HEADER LIGASE/LIGASE INHIBITOR 15-MAR-15 4YRF
TITLE CRYSTAL STRUCTURE OF T. CRUZI HISTIDYL-TRNA SYNTHETASE IN COMPLEX WITH
TITLE 2 5-BROMOPYRIDIN-2(1H)-ONE (CHEM 148)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTIDYL-TRNA SYNTHETASE, PUTATIVE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 45-478;
COMPND 5 EC: 6.1.1.21;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI (STRAIN CL BRENER);
SOURCE 3 ORGANISM_TAXID: 353153;
SOURCE 4 STRAIN: CL BRENER;
SOURCE 5 GENE: TC00.1047053507019.40;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS LIGASE, AMINOACYL-TRNA SYNTHETASE, AARS, HISRS, TRYPANOSOMA CRUZI,
KEYWDS 2 PROTEIN-INHIBITOR COMPLEX, LIGASE-LIGASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-Y.KOH,W.G.J.HOL
REVDAT 2 27-SEP-23 4YRF 1 REMARK
REVDAT 1 19-AUG-15 4YRF 0
JRNL AUTH C.Y.KOH,L.KALLUR SIDDARAMAIAH,R.M.RANADE,J.NGUYEN,T.JIAN,
JRNL AUTH 2 Z.ZHANG,J.R.GILLESPIE,F.S.BUCKNER,C.L.VERLINDE,E.FAN,W.G.HOL
JRNL TITL A BINDING HOTSPOT IN TRYPANOSOMA CRUZI HISTIDYL-TRNA
JRNL TITL 2 SYNTHETASE REVEALED BY FRAGMENT-BASED CRYSTALLOGRAPHIC
JRNL TITL 3 COCKTAIL SCREENS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 71 1684 2015
JRNL REFN ESSN 1399-0047
JRNL PMID 26249349
JRNL DOI 10.1107/S1399004715007683
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 23499
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1293
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3127
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 152
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.54000
REMARK 3 B22 (A**2) : 5.98000
REMARK 3 B33 (A**2) : -1.44000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.272
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.221
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.226
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.572
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4YRF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207946.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8 TO 5.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : VARIMAX HF (OSMIC)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.6
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24799
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 28.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.37400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 3LC0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 23 % TO 28 %
REMARK 280 PEG 3350, 0.1 M SODIUM CITRATE PH 4.8 TO 5.3, 1 MM TCEP, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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+1/2
REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2
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 30.84088
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.40700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 32.95880
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 30.84088
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 59.40700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 32.95880
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: 10280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 126.11476
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 65.91761
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 A 601 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 -21
REMARK 465 ALA A -20
REMARK 465 HIS 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 MET A -13
REMARK 465 GLY A -12
REMARK 465 THR A -11
REMARK 465 LEU A -10
REMARK 465 GLU A -9
REMARK 465 ALA A -8
REMARK 465 GLN A -7
REMARK 465 THR A -6
REMARK 465 GLN A -5
REMARK 465 GLY A -4
REMARK 465 PRO A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 MET A 0
REMARK 465 GLN A 45
REMARK 465 LYS A 46
REMARK 465 ASN A 47
REMARK 465 ALA A 159
REMARK 465 ILE A 160
REMARK 465 THR A 161
REMARK 465 ARG A 162
REMARK 465 GLY A 163
REMARK 465 VAL A 224
REMARK 465 LYS A 241
REMARK 465 ILE A 242
REMARK 465 PRO A 243
REMARK 465 GLU A 257
REMARK 465 PRO A 258
REMARK 465 GLU A 457
REMARK 465 GLY A 458
REMARK 465 THR A 459
REMARK 465 GLY A 460
REMARK 465 LYS A 461
REMARK 465 GLU A 462
REMARK 465 GLU A 463
REMARK 465 GLY A 464
REMARK 465 GLY A 465
REMARK 465 ALA A 466
REMARK 465 GLU A 467
REMARK 465 ARG A 468
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 LYS A 116 CG CD CE NZ
REMARK 470 LEU A 136 CG CD1 CD2
REMARK 470 GLU A 158 CG CD OE1 OE2
REMARK 470 ARG A 164 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 179 CG CD CE NZ
REMARK 470 GLU A 220 CG CD OE1 OE2
REMARK 470 LYS A 228 CG CD CE NZ
REMARK 470 GLU A 240 CG CD OE1 OE2
REMARK 470 ARG A 244 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 245 CG CD OE1 OE2
REMARK 470 GLU A 246 CG CD OE1 OE2
REMARK 470 VAL A 247 CG1 CG2
REMARK 470 GLU A 248 CG CD OE1 OE2
REMARK 470 GLN A 250 CG CD OE1 NE2
REMARK 470 LEU A 251 CG CD1 CD2
REMARK 470 VAL A 253 CG1 CG2
REMARK 470 LEU A 254 CG CD1 CD2
REMARK 470 LEU A 256 CG CD1 CD2
REMARK 470 VAL A 260 CG1 CG2
REMARK 470 LYS A 271 CG CD CE NZ
REMARK 470 VAL A 280 CG1 CG2
REMARK 470 GLU A 283 CG CD OE1 OE2
REMARK 470 ARG A 334 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 379 CG OD1 OD2
REMARK 470 GLU A 443 CG CD OE1 OE2
REMARK 470 GLU A 446 CG CD OE1 OE2
REMARK 470 PHE A 470 CG CD1 CD2 CE1 CE2 CZ
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 LYS A 101 61.91 36.16
REMARK 500 ALA A 102 17.57 -145.49
REMARK 500 GLN A 109 43.04 -94.70
REMARK 500 ARG A 314 155.23 70.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 752 DISTANCE = 5.87 ANGSTROMS
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 4HS A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YP0 RELATED DB: PDB
REMARK 900 RELATED ID: 4YPF RELATED DB: PDB
REMARK 900 RELATED ID: 4YRC RELATED DB: PDB
REMARK 900 RELATED ID: 4YRE RELATED DB: PDB
REMARK 900 RELATED ID: 4YRG RELATED DB: PDB
REMARK 900 RELATED ID: 4YRI RELATED DB: PDB
REMARK 900 RELATED ID: 4YRJ RELATED DB: PDB
REMARK 900 RELATED ID: 4YRK RELATED DB: PDB
REMARK 900 RELATED ID: 4YRL RELATED DB: PDB
REMARK 900 RELATED ID: 4YRM RELATED DB: PDB
REMARK 900 RELATED ID: 4YRN RELATED DB: PDB
REMARK 900 RELATED ID: 4YRO RELATED DB: PDB
REMARK 900 RELATED ID: 4YRP RELATED DB: PDB
REMARK 900 RELATED ID: 4YRQ RELATED DB: PDB
REMARK 900 RELATED ID: 4YRR RELATED DB: PDB
REMARK 900 RELATED ID: 4YRS RELATED DB: PDB
REMARK 900 RELATED ID: 4YRT RELATED DB: PDB
DBREF 4YRF A 45 478 UNP Q4DA54 Q4DA54_TRYCC 45 478
SEQADV 4YRF MET A -21 UNP Q4DA54 INITIATING METHIONINE
SEQADV 4YRF ALA A -20 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF HIS A -19 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF HIS A -18 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF HIS A -17 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF HIS A -16 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF HIS A -15 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF HIS A -14 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF MET A -13 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF GLY A -12 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF THR A -11 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF LEU A -10 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF GLU A -9 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF ALA A -8 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF GLN A -7 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF THR A -6 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF GLN A -5 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF GLY A -4 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF PRO A -3 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF GLY A -2 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF SER A -1 UNP Q4DA54 EXPRESSION TAG
SEQADV 4YRF MET A 0 UNP Q4DA54 EXPRESSION TAG
SEQRES 1 A 456 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 A 456 ALA GLN THR GLN GLY PRO GLY SER MET GLN LYS ASN MET
SEQRES 3 A 456 VAL GLU THR GLU PRO VAL GLN GLY CYS ARG ASP PHE PRO
SEQRES 4 A 456 PRO GLU ALA MET ARG CYS ARG ARG HIS LEU PHE ASP VAL
SEQRES 5 A 456 PHE HIS ALA THR ALA LYS THR PHE GLY PHE GLU GLU TYR
SEQRES 6 A 456 ASP ALA PRO VAL LEU GLU SER GLU GLU LEU TYR ILE ARG
SEQRES 7 A 456 LYS ALA GLY GLU GLU ILE THR GLU GLN MET PHE ASN PHE
SEQRES 8 A 456 ILE THR LYS GLY GLY HIS ARG VAL ALA LEU ARG PRO GLU
SEQRES 9 A 456 MET THR PRO SER LEU ALA ARG LEU LEU LEU GLY LYS GLY
SEQRES 10 A 456 ARG SER LEU LEU LEU PRO ALA LYS TRP TYR SER ILE PRO
SEQRES 11 A 456 GLN CYS TRP ARG TYR GLU ALA ILE THR ARG GLY ARG ARG
SEQRES 12 A 456 ARG GLU HIS TYR GLN TRP ASN MET ASP ILE VAL GLY VAL
SEQRES 13 A 456 LYS SER VAL SER ALA GLU VAL GLU LEU VAL CYS ALA ALA
SEQRES 14 A 456 CYS TRP ALA MET ARG SER LEU GLY LEU SER SER LYS ASP
SEQRES 15 A 456 VAL GLY ILE LYS VAL ASN SER ARG LYS VAL LEU GLN THR
SEQRES 16 A 456 VAL VAL GLU GLN ALA GLY VAL THR SER ASP LYS PHE ALA
SEQRES 17 A 456 PRO VAL CYS VAL ILE VAL ASP LYS MET GLU LYS ILE PRO
SEQRES 18 A 456 ARG GLU GLU VAL GLU ALA GLN LEU ALA VAL LEU GLY LEU
SEQRES 19 A 456 GLU PRO THR VAL VAL ASP ALA ILE THR THR THR LEU SER
SEQRES 20 A 456 LEU LYS SER ILE ASP GLU ILE ALA GLN ARG VAL GLY GLU
SEQRES 21 A 456 GLU HIS GLU ALA VAL LYS GLU LEU ARG GLN PHE PHE GLU
SEQRES 22 A 456 GLN VAL GLU ALA TYR GLY TYR GLY ASP TRP VAL LEU PHE
SEQRES 23 A 456 ASP ALA SER VAL VAL ARG GLY LEU ALA TYR TYR THR GLY
SEQRES 24 A 456 ILE VAL PHE GLU GLY PHE ASP ARG GLU GLY LYS PHE ARG
SEQRES 25 A 456 ALA LEU CYS GLY GLY GLY ARG TYR ASP ASN LEU LEU THR
SEQRES 26 A 456 THR TYR GLY SER PRO THR PRO ILE PRO CYS ALA GLY PHE
SEQRES 27 A 456 GLY PHE GLY ASP CYS VAL ILE VAL GLU LEU LEU GLN GLU
SEQRES 28 A 456 LYS ARG LEU LEU PRO ASP ILE PRO HIS VAL VAL ASP ASP
SEQRES 29 A 456 VAL VAL ILE PRO PHE ASP GLU SER MET ARG PRO HIS ALA
SEQRES 30 A 456 LEU ALA VAL LEU ARG ARG LEU ARG ASP ALA GLY ARG SER
SEQRES 31 A 456 ALA ASP ILE ILE LEU ASP LYS LYS LYS VAL VAL GLN ALA
SEQRES 32 A 456 PHE ASN TYR ALA ASP ARG VAL GLY ALA VAL ARG ALA VAL
SEQRES 33 A 456 LEU VAL ALA PRO GLU GLU TRP GLU ARG GLY GLU VAL GLN
SEQRES 34 A 456 VAL LYS MET LEU ARG GLU GLY THR GLY LYS GLU GLU GLY
SEQRES 35 A 456 GLY ALA GLU ARG GLY PHE ALA VAL PRO LEU ASP ARG LEU
SEQRES 36 A 456 VAL
HET HIS A 501 11
HET 4HS A 502 8
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 A 505 5
HET DMS A 506 4
HET DMS A 507 4
HET EDO A 508 4
HETNAM HIS HISTIDINE
HETNAM 4HS 5-BROMOPYRIDIN-2(1H)-ONE
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 HIS C6 H10 N3 O2 1+
FORMUL 3 4HS C5 H4 BR N O
FORMUL 4 SO4 3(O4 S 2-)
FORMUL 7 DMS 2(C2 H6 O S)
FORMUL 9 EDO C2 H6 O2
FORMUL 10 HOH *152(H2 O)
HELIX 1 AA1 PRO A 61 PHE A 82 1 22
HELIX 2 AA2 GLU A 96 ILE A 99 5 4
HELIX 3 AA3 GLU A 104 GLN A 109 1 6
HELIX 4 AA4 MET A 127 GLY A 139 1 13
HELIX 5 AA5 ARG A 140 LEU A 142 5 3
HELIX 6 AA6 VAL A 181 LEU A 198 1 18
HELIX 7 AA7 ARG A 212 ALA A 222 1 11
HELIX 8 AA8 THR A 225 ASP A 227 5 3
HELIX 9 AA9 LYS A 228 ASP A 237 1 10
HELIX 10 AB1 LYS A 238 GLU A 240 5 3
HELIX 11 AB2 GLU A 245 GLY A 255 1 11
HELIX 12 AB3 VAL A 260 SER A 269 1 10
HELIX 13 AB4 SER A 272 GLY A 281 1 10
HELIX 14 AB5 HIS A 284 GLY A 301 1 18
HELIX 15 AB6 TYR A 302 ASP A 304 5 3
HELIX 16 AB7 ASN A 344 TYR A 349 1 6
HELIX 17 AB8 CYS A 365 LYS A 374 1 10
HELIX 18 AB9 ASP A 392 SER A 394 5 3
HELIX 19 AC1 MET A 395 ALA A 409 1 15
HELIX 20 AC2 LYS A 421 VAL A 432 1 12
HELIX 21 AC3 ALA A 441 ARG A 447 1 7
SHEET 1 AA1 4 GLU A 85 GLU A 86 0
SHEET 2 AA1 4 ALA A 146 SER A 150 1 O LYS A 147 N GLU A 85
SHEET 3 AA1 4 GLU A 167 VAL A 176 -1 O ASN A 172 N SER A 150
SHEET 4 AA1 4 GLN A 153 TRP A 155 -1 N CYS A 154 O HIS A 168
SHEET 1 AA2 8 GLU A 85 GLU A 86 0
SHEET 2 AA2 8 ALA A 146 SER A 150 1 O LYS A 147 N GLU A 85
SHEET 3 AA2 8 GLU A 167 VAL A 176 -1 O ASN A 172 N SER A 150
SHEET 4 AA2 8 CYS A 357 GLY A 363 -1 O ALA A 358 N ILE A 175
SHEET 5 AA2 8 CYS A 337 ARG A 341 -1 N GLY A 338 O GLY A 361
SHEET 6 AA2 8 ILE A 322 ASP A 328 -1 N PHE A 324 O GLY A 339
SHEET 7 AA2 8 VAL A 205 SER A 211 -1 N ASN A 210 O VAL A 323
SHEET 8 AA2 8 VAL A 306 PHE A 308 1 O LEU A 307 N VAL A 209
SHEET 1 AA3 3 LEU A 92 SER A 94 0
SHEET 2 AA3 3 ARG A 120 LEU A 123 -1 O ALA A 122 N GLU A 93
SHEET 3 AA3 3 ASN A 112 ILE A 114 -1 N PHE A 113 O VAL A 121
SHEET 1 AA4 5 ALA A 413 ILE A 415 0
SHEET 2 AA4 5 VAL A 384 PRO A 390 1 N VAL A 388 O ASP A 414
SHEET 3 AA4 5 ALA A 434 VAL A 440 1 O VAL A 440 N ILE A 389
SHEET 4 AA4 5 GLU A 449 MET A 454 -1 O GLN A 451 N LEU A 439
SHEET 5 AA4 5 PHE A 470 PRO A 473 -1 O VAL A 472 N VAL A 450
SSBOND 1 SO4 A 503 SO4 A 503 1555 2756 2.01
CISPEP 1 LEU A 144 PRO A 145 0 1.20
SITE 1 AC1 17 GLU A 126 THR A 128 GLN A 170 ASN A 172
SITE 2 AC1 17 ASP A 174 LEU A 316 TYR A 318 TYR A 319
SITE 3 AC1 17 GLY A 338 TYR A 342 GLY A 359 PHE A 360
SITE 4 AC1 17 GLY A 361 HOH A 611 HOH A 632 HOH A 667
SITE 5 AC1 17 HOH A 688
SITE 1 AC2 8 ILE A 106 PRO A 125 CYS A 154 TRP A 155
SITE 2 AC2 8 ARG A 156 ARG A 165 GLU A 167 HIS A 168
SITE 1 AC3 3 ARG A 69 HIS A 76 HOH A 601
SITE 1 AC4 6 ARG A 165 HIS A 168 GLY A 363 ASP A 364
SITE 2 AC4 6 CYS A 365 VAL A 366
SITE 1 AC5 5 ARG A 196 SER A 201 SER A 202 TRP A 305
SITE 2 AC5 5 HOH A 697
SITE 1 AC6 7 GLU A 96 LEU A 97 ILE A 99 ARG A 100
SITE 2 AC6 7 THR A 348 TYR A 349 HOH A 674
SITE 1 AC7 6 TRP A 193 ARG A 196 SER A 197 TYR A 302
SITE 2 AC7 6 HOH A 661 HOH A 686
SITE 1 AC8 6 GLN A 55 THR A 115 GLY A 117 HIS A 119
SITE 2 AC8 6 TYR A 157 ARG A 166
CRYST1 64.433 118.814 65.975 90.00 92.39 90.00 I 1 2 1 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 0.015520 0.000000 0.000648 0.00000
SCALE2 0.000000 0.008417 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015170 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
