
HELIX 6 6 LEU A 176 GLN A 193 1 18
HELIX 7 7 HIS A 194 LEU A 198 5 5
HELIX 8 8 ASP A 199 TYR A 207 1 9
HELIX 9 9 PRO A 210 ASP A 215 1 6
HELIX 10 10 ASN A 218 ALA A 220 5 3
HELIX 11 11 LEU A 221 ASN A 227 1 7
HELIX 12 12 LYS A 230 LEU A 235 5 6
HELIX 13 13 GLY A 236 ASN A 253 1 18
HELIX 14 14 PRO A 296 LEU A 301 1 6
HELIX 15 15 ILE A 315 GLU A 325 1 11
HELIX 16 16 GLY A 342 THR A 359 1 18
HELIX 17 17 SER A 375 SER A 386 1 12
HELIX 18 18 GLY A 395 GLY A 402 1 8
HELIX 19 19 SER A 428 ALA A 439 1 12
HELIX 20 20 LEU B 21 TYR B 42 1 22
HELIX 21 21 THR B 55 ARG B 60 1 6
HELIX 22 22 ASN B 91 HIS B 102 1 12
HELIX 23 23 PRO B 145 GLY B 163 1 19
HELIX 24 24 LEU B 176 GLN B 193 1 18
HELIX 25 25 ASN B 209 LEU B 214 5 6
HELIX 26 26 LEU B 221 ASN B 227 1 7
HELIX 27 27 LYS B 230 LEU B 235 5 6
HELIX 28 28 GLY B 236 ASN B 253 1 18
HELIX 29 29 PRO B 296 LEU B 301 1 6
HELIX 30 30 ILE B 315 GLU B 325 1 11
HELIX 31 31 GLY B 342 THR B 359 1 18
HELIX 32 32 SER B 375 SER B 386 1 12
HELIX 33 33 GLY B 395 GLY B 402 1 8
HELIX 34 34 SER B 428 ALA B 439 1 12
SHEET 1 A 8 GLN A 45 ASN A 46 0
SHEET 2 A 8 LYS A 110 PHE A 119 1 O ARG A 111 N GLN A 45
SHEET 3 A 8 GLN A 131 LEU A 140 -1 O PHE A 132 N MET A 118
SHEET 4 A 8 ALA A 308 GLY A 314 -1 O CYS A 309 N ALA A 139
SHEET 5 A 8 THR A 287 ARG A 293 -1 N GLY A 292 O GLY A 310
SHEET 6 A 8 THR A 273 THR A 279 -1 N TRP A 277 O VAL A 288
SHEET 7 A 8 ILE A 167 SER A 173 -1 N ASN A 172 O VAL A 274
SHEET 8 A 8 PHE A 257 ILE A 259 1 O THR A 258 N ILE A 171
SHEET 1 B 3 VAL A 52 HIS A 54 0
SHEET 2 B 3 ASN A 84 LEU A 87 -1 O THR A 86 N GLU A 53
SHEET 3 B 3 SER A 75 VAL A 77 -1 N PHE A 76 O LEU A 85
SHEET 1 C 5 VAL A 363 LEU A 365 0
SHEET 2 C 5 VAL A 336 HIS A 340 1 N VAL A 338 O ILE A 364
SHEET 3 C 5 PHE A 390 PHE A 394 1 O VAL A 392 N VAL A 339
SHEET 4 C 5 THR A 403 PRO A 408 -1 O SER A 405 N ILE A 393
SHEET 5 C 5 GLN A 422 PRO A 425 -1 O GLN A 422 N VAL A 406
SHEET 1 D 8 GLN B 45 ASN B 46 0
SHEET 2 D 8 LYS B 110 PHE B 119 1 O ARG B 111 N GLN B 45
SHEET 3 D 8 GLN B 131 LEU B 140 -1 O PHE B 132 N MET B 118
SHEET 4 D 8 ALA B 308 GLY B 314 -1 O CYS B 309 N ALA B 139
SHEET 5 D 8 THR B 287 ARG B 293 -1 N GLY B 292 O GLY B 310
SHEET 6 D 8 THR B 273 THR B 279 -1 N TRP B 277 O VAL B 288
SHEET 7 D 8 ILE B 167 SER B 173 -1 N ASN B 172 O VAL B 274
SHEET 8 D 8 PHE B 257 ILE B 259 1 O THR B 258 N ILE B 171
SHEET 1 E 3 VAL B 52 HIS B 54 0
SHEET 2 E 3 ASN B 84 LEU B 87 -1 O THR B 86 N GLU B 53
SHEET 3 E 3 SER B 75 VAL B 77 -1 N PHE B 76 O LEU B 85
SHEET 1 F 5 VAL B 363 LEU B 365 0
SHEET 2 F 5 VAL B 336 HIS B 340 1 N VAL B 338 O ILE B 364
SHEET 3 F 5 PHE B 390 PHE B 394 1 O VAL B 392 N VAL B 339
SHEET 4 F 5 THR B 403 PRO B 408 -1 O SER B 405 N ILE B 393
SHEET 5 F 5 GLN B 422 PRO B 425 -1 O GLN B 422 N VAL B 406
CISPEP 1 GLY A 144 PRO A 145 0 4.62
CISPEP 2 GLY B 144 PRO B 145 0 4.77
SITE 1 AC1 11 GLU A 90 THR A 92 ARG A 120 GLN A 134
SITE 2 AC1 11 GLU A 138 ARG A 265 TYR A 269 TYR A 270
SITE 3 AC1 11 TYR A 294 GLY A 310 TRP A 311
SITE 1 AC2 9 GLU B 90 THR B 92 GLN B 134 GLU B 138
SITE 2 AC2 9 TYR B 269 TYR B 270 TYR B 294 GLY B 310
SITE 3 AC2 9 TRP B 311
CRYST1 70.160 116.360 142.990 90.00 90.00 90.00 P 21 21 21 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 0.014253 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008594 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006993 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
