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HEADER STRUCTURAL GENOMICS 11-MAR-19 6QZ3
TITLE STRUCTURE OF MHETASE FROM IDEONELLA SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO(2-HYDROXYETHYL) TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MHETASE;
COMPND 5 EC: 3.1.1.102;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN 201-F6);
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 STRAIN: 201-F6;
SOURCE 5 GENE: ISF6_0224;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C41;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCJ136
KEYWDS MHETASE, PET DEGRADATION, STRUCTURAL GENOMICS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.ALLEN,C.W.JOHNSON,B.C.KNOTT,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT 1 30-SEP-20 6QZ3 0
JRNL AUTH M.D.ALLEN,C.W.JOHNSON,B.C.KNOTT,G.T.BECKHAM,J.E.MCGEEHAN
JRNL TITL STRUCTURE OF FROM MHETASE FROM IDEONELLA SAKAIENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.130
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 161084
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160
REMARK 3 FREE R VALUE TEST SET COUNT : 8305
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 45.8403 - 4.9695 1.00 5138 227 0.1609 0.1471
REMARK 3 2 4.9695 - 3.9452 1.00 5174 226 0.1329 0.1302
REMARK 3 3 3.9452 - 3.4467 1.00 5079 290 0.1425 0.1471
REMARK 3 4 3.4467 - 3.1316 1.00 5110 269 0.1506 0.1641
REMARK 3 5 3.1316 - 2.9072 1.00 5125 246 0.1535 0.1848
REMARK 3 6 2.9072 - 2.7358 1.00 5116 289 0.1611 0.1776
REMARK 3 7 2.7358 - 2.5988 1.00 5050 322 0.1605 0.1608
REMARK 3 8 2.5988 - 2.4857 1.00 5121 247 0.1613 0.1642
REMARK 3 9 2.4857 - 2.3900 1.00 5089 283 0.1567 0.1895
REMARK 3 10 2.3900 - 2.3075 1.00 5083 291 0.1599 0.2006
REMARK 3 11 2.3075 - 2.2354 1.00 5110 260 0.1547 0.1478
REMARK 3 12 2.2354 - 2.1715 1.00 5104 282 0.1598 0.1901
REMARK 3 13 2.1715 - 2.1143 1.00 5123 274 0.1689 0.1745
REMARK 3 14 2.1143 - 2.0627 1.00 5098 262 0.1737 0.2118
REMARK 3 15 2.0627 - 2.0158 1.00 5090 313 0.1715 0.2025
REMARK 3 16 2.0158 - 1.9729 1.00 5095 300 0.1732 0.2107
REMARK 3 17 1.9729 - 1.9335 1.00 4982 324 0.1829 0.2051
REMARK 3 18 1.9335 - 1.8970 1.00 5153 273 0.1862 0.2476
REMARK 3 19 1.8970 - 1.8631 1.00 5068 310 0.1825 0.2125
REMARK 3 20 1.8631 - 1.8315 1.00 5118 265 0.1936 0.2548
REMARK 3 21 1.8315 - 1.8020 1.00 5041 287 0.1966 0.2097
REMARK 3 22 1.8020 - 1.7743 1.00 5118 301 0.1962 0.2217
REMARK 3 23 1.7743 - 1.7482 1.00 5101 296 0.1964 0.2174
REMARK 3 24 1.7482 - 1.7235 1.00 5038 324 0.1991 0.2458
REMARK 3 25 1.7235 - 1.7003 1.00 5089 254 0.2059 0.2558
REMARK 3 26 1.7003 - 1.6782 1.00 5117 251 0.2129 0.2482
REMARK 3 27 1.6782 - 1.6572 1.00 5116 308 0.2272 0.2561
REMARK 3 28 1.6572 - 1.6372 1.00 5096 255 0.2377 0.2606
REMARK 3 29 1.6372 - 1.6182 1.00 5116 227 0.2445 0.2829
REMARK 3 30 1.6182 - 1.6000 0.95 4921 249 0.2712 0.2821
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 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 : 0.003 4253
REMARK 3 ANGLE : 0.613 5799
REMARK 3 CHIRALITY : 0.043 609
REMARK 3 PLANARITY : 0.004 775
REMARK 3 DIHEDRAL : 3.813 3359
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6QZ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1292101169.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83917
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 49.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 12.60
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 11.00
REMARK 200 R MERGE FOR SHELL (I) : 0.56200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE (PH 6.5), 9%
REMARK 280 PEG 8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
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,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.50800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.82150
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.50800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 45.82150
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 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 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 843 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1491 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 MSE A 1
REMARK 465 GLN A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 VAL A 5
REMARK 465 THR A 6
REMARK 465 THR A 7
REMARK 465 MSE A 8
REMARK 465 LEU A 9
REMARK 465 LEU A 10
REMARK 465 ALA A 11
REMARK 465 SER A 12
REMARK 465 VAL A 13
REMARK 465 ALA A 14
REMARK 465 LEU A 15
REMARK 465 ALA A 16
REMARK 465 ALA A 17
REMARK 465 CYS A 18
REMARK 465 ALA A 19
REMARK 465 GLY A 20
REMARK 465 GLY A 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 THR A 24
REMARK 465 PRO A 25
REMARK 465 LEU A 26
REMARK 465 PRO A 27
REMARK 465 LEU A 28
REMARK 465 PRO A 29
REMARK 465 GLN A 30
REMARK 465 GLN A 31
REMARK 465 GLN A 32
REMARK 465 PRO A 33
REMARK 465 PRO A 34
REMARK 465 GLN A 35
REMARK 465 GLN A 36
REMARK 465 GLU A 37
REMARK 465 PRO A 38
REMARK 465 PRO A 39
REMARK 465 ASP A 56
REMARK 465 GLY A 57
REMARK 465 ASN A 58
REMARK 465 GLY A 59
REMARK 465 ASP A 60
REMARK 465 MSE A 61
REMARK 465 LEU A 604
REMARK 465 GLU A 605
REMARK 465 HIS A 606
REMARK 465 HIS A 607
REMARK 465 HIS A 608
REMARK 465 HIS A 609
REMARK 465 HIS A 610
REMARK 465 HIS A 611
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 1313 O HOH A 1393 1.82
REMARK 500 O HOH A 1430 O HOH A 1480 1.83
REMARK 500 O HOH A 860 O HOH A 939 1.83
REMARK 500 O HOH A 1300 O HOH A 1383 1.83
REMARK 500 O HOH A 808 O HOH A 1352 1.84
REMARK 500 O HOH A 1419 O HOH A 1532 1.84
REMARK 500 O HOH A 1222 O HOH A 1487 1.86
REMARK 500 O HOH A 1011 O HOH A 1235 1.89
REMARK 500 O HOH A 1217 O HOH A 1466 1.89
REMARK 500 O HOH A 1266 O HOH A 1322 1.91
REMARK 500 O HOH A 1405 O HOH A 1535 1.92
REMARK 500 O HOH A 1307 O HOH A 1318 1.96
REMARK 500 O HOH A 1324 O HOH A 1343 1.96
REMARK 500 O HOH A 889 O HOH A 1372 2.00
REMARK 500 O HOH A 1224 O HOH A 1464 2.01
REMARK 500 O ALA A 343 O HOH A 801 2.01
REMARK 500 O HOH A 1299 O HOH A 1341 2.06
REMARK 500 O HOH A 1378 O HOH A 1481 2.09
REMARK 500 O HOH A 1197 O HOH A 1278 2.09
REMARK 500 O HOH A 1226 O HOH A 1268 2.13
REMARK 500 O HOH A 909 O HOH A 1335 2.15
REMARK 500 O HOH A 1470 O HOH A 1501 2.16
REMARK 500 O HOH A 816 O HOH A 1250 2.16
REMARK 500 O HOH A 943 O HOH A 1145 2.16
REMARK 500 O HOH A 1348 O HOH A 1404 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 1334 O HOH A 1398 4654 2.09
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 ALA A 67 33.57 -95.03
REMARK 500 ASN A 134 -144.94 57.93
REMARK 500 TYR A 194 -30.62 -154.08
REMARK 500 SER A 225 -122.36 70.06
REMARK 500 ALA A 249 59.13 31.94
REMARK 500 ASP A 311 14.53 -146.96
REMARK 500 TYR A 373 -96.44 -143.61
REMARK 500 SER A 383 -144.35 -137.15
REMARK 500 VAL A 412 -61.48 -97.08
REMARK 500 SER A 491 32.89 -99.47
REMARK 500 ASN A 527 -153.15 -87.34
REMARK 500 CYS A 529 -21.58 68.53
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 A1543 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A1544 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A1545 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A1546 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH A1547 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH A1548 DISTANCE = 6.87 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 304 O
REMARK 620 2 ASP A 304 OD1 70.7
REMARK 620 3 ASP A 307 OD1 72.0 136.5
REMARK 620 4 ASP A 307 OD2 75.7 135.6 50.2
REMARK 620 5 LEU A 309 O 83.0 82.9 71.0 121.0
REMARK 620 6 ASP A 311 OD1 145.4 75.4 134.0 136.8 86.0
REMARK 620 7 ILE A 313 O 98.7 78.7 128.9 78.6 159.7 81.2
REMARK 620 8 HOH A 823 O 142.5 146.6 72.0 73.2 95.4 71.1 95.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 702
DBREF1 6QZ3 A 1 603 UNP MHETH_IDESA
DBREF2 6QZ3 A A0A0K8P8E7 1 603
SEQADV 6QZ3 LEU A 604 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ3 GLU A 605 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ3 HIS A 606 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ3 HIS A 607 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ3 HIS A 608 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ3 HIS A 609 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ3 HIS A 610 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6QZ3 HIS A 611 UNP A0A0K8P8E EXPRESSION TAG
SEQRES 1 A 611 MSE GLN THR THR VAL THR THR MSE LEU LEU ALA SER VAL
SEQRES 2 A 611 ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES 3 A 611 PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES 4 A 611 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 5 A 611 ALA LEU LYS ASP GLY ASN GLY ASP MSE VAL TRP PRO ASN
SEQRES 6 A 611 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 7 A 611 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 8 A 611 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 9 A 611 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MSE
SEQRES 10 A 611 PRO ALA GLU TRP ASN GLY ARG PHE PHE MSE GLU GLY GLY
SEQRES 11 A 611 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 12 A 611 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 13 A 611 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 14 A 611 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 15 A 611 GLY LEU ASP PRO GLN ALA ARG LEU ASP MSE GLY TYR ASN
SEQRES 16 A 611 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 17 A 611 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 18 A 611 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MSE MSE LEU
SEQRES 19 A 611 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 20 A 611 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 21 A 611 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 22 A 611 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 23 A 611 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 24 A 611 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 25 A 611 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 26 A 611 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 27 A 611 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 28 A 611 VAL GLN VAL THR ALA ILE LYS ARG ALA MSE ALA GLY PRO
SEQRES 29 A 611 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 30 A 611 TRP ASP ALA GLY MSE SER GLY LEU SER GLY THR THR TYR
SEQRES 31 A 611 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 32 A 611 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 33 A 611 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 34 A 611 PRO MSE PRO MSE THR GLN VAL ALA ALA ARG MSE MSE LYS
SEQRES 35 A 611 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 36 A 611 SER GLY GLN PHE THR GLN SER SER MSE ASP TRP HIS GLY
SEQRES 37 A 611 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 38 A 611 GLY LYS MSE ILE LEU TYR HIS GLY MSE SER ASP ALA ALA
SEQRES 39 A 611 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 40 A 611 GLY ALA ALA MSE PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 41 A 611 PHE LEU VAL PRO GLY MSE ASN HIS CYS SER GLY GLY PRO
SEQRES 42 A 611 GLY THR ASP ARG PHE ASP MSE LEU THR PRO LEU VAL ALA
SEQRES 43 A 611 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 44 A 611 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 45 A 611 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 46 A 611 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 47 A 611 CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 6QZ3 MSE A 117 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 127 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 192 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 232 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 233 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 361 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 382 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 431 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 433 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 440 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 441 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 464 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 484 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 490 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 511 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 526 MET MODIFIED RESIDUE
MODRES 6QZ3 MSE A 540 MET MODIFIED RESIDUE
HET MSE A 117 8
HET MSE A 127 8
HET MSE A 192 8
HET MSE A 232 8
HET MSE A 233 8
HET MSE A 361 8
HET MSE A 382 8
HET MSE A 431 8
HET MSE A 433 8
HET MSE A 440 8
HET MSE A 441 8
HET MSE A 464 8
HET MSE A 484 8
HET MSE A 490 8
HET MSE A 511 8
HET MSE A 526 8
HET MSE A 540 8
HET BEZ A 701 9
HET CA A 702 1
HETNAM MSE SELENOMETHIONINE
HETNAM BEZ BENZOIC ACID
HETNAM CA CALCIUM ION
FORMUL 1 MSE 17(C5 H11 N O2 SE)
FORMUL 2 BEZ C7 H6 O2
FORMUL 3 CA CA 2+
FORMUL 4 HOH *748(H2 O)
HELIX 1 AA1 SER A 47 ALA A 53 1 7
HELIX 2 AA2 ALA A 152 ASN A 156 5 5
HELIX 3 AA3 LEU A 177 LEU A 184 5 8
HELIX 4 AA4 ASP A 185 TYR A 194 1 10
HELIX 5 AA5 TYR A 194 GLY A 213 1 20
HELIX 6 AA6 SER A 225 PHE A 238 1 14
HELIX 7 AA7 GLN A 253 PRO A 255 5 3
HELIX 8 AA8 LYS A 256 ALA A 269 1 14
HELIX 9 AA9 PRO A 270 ALA A 272 5 3
HELIX 10 AB1 LEU A 282 SER A 286 5 5
HELIX 11 AB2 SER A 288 ASP A 304 1 17
HELIX 12 AB3 ALA A 305 GLY A 308 5 4
HELIX 13 AB4 ASN A 316 PHE A 324 1 9
HELIX 14 AB5 SER A 350 GLY A 363 1 14
HELIX 15 AB6 ASP A 379 SER A 383 5 5
HELIX 16 AB7 TRP A 394 LEU A 399 1 6
HELIX 17 AB8 GLY A 414 PHE A 424 1 11
HELIX 18 AB9 PRO A 432 THR A 434 5 3
HELIX 19 AC1 GLN A 435 LYS A 442 1 8
HELIX 20 AC2 ILE A 447 TRP A 453 5 7
HELIX 21 AC3 SER A 462 GLY A 468 1 7
HELIX 22 AC4 LEU A 474 ARG A 480 1 7
HELIX 23 AC5 SER A 496 MSE A 511 1 16
HELIX 24 AC6 GLY A 513 GLY A 516 5 4
HELIX 25 AC7 MSE A 540 GLY A 551 1 12
HELIX 26 AC8 THR A 563 GLY A 568 5 6
HELIX 27 AC9 THR A 593 ALA A 595 5 3
SHEET 1 AA1 9 THR A 68 ARG A 76 0
SHEET 2 AA1 9 HIS A 91 THR A 102 -1 O HIS A 91 N ARG A 76
SHEET 3 AA1 9 PRO A 108 PRO A 118 -1 O LEU A 115 N VAL A 94
SHEET 4 AA1 9 ALA A 158 THR A 162 -1 O THR A 159 N ARG A 116
SHEET 5 AA1 9 ARG A 124 GLU A 128 1 N PHE A 126 O ALA A 158
SHEET 6 AA1 9 LYS A 218 CYS A 224 1 O TYR A 220 N PHE A 125
SHEET 7 AA1 9 GLY A 244 GLY A 248 1 O GLY A 248 N GLY A 223
SHEET 8 AA1 9 LYS A 483 GLY A 489 1 O ILE A 485 N ILE A 245
SHEET 9 AA1 9 ALA A 518 VAL A 523 1 O ARG A 519 N LEU A 486
SHEET 1 AA2 2 LEU A 385 SER A 386 0
SHEET 2 AA2 2 THR A 389 TYR A 390 -1 O THR A 389 N SER A 386
SHEET 1 AA3 2 ILE A 557 TRP A 560 0
SHEET 2 AA3 2 THR A 573 LEU A 576 -1 O LEU A 576 N ILE A 557
SHEET 1 AA4 2 ILE A 582 TYR A 585 0
SHEET 2 AA4 2 PHE A 597 ALA A 600 -1 O ALA A 600 N ILE A 582
SSBOND 1 CYS A 51 CYS A 92 1555 1555 2.04
SSBOND 2 CYS A 224 CYS A 529 1555 1555 2.06
SSBOND 3 CYS A 303 CYS A 320 1555 1555 2.05
SSBOND 4 CYS A 340 CYS A 348 1555 1555 2.04
SSBOND 5 CYS A 577 CYS A 599 1555 1555 2.05
LINK C ARG A 116 N MSE A 117 1555 1555 1.33
LINK C MSE A 117 N PRO A 118 1555 1555 1.33
LINK C PHE A 126 N MSE A 127 1555 1555 1.33
LINK C MSE A 127 N GLU A 128 1555 1555 1.33
LINK C ASP A 191 N MSE A 192 1555 1555 1.33
LINK C MSE A 192 N GLY A 193 1555 1555 1.33
LINK C GLY A 231 N MSE A 232 1555 1555 1.33
LINK C MSE A 232 N MSE A 233 1555 1555 1.33
LINK C MSE A 233 N LEU A 234 1555 1555 1.34
LINK C ALA A 360 N MSE A 361 1555 1555 1.33
LINK C MSE A 361 N ALA A 362 1555 1555 1.34
LINK C GLY A 381 N MSE A 382 1555 1555 1.33
LINK C MSE A 382 N SER A 383 1555 1555 1.33
LINK C PRO A 430 N MSE A 431 1555 1555 1.33
LINK C MSE A 431 N PRO A 432 1555 1555 1.34
LINK C PRO A 432 N MSE A 433 1555 1555 1.33
LINK C MSE A 433 N THR A 434 1555 1555 1.34
LINK C ARG A 439 N MSE A 440 1555 1555 1.33
LINK C MSE A 440 N MSE A 441 1555 1555 1.33
LINK C MSE A 441 N LYS A 442 1555 1555 1.33
LINK C SER A 463 N MSE A 464 1555 1555 1.33
LINK C MSE A 464 N ASP A 465 1555 1555 1.34
LINK C LYS A 483 N MSE A 484 1555 1555 1.33
LINK C MSE A 484 N ILE A 485 1555 1555 1.33
LINK C GLY A 489 N MSE A 490 1555 1555 1.33
LINK C MSE A 490 N SER A 491 1555 1555 1.34
LINK C ALA A 510 N MSE A 511 1555 1555 1.33
LINK C MSE A 511 N PRO A 512 1555 1555 1.33
LINK C GLY A 525 N MSE A 526 1555 1555 1.33
LINK C MSE A 526 N ASN A 527 1555 1555 1.33
LINK C ASP A 539 N MSE A 540 1555 1555 1.33
LINK C MSE A 540 N LEU A 541 1555 1555 1.34
LINK O ASP A 304 CA CA A 702 1555 1555 2.49
LINK OD1 ASP A 304 CA CA A 702 1555 1555 2.45
LINK OD1 ASP A 307 CA CA A 702 1555 1555 2.66
LINK OD2 ASP A 307 CA CA A 702 1555 1555 2.49
LINK O LEU A 309 CA CA A 702 1555 1555 2.33
LINK OD1 ASP A 311 CA CA A 702 1555 1555 2.53
LINK O ILE A 313 CA CA A 702 1555 1555 2.38
LINK CA CA A 702 O HOH A 823 1555 1555 2.53
CISPEP 1 THR A 426 PRO A 427 0 -2.35
CISPEP 2 TYR A 579 PRO A 580 0 4.20
SITE 1 AC1 11 GLY A 132 SER A 225 LEU A 254 ALA A 257
SITE 2 AC1 11 TRP A 397 ARG A 411 PHE A 415 SER A 416
SITE 3 AC1 11 PHE A 495 HOH A 855 HOH A1068
SITE 1 AC2 6 ASP A 304 ASP A 307 LEU A 309 ASP A 311
SITE 2 AC2 6 ILE A 313 HOH A 823
CRYST1 77.368 89.016 91.643 90.00 90.00 90.00 P 2 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012925 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011234 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010912 0.00000
TER 4128 PRO A 603
MASTER 416 0 19 27 15 0 5 6 4879 1 195 47
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