HEADER LIGASE 16-OCT-03 1R6U
TITLE CRYSTAL STRUCTURE OF AN ACTIVE FRAGMENT OF HUMAN TRYPTOPHANYL-TRNA
TITLE 2 SYNTHETASE WITH CYTOKINE ACTIVITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPTOPHANYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TRYPTOPHAN-TRNA LIGASE, TRPRS, IFP53, HWRS;
COMPND 5 EC: 6.1.1.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: WARS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET20B+
KEYWDS CLASS IC TRNA SYNTHETASE, ROSSMANN FOLD CATALYTIC DOMAIN, ANTICODON
KEYWDS 2 RECOGNITION DOMAIN, BOUND TRP-AMP, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.-L.YANG,F.J.OTERO,R.J.SKENE,D.E.MCREE,L.RIBAS DE POUPLANA,
AUTHOR 2 P.SCHIMMEL
REVDAT 6 27-OCT-21 1R6U 1 REMARK SEQADV LINK
REVDAT 5 13-JUL-11 1R6U 1 VERSN
REVDAT 4 24-FEB-09 1R6U 1 VERSN
REVDAT 3 28-AUG-07 1R6U 1 JRNL
REVDAT 2 22-MAY-07 1R6U 1 JRNL
REVDAT 1 06-JAN-04 1R6U 0
JRNL AUTH X.-L.YANG,M.GUO,M.KAPOOR,K.L.EWALT,F.J.OTERO,R.J.SKENE,
JRNL AUTH 2 D.E.MCREE,P.SCHIMMEL
JRNL TITL FUNCTIONAL AND CRYSTAL STRUCTURE ANALYSIS OF ACTIVE SITE
JRNL TITL 2 ADAPTATIONS OF A POTENT ANTI-ANGIOGENIC HUMAN TRNA
JRNL TITL 3 SYNTHETASE
JRNL REF STRUCTURE V. 15 793 2007
JRNL REFN ISSN 0969-2126
JRNL PMID 17637340
JRNL DOI 10.1016/J.STR.2007.05.009
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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 : 118345
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.254
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5859
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 : 6056
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 100
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) : 6.34200
REMARK 3 B22 (A**2) : -6.46300
REMARK 3 B33 (A**2) : 0.12100
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.33600
REMARK 3 B23 (A**2) : 0.00000
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 54.39
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 : DNA-RNA.PARAM
REMARK 3 PARAMETER FILE 3 : WPA.PARAM
REMARK 3 PARAMETER FILE 4 : GOLN.PARAM
REMARK 3 PARAMETER FILE 5 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R6U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020508.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-DEC-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.02
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91162
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BLU-ICE
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 126480
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : 0.03800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: MODEL DERIVED FROM THE STRUCTURE OF THE FULL
REMARK 200 -LENGTH HUMAN TRPRS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 550, HEPES, PH 7.02, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 279K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 67.32900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.23000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 67.32900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.23000
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: 4520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1085 LIES ON A SPECIAL POSITION.
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 48
REMARK 465 SER A 49
REMARK 465 TYR A 50
REMARK 465 LYS A 51
REMARK 465 ALA A 52
REMARK 465 ALA A 53
REMARK 465 ALA A 54
REMARK 465 GLY A 55
REMARK 465 GLU A 56
REMARK 465 ASP A 57
REMARK 465 TYR A 58
REMARK 465 LYS A 59
REMARK 465 ALA A 60
REMARK 465 ASP A 61
REMARK 465 CYS A 62
REMARK 465 PRO A 63
REMARK 465 PRO A 64
REMARK 465 GLY A 65
REMARK 465 ASN A 66
REMARK 465 PRO A 67
REMARK 465 ALA A 68
REMARK 465 PRO A 69
REMARK 465 THR A 70
REMARK 465 SER A 71
REMARK 465 ASN A 72
REMARK 465 HIS A 73
REMARK 465 GLY A 74
REMARK 465 PRO A 75
REMARK 465 ASP A 76
REMARK 465 ALA A 77
REMARK 465 THR A 78
REMARK 465 GLU A 79
REMARK 465 ALA A 80
REMARK 465 GLU A 81
REMARK 465 PHE A 470
REMARK 465 GLN A 471
REMARK 465 LYS A 472
REMARK 465 LEU A 473
REMARK 465 ALA A 474
REMARK 465 ALA A 475
REMARK 465 ALA A 476
REMARK 465 LEU A 477
REMARK 465 GLU A 478
REMARK 465 HIS A 479
REMARK 465 HIS A 480
REMARK 465 HIS A 481
REMARK 465 HIS A 482
REMARK 465 HIS A 483
REMARK 465 HIS A 484
REMARK 465 MET B 48
REMARK 465 SER B 49
REMARK 465 TYR B 50
REMARK 465 LYS B 51
REMARK 465 ALA B 52
REMARK 465 ALA B 53
REMARK 465 ALA B 54
REMARK 465 GLY B 55
REMARK 465 GLU B 56
REMARK 465 ASP B 57
REMARK 465 TYR B 58
REMARK 465 LYS B 59
REMARK 465 ALA B 60
REMARK 465 ASP B 61
REMARK 465 CYS B 62
REMARK 465 PRO B 63
REMARK 465 PRO B 64
REMARK 465 GLY B 65
REMARK 465 ASN B 66
REMARK 465 PRO B 67
REMARK 465 ALA B 68
REMARK 465 PRO B 69
REMARK 465 THR B 70
REMARK 465 SER B 71
REMARK 465 ASN B 72
REMARK 465 HIS B 73
REMARK 465 GLY B 74
REMARK 465 PRO B 75
REMARK 465 ASP B 76
REMARK 465 ALA B 77
REMARK 465 THR B 78
REMARK 465 GLU B 79
REMARK 465 ALA B 80
REMARK 465 GLU B 81
REMARK 465 GLU B 82
REMARK 465 ASP B 83
REMARK 465 PHE B 84
REMARK 465 VAL B 85
REMARK 465 ASP B 86
REMARK 465 PRO B 87
REMARK 465 TRP B 88
REMARK 465 THR B 89
REMARK 465 VAL B 90
REMARK 465 GLN B 91
REMARK 465 THR B 92
REMARK 465 SER B 93
REMARK 465 SER B 94
REMARK 465 ALA B 95
REMARK 465 LYS B 96
REMARK 465 ALA B 346
REMARK 465 GLN B 347
REMARK 465 THR B 348
REMARK 465 LYS B 349
REMARK 465 MSE B 350
REMARK 465 SER B 351
REMARK 465 ALA B 352
REMARK 465 SER B 353
REMARK 465 ASP B 354
REMARK 465 PHE B 468
REMARK 465 ASP B 469
REMARK 465 PHE B 470
REMARK 465 GLN B 471
REMARK 465 LYS B 472
REMARK 465 LEU B 473
REMARK 465 ALA B 474
REMARK 465 ALA B 475
REMARK 465 ALA B 476
REMARK 465 LEU B 477
REMARK 465 GLU B 478
REMARK 465 HIS B 479
REMARK 465 HIS B 480
REMARK 465 HIS B 481
REMARK 465 HIS B 482
REMARK 465 HIS B 483
REMARK 465 HIS B 484
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 LEU A 430 N - CA - C ANGL. DEV. = -22.5 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 87 -8.40 -49.42
REMARK 500 ASP A 101 -14.47 77.80
REMARK 500 ALA A 168 -150.48 -53.86
REMARK 500 MSE A 169 84.64 76.02
REMARK 500 LYS A 204 -165.34 -108.11
REMARK 500 ARG A 298 -110.62 59.31
REMARK 500 ALA A 346 21.27 -77.86
REMARK 500 PRO A 355 -80.93 -43.12
REMARK 500 LEU A 361 7.80 -69.43
REMARK 500 ALA A 376 109.03 -59.22
REMARK 500 ARG A 381 150.25 -29.97
REMARK 500 GLU A 429 57.20 10.88
REMARK 500 SER A 467 37.26 -67.50
REMARK 500 ASP B 99 107.87 73.04
REMARK 500 ARG B 134 -7.18 -170.16
REMARK 500 ASP B 142 19.63 59.44
REMARK 500 ASN B 152 33.12 -90.63
REMARK 500 PRO B 164 123.83 -36.93
REMARK 500 LYS B 231 24.07 -150.70
REMARK 500 ARG B 298 -121.51 66.74
REMARK 500 ILE B 303 101.44 -55.38
REMARK 500 LEU B 343 -78.59 -47.48
REMARK 500 VAL B 372 -73.90 -61.47
REMARK 500 LEU B 466 -169.93 -106.43
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 TYM A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R6T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FULL-LENGTH HUMAN TRYPTOPHANYL-TRNA
REMARK 900 SYNTHETASE
REMARK 900 RELATED ID: 1N3L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN ACTIVE FRAGMENT OF HUMAN TYROSYL-TRNA
REMARK 900 SYNTHETASE WITH CYTOKINE ACTIVITY
REMARK 900 RELATED ID: 1NTG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN EMAP-II LIKE CYTOKINE RELEASED FROM HUMAN
REMARK 900 TYROSYL-TRNA SYNTHETASE
DBREF 1R6U A 48 471 UNP P23381 SYW_HUMAN 48 471
DBREF 1R6U B 48 471 UNP P23381 SYW_HUMAN 48 471
SEQADV 1R6U MSE A 143 UNP P23381 MET 143 MODIFIED RESIDUE
SEQADV 1R6U MSE A 169 UNP P23381 MET 169 MODIFIED RESIDUE
SEQADV 1R6U MSE A 195 UNP P23381 MET 195 MODIFIED RESIDUE
SEQADV 1R6U GLY A 213 UNP P23381 SER 213 ENGINEERED MUTATION
SEQADV 1R6U ASP A 214 UNP P23381 TYR 214 ENGINEERED MUTATION
SEQADV 1R6U MSE A 241 UNP P23381 MET 241 MODIFIED RESIDUE
SEQADV 1R6U MSE A 243 UNP P23381 MET 243 MODIFIED RESIDUE
SEQADV 1R6U MSE A 319 UNP P23381 MET 319 MODIFIED RESIDUE
SEQADV 1R6U MSE A 350 UNP P23381 MET 350 MODIFIED RESIDUE
SEQADV 1R6U MSE A 401 UNP P23381 MET 401 MODIFIED RESIDUE
SEQADV 1R6U MSE A 425 UNP P23381 MET 425 MODIFIED RESIDUE
SEQADV 1R6U MSE A 461 UNP P23381 MET 461 MODIFIED RESIDUE
SEQADV 1R6U LYS A 472 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U LEU A 473 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U ALA A 474 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U ALA A 475 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U ALA A 476 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U LEU A 477 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U GLU A 478 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U HIS A 479 UNP P23381 EXPRESSION TAG
SEQADV 1R6U HIS A 480 UNP P23381 EXPRESSION TAG
SEQADV 1R6U HIS A 481 UNP P23381 EXPRESSION TAG
SEQADV 1R6U HIS A 482 UNP P23381 EXPRESSION TAG
SEQADV 1R6U HIS A 483 UNP P23381 EXPRESSION TAG
SEQADV 1R6U HIS A 484 UNP P23381 EXPRESSION TAG
SEQADV 1R6U MSE B 143 UNP P23381 MET 143 MODIFIED RESIDUE
SEQADV 1R6U MSE B 169 UNP P23381 MET 169 MODIFIED RESIDUE
SEQADV 1R6U MSE B 195 UNP P23381 MET 195 MODIFIED RESIDUE
SEQADV 1R6U GLY B 213 UNP P23381 SER 213 ENGINEERED MUTATION
SEQADV 1R6U ASP B 214 UNP P23381 TYR 214 ENGINEERED MUTATION
SEQADV 1R6U MSE B 241 UNP P23381 MET 241 MODIFIED RESIDUE
SEQADV 1R6U MSE B 243 UNP P23381 MET 243 MODIFIED RESIDUE
SEQADV 1R6U MSE B 319 UNP P23381 MET 319 MODIFIED RESIDUE
SEQADV 1R6U MSE B 350 UNP P23381 MET 350 MODIFIED RESIDUE
SEQADV 1R6U MSE B 401 UNP P23381 MET 401 MODIFIED RESIDUE
SEQADV 1R6U MSE B 425 UNP P23381 MET 425 MODIFIED RESIDUE
SEQADV 1R6U MSE B 461 UNP P23381 MET 461 MODIFIED RESIDUE
SEQADV 1R6U LYS B 472 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U LEU B 473 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U ALA B 474 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U ALA B 475 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U ALA B 476 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U LEU B 477 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U GLU B 478 UNP P23381 CLONING ARTIFACT
SEQADV 1R6U HIS B 479 UNP P23381 EXPRESSION TAG
SEQADV 1R6U HIS B 480 UNP P23381 EXPRESSION TAG
SEQADV 1R6U HIS B 481 UNP P23381 EXPRESSION TAG
SEQADV 1R6U HIS B 482 UNP P23381 EXPRESSION TAG
SEQADV 1R6U HIS B 483 UNP P23381 EXPRESSION TAG
SEQADV 1R6U HIS B 484 UNP P23381 EXPRESSION TAG
SEQRES 1 A 437 MET SER TYR LYS ALA ALA ALA GLY GLU ASP TYR LYS ALA
SEQRES 2 A 437 ASP CYS PRO PRO GLY ASN PRO ALA PRO THR SER ASN HIS
SEQRES 3 A 437 GLY PRO ASP ALA THR GLU ALA GLU GLU ASP PHE VAL ASP
SEQRES 4 A 437 PRO TRP THR VAL GLN THR SER SER ALA LYS GLY ILE ASP
SEQRES 5 A 437 TYR ASP LYS LEU ILE VAL ARG PHE GLY SER SER LYS ILE
SEQRES 6 A 437 ASP LYS GLU LEU ILE ASN ARG ILE GLU ARG ALA THR GLY
SEQRES 7 A 437 GLN ARG PRO HIS HIS PHE LEU ARG ARG GLY ILE PHE PHE
SEQRES 8 A 437 SER HIS ARG ASP MSE ASN GLN VAL LEU ASP ALA TYR GLU
SEQRES 9 A 437 ASN LYS LYS PRO PHE TYR LEU TYR THR GLY ARG GLY PRO
SEQRES 10 A 437 SER SER GLU ALA MSE HIS VAL GLY HIS LEU ILE PRO PHE
SEQRES 11 A 437 ILE PHE THR LYS TRP LEU GLN ASP VAL PHE ASN VAL PRO
SEQRES 12 A 437 LEU VAL ILE GLN MSE THR ASP ASP GLU LYS TYR LEU TRP
SEQRES 13 A 437 LYS ASP LEU THR LEU ASP GLN ALA TYR GLY ASP ALA VAL
SEQRES 14 A 437 GLU ASN ALA LYS ASP ILE ILE ALA CYS GLY PHE ASP ILE
SEQRES 15 A 437 ASN LYS THR PHE ILE PHE SER ASP LEU ASP TYR MSE GLY
SEQRES 16 A 437 MSE SER SER GLY PHE TYR LYS ASN VAL VAL LYS ILE GLN
SEQRES 17 A 437 LYS HIS VAL THR PHE ASN GLN VAL LYS GLY ILE PHE GLY
SEQRES 18 A 437 PHE THR ASP SER ASP CYS ILE GLY LYS ILE SER PHE PRO
SEQRES 19 A 437 ALA ILE GLN ALA ALA PRO SER PHE SER ASN SER PHE PRO
SEQRES 20 A 437 GLN ILE PHE ARG ASP ARG THR ASP ILE GLN CYS LEU ILE
SEQRES 21 A 437 PRO CYS ALA ILE ASP GLN ASP PRO TYR PHE ARG MSE THR
SEQRES 22 A 437 ARG ASP VAL ALA PRO ARG ILE GLY TYR PRO LYS PRO ALA
SEQRES 23 A 437 LEU LEU HIS SER THR PHE PHE PRO ALA LEU GLN GLY ALA
SEQRES 24 A 437 GLN THR LYS MSE SER ALA SER ASP PRO ASN SER SER ILE
SEQRES 25 A 437 PHE LEU THR ASP THR ALA LYS GLN ILE LYS THR LYS VAL
SEQRES 26 A 437 ASN LYS HIS ALA PHE SER GLY GLY ARG ASP THR ILE GLU
SEQRES 27 A 437 GLU HIS ARG GLN PHE GLY GLY ASN CYS ASP VAL ASP VAL
SEQRES 28 A 437 SER PHE MSE TYR LEU THR PHE PHE LEU GLU ASP ASP ASP
SEQRES 29 A 437 LYS LEU GLU GLN ILE ARG LYS ASP TYR THR SER GLY ALA
SEQRES 30 A 437 MSE LEU THR GLY GLU LEU LYS LYS ALA LEU ILE GLU VAL
SEQRES 31 A 437 LEU GLN PRO LEU ILE ALA GLU HIS GLN ALA ARG ARG LYS
SEQRES 32 A 437 GLU VAL THR ASP GLU ILE VAL LYS GLU PHE MSE THR PRO
SEQRES 33 A 437 ARG LYS LEU SER PHE ASP PHE GLN LYS LEU ALA ALA ALA
SEQRES 34 A 437 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 437 MET SER TYR LYS ALA ALA ALA GLY GLU ASP TYR LYS ALA
SEQRES 2 B 437 ASP CYS PRO PRO GLY ASN PRO ALA PRO THR SER ASN HIS
SEQRES 3 B 437 GLY PRO ASP ALA THR GLU ALA GLU GLU ASP PHE VAL ASP
SEQRES 4 B 437 PRO TRP THR VAL GLN THR SER SER ALA LYS GLY ILE ASP
SEQRES 5 B 437 TYR ASP LYS LEU ILE VAL ARG PHE GLY SER SER LYS ILE
SEQRES 6 B 437 ASP LYS GLU LEU ILE ASN ARG ILE GLU ARG ALA THR GLY
SEQRES 7 B 437 GLN ARG PRO HIS HIS PHE LEU ARG ARG GLY ILE PHE PHE
SEQRES 8 B 437 SER HIS ARG ASP MSE ASN GLN VAL LEU ASP ALA TYR GLU
SEQRES 9 B 437 ASN LYS LYS PRO PHE TYR LEU TYR THR GLY ARG GLY PRO
SEQRES 10 B 437 SER SER GLU ALA MSE HIS VAL GLY HIS LEU ILE PRO PHE
SEQRES 11 B 437 ILE PHE THR LYS TRP LEU GLN ASP VAL PHE ASN VAL PRO
SEQRES 12 B 437 LEU VAL ILE GLN MSE THR ASP ASP GLU LYS TYR LEU TRP
SEQRES 13 B 437 LYS ASP LEU THR LEU ASP GLN ALA TYR GLY ASP ALA VAL
SEQRES 14 B 437 GLU ASN ALA LYS ASP ILE ILE ALA CYS GLY PHE ASP ILE
SEQRES 15 B 437 ASN LYS THR PHE ILE PHE SER ASP LEU ASP TYR MSE GLY
SEQRES 16 B 437 MSE SER SER GLY PHE TYR LYS ASN VAL VAL LYS ILE GLN
SEQRES 17 B 437 LYS HIS VAL THR PHE ASN GLN VAL LYS GLY ILE PHE GLY
SEQRES 18 B 437 PHE THR ASP SER ASP CYS ILE GLY LYS ILE SER PHE PRO
SEQRES 19 B 437 ALA ILE GLN ALA ALA PRO SER PHE SER ASN SER PHE PRO
SEQRES 20 B 437 GLN ILE PHE ARG ASP ARG THR ASP ILE GLN CYS LEU ILE
SEQRES 21 B 437 PRO CYS ALA ILE ASP GLN ASP PRO TYR PHE ARG MSE THR
SEQRES 22 B 437 ARG ASP VAL ALA PRO ARG ILE GLY TYR PRO LYS PRO ALA
SEQRES 23 B 437 LEU LEU HIS SER THR PHE PHE PRO ALA LEU GLN GLY ALA
SEQRES 24 B 437 GLN THR LYS MSE SER ALA SER ASP PRO ASN SER SER ILE
SEQRES 25 B 437 PHE LEU THR ASP THR ALA LYS GLN ILE LYS THR LYS VAL
SEQRES 26 B 437 ASN LYS HIS ALA PHE SER GLY GLY ARG ASP THR ILE GLU
SEQRES 27 B 437 GLU HIS ARG GLN PHE GLY GLY ASN CYS ASP VAL ASP VAL
SEQRES 28 B 437 SER PHE MSE TYR LEU THR PHE PHE LEU GLU ASP ASP ASP
SEQRES 29 B 437 LYS LEU GLU GLN ILE ARG LYS ASP TYR THR SER GLY ALA
SEQRES 30 B 437 MSE LEU THR GLY GLU LEU LYS LYS ALA LEU ILE GLU VAL
SEQRES 31 B 437 LEU GLN PRO LEU ILE ALA GLU HIS GLN ALA ARG ARG LYS
SEQRES 32 B 437 GLU VAL THR ASP GLU ILE VAL LYS GLU PHE MSE THR PRO
SEQRES 33 B 437 ARG LYS LEU SER PHE ASP PHE GLN LYS LEU ALA ALA ALA
SEQRES 34 B 437 LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 1R6U MSE A 143 MET SELENOMETHIONINE
MODRES 1R6U MSE A 169 MET SELENOMETHIONINE
MODRES 1R6U MSE A 195 MET SELENOMETHIONINE
MODRES 1R6U MSE A 241 MET SELENOMETHIONINE
MODRES 1R6U MSE A 243 MET SELENOMETHIONINE
MODRES 1R6U MSE A 319 MET SELENOMETHIONINE
MODRES 1R6U MSE A 350 MET SELENOMETHIONINE
MODRES 1R6U MSE A 401 MET SELENOMETHIONINE
MODRES 1R6U MSE A 425 MET SELENOMETHIONINE
MODRES 1R6U MSE A 461 MET SELENOMETHIONINE
MODRES 1R6U MSE B 143 MET SELENOMETHIONINE
MODRES 1R6U MSE B 169 MET SELENOMETHIONINE
MODRES 1R6U MSE B 195 MET SELENOMETHIONINE
MODRES 1R6U MSE B 241 MET SELENOMETHIONINE
MODRES 1R6U MSE B 243 MET SELENOMETHIONINE
MODRES 1R6U MSE B 319 MET SELENOMETHIONINE
MODRES 1R6U MSE B 401 MET SELENOMETHIONINE
MODRES 1R6U MSE B 425 MET SELENOMETHIONINE
MODRES 1R6U MSE B 461 MET SELENOMETHIONINE
HET MSE A 143 8
HET MSE A 169 8
HET MSE A 195 8
HET MSE A 241 8
HET MSE A 243 8
HET MSE A 319 8
HET MSE A 350 8
HET MSE A 401 8
HET MSE A 425 8
HET MSE A 461 8
HET MSE B 143 8
HET MSE B 169 8
HET MSE B 195 8
HET MSE B 241 8
HET MSE B 243 8
HET MSE B 319 8
HET MSE B 401 8
HET MSE B 425 8
HET MSE B 461 8
HET TYM A 501 37
HET GOL A 601 6
HET GOL A 602 6
HETNAM MSE SELENOMETHIONINE
HETNAM TYM TRYPTOPHANYL-5'AMP
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 19(C5 H11 N O2 SE)
FORMUL 3 TYM C21 H24 N7 O8 P
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 6 HOH *100(H2 O)
HELIX 1 1 LYS A 102 PHE A 107 1 6
HELIX 2 2 ASP A 113 GLY A 125 1 13
HELIX 3 3 HIS A 129 ARG A 134 1 6
HELIX 4 4 ASP A 142 GLU A 151 1 10
HELIX 5 5 HIS A 170 ASN A 188 1 19
HELIX 6 6 THR A 196 LYS A 204 1 9
HELIX 7 7 THR A 207 ALA A 224 1 18
HELIX 8 8 ASP A 228 ASN A 230 5 3
HELIX 9 9 ASP A 237 MSE A 241 1 5
HELIX 10 10 GLY A 242 SER A 244 5 3
HELIX 11 11 GLY A 246 HIS A 257 1 12
HELIX 12 12 THR A 259 GLY A 268 1 10
HELIX 13 13 CYS A 274 ALA A 286 1 13
HELIX 14 14 PRO A 287 SER A 292 5 6
HELIX 15 15 PHE A 293 ARG A 298 1 6
HELIX 16 16 GLN A 313 ALA A 324 1 12
HELIX 17 17 PRO A 325 GLY A 328 5 4
HELIX 18 18 THR A 364 HIS A 375 1 12
HELIX 19 19 THR A 383 GLY A 391 1 9
HELIX 20 20 ASP A 397 LEU A 407 1 11
HELIX 21 21 ASP A 409 GLY A 423 1 15
HELIX 22 22 GLU A 429 GLU A 451 1 23
HELIX 23 23 THR A 453 MSE A 461 1 9
HELIX 24 24 TYR B 100 GLY B 108 1 9
HELIX 25 25 ASP B 113 GLY B 125 1 13
HELIX 26 26 ASP B 142 ASN B 152 1 11
HELIX 27 27 HIS B 170 GLY B 172 5 3
HELIX 28 28 HIS B 173 ASN B 188 1 16
HELIX 29 29 THR B 196 LYS B 204 1 9
HELIX 30 30 THR B 207 CYS B 225 1 19
HELIX 31 31 ASP B 237 MSE B 241 1 5
HELIX 32 32 GLY B 242 SER B 244 5 3
HELIX 33 33 GLY B 246 HIS B 257 1 12
HELIX 34 34 THR B 259 GLY B 268 1 10
HELIX 35 35 CYS B 274 ALA B 286 1 13
HELIX 36 36 PRO B 287 SER B 292 5 6
HELIX 37 37 PHE B 293 ARG B 298 1 6
HELIX 38 38 GLN B 313 ILE B 327 1 15
HELIX 39 39 THR B 364 ALA B 376 1 13
HELIX 40 40 THR B 383 GLY B 391 1 9
HELIX 41 41 ASP B 397 LEU B 407 1 11
HELIX 42 42 ASP B 409 GLY B 423 1 15
HELIX 43 43 LEU B 426 GLU B 451 1 26
HELIX 44 44 THR B 453 MSE B 461 1 9
SHEET 1 A 2 PHE A 84 ASP A 86 0
SHEET 2 A 2 THR A 89 GLN A 91 -1 O GLN A 91 N PHE A 84
SHEET 1 B 7 SER A 110 LYS A 111 0
SHEET 2 B 7 PHE A 137 ARG A 141 -1 O HIS A 140 N SER A 110
SHEET 3 B 7 ALA A 333 SER A 337 -1 O HIS A 336 N SER A 139
SHEET 4 B 7 GLN A 304 ALA A 310 1 N ILE A 307 O ALA A 333
SHEET 5 B 7 PHE A 156 ARG A 162 1 N TYR A 157 O LEU A 306
SHEET 6 B 7 LEU A 191 MSE A 195 1 O GLN A 194 N ARG A 162
SHEET 7 B 7 THR A 232 SER A 236 1 O PHE A 233 N ILE A 193
SHEET 1 C 2 PRO A 341 ALA A 342 0
SHEET 2 C 2 GLY A 345 LYS A 349 -1 O THR A 348 N ALA A 342
SHEET 1 D 7 SER B 110 LYS B 111 0
SHEET 2 D 7 SER B 139 ARG B 141 -1 O HIS B 140 N SER B 110
SHEET 3 D 7 ALA B 333 SER B 337 -1 O LEU B 334 N ARG B 141
SHEET 4 D 7 CYS B 305 ALA B 310 1 N CYS B 309 O LEU B 335
SHEET 5 D 7 TYR B 157 ARG B 162 1 N TYR B 157 O LEU B 306
SHEET 6 D 7 LEU B 191 MSE B 195 1 O VAL B 192 N LEU B 158
SHEET 7 D 7 THR B 232 SER B 236 1 O PHE B 233 N LEU B 191
LINK C ASP A 142 N MSE A 143 1555 1555 1.33
LINK C MSE A 143 N ASN A 144 1555 1555 1.33
LINK C ALA A 168 N MSE A 169 1555 1555 1.33
LINK C MSE A 169 N HIS A 170 1555 1555 1.33
LINK C GLN A 194 N MSE A 195 1555 1555 1.33
LINK C MSE A 195 N THR A 196 1555 1555 1.33
LINK C TYR A 240 N MSE A 241 1555 1555 1.33
LINK C MSE A 241 N GLY A 242 1555 1555 1.33
LINK C GLY A 242 N MSE A 243 1555 1555 1.33
LINK C MSE A 243 N SER A 244 1555 1555 1.33
LINK C ARG A 318 N MSE A 319 1555 1555 1.33
LINK C MSE A 319 N THR A 320 1555 1555 1.33
LINK C LYS A 349 N MSE A 350 1555 1555 1.33
LINK C MSE A 350 N SER A 351 1555 1555 1.33
LINK C PHE A 400 N MSE A 401 1555 1555 1.33
LINK C MSE A 401 N TYR A 402 1555 1555 1.33
LINK C ALA A 424 N MSE A 425 1555 1555 1.33
LINK C MSE A 425 N LEU A 426 1555 1555 1.32
LINK C PHE A 460 N MSE A 461 1555 1555 1.33
LINK C MSE A 461 N THR A 462 1555 1555 1.33
LINK C ASP B 142 N MSE B 143 1555 1555 1.33
LINK C MSE B 143 N ASN B 144 1555 1555 1.33
LINK C ALA B 168 N MSE B 169 1555 1555 1.32
LINK C MSE B 169 N HIS B 170 1555 1555 1.33
LINK C GLN B 194 N MSE B 195 1555 1555 1.33
LINK C MSE B 195 N THR B 196 1555 1555 1.32
LINK C TYR B 240 N MSE B 241 1555 1555 1.33
LINK C MSE B 241 N GLY B 242 1555 1555 1.33
LINK C GLY B 242 N MSE B 243 1555 1555 1.33
LINK C MSE B 243 N SER B 244 1555 1555 1.33
LINK C ARG B 318 N MSE B 319 1555 1555 1.33
LINK C MSE B 319 N THR B 320 1555 1555 1.33
LINK C PHE B 400 N MSE B 401 1555 1555 1.33
LINK C MSE B 401 N TYR B 402 1555 1555 1.33
LINK C ALA B 424 N MSE B 425 1555 1555 1.33
LINK C MSE B 425 N LEU B 426 1555 1555 1.33
LINK C PHE B 460 N MSE B 461 1555 1555 1.34
LINK C MSE B 461 N THR B 462 1555 1555 1.32
SITE 1 AC1 22 TYR A 159 THR A 160 GLY A 161 ARG A 162
SITE 2 AC1 22 GLY A 163 GLY A 172 HIS A 173 PRO A 176
SITE 3 AC1 22 GLN A 194 GLU A 199 GLN A 284 ILE A 307
SITE 4 AC1 22 CYS A 309 ALA A 310 ASP A 312 GLN A 313
SITE 5 AC1 22 PHE A 317 PHE A 340 LYS A 349 MSE A 350
SITE 6 AC1 22 HOH A1012 HOH A1046
SITE 1 AC2 4 TYR A 201 THR A 207 LEU A 208 LYS B 253
SITE 1 AC3 5 HIS A 129 ILE A 178 LYS A 181 TRP A 182
SITE 2 AC3 5 ASP A 185
CRYST1 134.658 96.460 97.132 90.00 129.90 90.00 C 1 2 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 0.007426 0.000000 0.006209 0.00000
SCALE2 0.000000 0.010367 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013420 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
