HEADER LIGASE 08-FEB-11 3QNE
TITLE CANDIDA ALBICANS SERYL-TRNA SYNTHETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERYL-TRNA SYNTHETASE, CYTOPLASMIC;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SERINE--TRNA LIGASE, SERRS, SERYL-TRNA(SER/SEC) SYNTHETASE;
COMPND 5 EC: 6.1.1.11;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA ALBICANS;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 5476;
SOURCE 5 GENE: CAO19.7901, SES1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P7-7
KEYWDS AMINO ACID BIOSYNTHESIS, CTG-CLADE, CODON AMBIGUITY, PATHOGEN, CLASS-
KEYWDS 2 II AMINOACYL-TRNA SYNTHETASE FAMILY, TYPE-1 SERYL-TRNA SYNTHETASE
KEYWDS 3 SUBFAMILY, TRNA, SERINE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ROCHA,M.A.SANTOS,P.J.B.PEREIRA,S.MACEDO-RIBEIRO
REVDAT 6 13-SEP-23 3QNE 1 SEQADV
REVDAT 5 10-SEP-14 3QNE 1 JRNL REMARK
REVDAT 4 14-SEP-11 3QNE 1 JRNL
REVDAT 3 31-AUG-11 3QNE 1 JRNL
REVDAT 2 24-AUG-11 3QNE 1 JRNL
REVDAT 1 03-AUG-11 3QNE 0
JRNL AUTH R.ROCHA,P.J.PEREIRA,M.A.SANTOS,S.MACEDO-RIBEIRO
JRNL TITL UNVEILING THE STRUCTURAL BASIS FOR TRANSLATIONAL AMBIGUITY
JRNL TITL 2 TOLERANCE IN A HUMAN FUNGAL PATHOGEN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 14091 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21825144
JRNL DOI 10.1073/PNAS.1102835108
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.ROCHA,P.J.BARBOSA PEREIRA,M.A.SANTOS,S.MACEDO-RIBEIRO
REMARK 1 TITL PURIFICATION, CRYSTALLIZATION AND PRELIMINARY X-RAY
REMARK 1 TITL 2 DIFFRACTION ANALYSIS OF THE SERYL-TRNA SYNTHETASE FROM
REMARK 1 TITL 3 CANDIDA ALBICANS.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 67 153 2011
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 21206050
REMARK 1 DOI 10.1107/S1744309110048542
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 43422
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2197
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 67.9785 - 4.3079 0.99 4684 251 0.1698 0.1761
REMARK 3 2 4.3079 - 3.4193 0.99 4431 212 0.1462 0.2065
REMARK 3 3 3.4193 - 2.9871 0.99 4298 249 0.1716 0.2126
REMARK 3 4 2.9871 - 2.7140 0.98 4289 207 0.1804 0.2224
REMARK 3 5 2.7140 - 2.5194 0.98 4235 210 0.1712 0.2117
REMARK 3 6 2.5194 - 2.3709 0.97 4156 229 0.1601 0.2101
REMARK 3 7 2.3709 - 2.2521 0.96 4161 209 0.1698 0.2559
REMARK 3 8 2.2521 - 2.1541 0.96 4061 253 0.1650 0.2121
REMARK 3 9 2.1541 - 2.0712 0.91 3874 221 0.1607 0.2208
REMARK 3 10 2.0712 - 1.9997 0.72 3036 156 0.1737 0.2342
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 50.02
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.200
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) : 4.31150
REMARK 3 B22 (A**2) : 4.31150
REMARK 3 B33 (A**2) : -8.62300
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 3653
REMARK 3 ANGLE : 1.157 4932
REMARK 3 CHIRALITY : 0.087 526
REMARK 3 PLANARITY : 0.005 646
REMARK 3 DIHEDRAL : 14.133 1403
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 1:101)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2173 31.2727 -27.5898
REMARK 3 T TENSOR
REMARK 3 T11: 0.2026 T22: 0.3253
REMARK 3 T33: 0.2506 T12: -0.0717
REMARK 3 T13: 0.0647 T23: -0.1187
REMARK 3 L TENSOR
REMARK 3 L11: 1.7639 L22: -0.0308
REMARK 3 L33: 0.6405 L12: -0.9793
REMARK 3 L13: -1.1340 L23: 0.1808
REMARK 3 S TENSOR
REMARK 3 S11: 0.0085 S12: 0.1384 S13: 0.0348
REMARK 3 S21: 0.0230 S22: -0.0309 S23: -0.0868
REMARK 3 S31: 0.0958 S32: 0.1230 S33: -0.0342
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 102:162)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.3437 26.1078 -0.9951
REMARK 3 T TENSOR
REMARK 3 T11: 0.1801 T22: 0.1569
REMARK 3 T33: 0.1505 T12: -0.0057
REMARK 3 T13: 0.0414 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.6259 L22: 0.1307
REMARK 3 L33: 0.4403 L12: 0.3451
REMARK 3 L13: -0.2833 L23: -0.1118
REMARK 3 S TENSOR
REMARK 3 S11: 0.0334 S12: -0.1394 S13: -0.0401
REMARK 3 S21: -0.0036 S22: 0.0160 S23: 0.0022
REMARK 3 S31: -0.1168 S32: 0.0213 S33: -0.0477
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 163:297)
REMARK 3 ORIGIN FOR THE GROUP (A): -17.7285 18.5861 -19.7176
REMARK 3 T TENSOR
REMARK 3 T11: 0.1087 T22: 0.1072
REMARK 3 T33: 0.1227 T12: 0.0111
REMARK 3 T13: 0.0019 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.8182 L22: 0.5192
REMARK 3 L33: 0.9244 L12: 0.6364
REMARK 3 L13: -0.3991 L23: -0.2662
REMARK 3 S TENSOR
REMARK 3 S11: 0.0980 S12: -0.0475 S13: -0.0548
REMARK 3 S21: 0.0513 S22: -0.0563 S23: -0.0670
REMARK 3 S31: -0.0327 S32: 0.1214 S33: -0.0461
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 298:452)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5583 27.2023 -10.2827
REMARK 3 T TENSOR
REMARK 3 T11: 0.1313 T22: 0.0876
REMARK 3 T33: 0.1173 T12: -0.0061
REMARK 3 T13: 0.0363 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 0.5216 L22: 0.0872
REMARK 3 L33: 1.1801 L12: -0.2161
REMARK 3 L13: -0.0473 L23: 0.0280
REMARK 3 S TENSOR
REMARK 3 S11: 0.0898 S12: -0.0823 S13: 0.0403
REMARK 3 S21: 0.0261 S22: 0.0149 S23: 0.0432
REMARK 3 S31: -0.1990 S32: -0.0062 S33: -0.1002
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QNE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063863.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSING GE (220)
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43773
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 78.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 21.80
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
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) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.0
REMARK 200 DATA REDUNDANCY IN SHELL : 15.00
REMARK 200 R MERGE FOR SHELL (I) : 0.23000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 2DQ0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.2-3.4 M AMMONIUM SULFATE, 0-2% V/V
REMARK 280 GLYCEROL, 100 MM MES/SODIUM, PH 5.6-5.8, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 92.25233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 184.50467
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 138.37850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 230.63083
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 46.12617
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 92.25233
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 184.50467
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 230.63083
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 138.37850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 46.12617
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: 4570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -46.12617
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 SER A 284
REMARK 465 HIS A 285
REMARK 465 GLY A 286
REMARK 465 LYS A 287
REMARK 465 ASP A 288
REMARK 465 LYS A 388
REMARK 465 GLN A 389
REMARK 465 GLN A 390
REMARK 465 ASN A 391
REMARK 465 GLN A 392
REMARK 465 GLN A 393
REMARK 465 THR A 453
REMARK 465 SER A 454
REMARK 465 VAL A 455
REMARK 465 LYS A 456
REMARK 465 LYS A 457
REMARK 465 ALA A 458
REMARK 465 LYS A 459
REMARK 465 GLY A 460
REMARK 465 LYS A 461
REMARK 465 ASN A 462
REMARK 465 PRO A 463
REMARK 465 LYS A 464
REMARK 465 ASN A 465
REMARK 465 THR A 466
REMARK 465 THR A 467
REMARK 465 SER A 468
REMARK 465 VAL A 469
REMARK 465 LYS A 470
REMARK 465 LYS A 471
REMARK 465 ALA A 472
REMARK 465 LYS A 473
REMARK 465 GLY A 474
REMARK 465 LYS A 475
REMARK 465 ASN A 476
REMARK 465 GLY A 477
REMARK 465 SER A 478
REMARK 465 ARG 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 HIS A 485
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 ASP A 3 CG OD1 OD2
REMARK 470 TRP A 290 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 290 CZ3 CH2
REMARK 470 GLU A 394 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 10 CD
REMARK 480 GLU A 230 CD
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 O HOH A 584 O HOH A 610 10554 2.18
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 ASN A 182 -123.01 53.15
REMARK 500 ASN A 182 -117.14 44.34
REMARK 500 ASP A 228 38.77 -83.39
REMARK 500 GLU A 229 -48.36 -170.91
REMARK 500 THR A 246 144.96 -173.49
REMARK 500 ALA A 282 58.87 -141.03
REMARK 500 THR A 374 -127.45 35.94
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3QNE A 1 462 UNP Q9HGT6 SYSC_CANAL 1 462
SEQADV 3QNE PRO A 463 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE LYS A 464 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE ASN A 465 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE THR A 466 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE THR A 467 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE SER A 468 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE VAL A 469 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE LYS A 470 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE LYS A 471 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE ALA A 472 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE LYS A 473 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE GLY A 474 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE LYS A 475 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE ASN A 476 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE GLY A 477 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE SER A 478 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE ARG A 479 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE HIS A 480 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE HIS A 481 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE HIS A 482 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE HIS A 483 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE HIS A 484 UNP Q9HGT6 EXPRESSION TAG
SEQADV 3QNE HIS A 485 UNP Q9HGT6 EXPRESSION TAG
SEQRES 1 A 485 MET LEU ASP ILE ASN ALA PHE LEU VAL GLU LYS GLY GLY
SEQRES 2 A 485 ASP PRO GLU ILE ILE LYS ALA SER GLN LYS LYS ARG GLY
SEQRES 3 A 485 ASP SER VAL GLU LEU VAL ASP GLU ILE ILE ALA GLU TYR
SEQRES 4 A 485 LYS GLU TRP VAL LYS LEU ARG PHE ASP LEU ASP GLU HIS
SEQRES 5 A 485 ASN LYS LYS LEU ASN SER VAL GLN LYS GLU ILE GLY LYS
SEQRES 6 A 485 ARG PHE LYS ALA LYS GLU ASP ALA LYS ASP LEU ILE ALA
SEQRES 7 A 485 GLU LYS GLU LYS LEU SER ASN GLU LYS LYS GLU ILE ILE
SEQRES 8 A 485 GLU LYS GLU ALA GLU ALA ASP LYS ASN LEU ARG SER LYS
SEQRES 9 A 485 ILE ASN GLN VAL GLY ASN ILE VAL HIS GLU SER VAL VAL
SEQRES 10 A 485 ASP SER GLN ASP GLU GLU ASN ASN GLU LEU VAL ARG THR
SEQRES 11 A 485 TRP THR PRO GLU ASN TYR LYS LYS PRO GLU GLN ILE ALA
SEQRES 12 A 485 ALA ALA THR GLY ALA PRO ALA LYS LEU SER HIS HIS GLU
SEQRES 13 A 485 VAL LEU LEU ARG LEU ASP GLY TYR ASP PRO GLU ARG GLY
SEQRES 14 A 485 VAL ARG ILE VAL GLY HIS ARG GLY TYR PHE LEU ARG ASN
SEQRES 15 A 485 TYR GLY VAL PHE LEU ASN GLN ALA LEU ILE ASN TYR GLY
SEQRES 16 A 485 LEU SER PHE LEU SER SER LYS GLY TYR VAL PRO LEU GLN
SEQRES 17 A 485 ALA PRO VAL MET MET ASN LYS GLU VAL MET ALA LYS THR
SEQRES 18 A 485 ALA GLN LEU SER GLN PHE ASP GLU GLU LEU TYR LYS VAL
SEQRES 19 A 485 ILE ASP GLY GLU ASP GLU LYS TYR LEU ILE ALA THR SER
SEQRES 20 A 485 GLU GLN PRO ILE SER ALA TYR HIS ALA GLY GLU TRP PHE
SEQRES 21 A 485 GLU SER PRO ALA GLU GLN LEU PRO VAL ARG TYR ALA GLY
SEQRES 22 A 485 TYR SER SER CYS PHE ARG ARG GLU ALA GLY SER HIS GLY
SEQRES 23 A 485 LYS ASP ALA TRP GLY ILE PHE ARG VAL HIS ALA PHE GLU
SEQRES 24 A 485 LYS ILE GLU GLN PHE VAL LEU THR GLU PRO GLU LYS SER
SEQRES 25 A 485 TRP GLU GLU PHE ASP ARG MET ILE GLY CYS SER GLU GLU
SEQRES 26 A 485 PHE TYR GLN SER LEU GLY LEU PRO TYR ARG VAL VAL GLY
SEQRES 27 A 485 ILE VAL SER GLY GLU LEU ASN ASN ALA ALA ALA LYS LYS
SEQRES 28 A 485 TYR ASP LEU GLU ALA TRP PHE PRO PHE GLN GLN GLU TYR
SEQRES 29 A 485 LYS GLU LEU VAL SER CYS SER ASN CYS THR ASP TYR GLN
SEQRES 30 A 485 SER ARG ASN LEU GLU ILE ARG CYS GLY ILE LYS GLN GLN
SEQRES 31 A 485 ASN GLN GLN GLU LYS LYS TYR VAL HIS CYS LEU ASN SER
SEQRES 32 A 485 THR LEU SER ALA THR GLU ARG THR ILE CYS CYS ILE LEU
SEQRES 33 A 485 GLU ASN TYR GLN LYS GLU ASP GLY LEU VAL ILE PRO GLU
SEQRES 34 A 485 VAL LEU ARG LYS TYR ILE PRO GLY GLU PRO GLU PHE ILE
SEQRES 35 A 485 PRO TYR ILE LYS GLU LEU PRO LYS ASN THR THR SER VAL
SEQRES 36 A 485 LYS LYS ALA LYS GLY LYS ASN PRO LYS ASN THR THR SER
SEQRES 37 A 485 VAL LYS LYS ALA LYS GLY LYS ASN GLY SER ARG HIS HIS
SEQRES 38 A 485 HIS HIS HIS HIS
FORMUL 2 HOH *326(H2 O)
HELIX 1 1 ASP A 3 GLY A 12 5 10
HELIX 2 2 ASP A 14 GLY A 26 1 13
HELIX 3 3 VAL A 29 ALA A 69 1 41
HELIX 4 4 ALA A 73 ASN A 106 1 34
HELIX 5 5 ASP A 121 ASN A 125 5 5
HELIX 6 6 SER A 153 LEU A 161 1 9
HELIX 7 7 PRO A 166 GLY A 174 1 9
HELIX 8 8 ASN A 182 SER A 201 1 20
HELIX 9 9 LYS A 215 ALA A 222 1 8
HELIX 10 10 GLN A 223 ASP A 228 1 6
HELIX 11 11 SER A 247 HIS A 255 1 9
HELIX 12 12 SER A 262 LEU A 267 1 6
HELIX 13 13 GLU A 308 GLU A 310 5 3
HELIX 14 14 LYS A 311 LEU A 330 1 20
HELIX 15 15 VAL A 340 LEU A 344 5 5
HELIX 16 16 ASP A 375 LEU A 381 1 7
HELIX 17 17 THR A 408 TYR A 419 1 12
HELIX 18 18 PRO A 428 ILE A 435 5 8
SHEET 1 A 8 GLU A 126 TRP A 131 0
SHEET 2 A 8 TYR A 334 GLY A 338 -1 O VAL A 336 N ARG A 129
SHEET 3 A 8 LYS A 350 PHE A 358 -1 O GLU A 355 N ARG A 335
SHEET 4 A 8 GLU A 363 ASN A 372 -1 O CYS A 370 N TYR A 352
SHEET 5 A 8 HIS A 399 ALA A 407 -1 O ASN A 402 N SER A 371
SHEET 6 A 8 ALA A 297 THR A 307 -1 N GLN A 303 O SER A 403
SHEET 7 A 8 VAL A 269 PHE A 278 -1 N TYR A 271 O PHE A 304
SHEET 8 A 8 VAL A 205 GLN A 208 1 N VAL A 205 O ARG A 270
SHEET 1 B 2 TYR A 164 ASP A 165 0
SHEET 2 B 2 PHE A 179 LEU A 180 -1 O PHE A 179 N ASP A 165
SHEET 1 C 3 MET A 212 ASN A 214 0
SHEET 2 C 3 ASP A 239 LEU A 243 -1 O TYR A 242 N MET A 213
SHEET 3 C 3 LYS A 233 ASP A 236 -1 N VAL A 234 O LYS A 241
SHEET 1 D 2 TRP A 259 PHE A 260 0
SHEET 2 D 2 ARG A 384 CYS A 385 1 O ARG A 384 N PHE A 260
SHEET 1 E 3 GLN A 420 LYS A 421 0
SHEET 2 E 3 GLY A 424 VAL A 426 -1 O GLY A 424 N LYS A 421
SHEET 3 E 3 PHE A 441 PRO A 443 -1 O ILE A 442 N LEU A 425
CISPEP 1 LEU A 267 PRO A 268 0 -0.57
CRYST1 90.050 90.050 276.757 90.00 90.00 120.00 P 61 2 2 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011105 0.006411 0.000000 0.00000
SCALE2 0.000000 0.012823 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003613 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
