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HEADER HYDROLASE 26-NOV-12 4I3F
TITLE CRYSTAL STRUCTURE OF SERINE HYDROLASE CCSP0084 FROM THE POLYAROMATIC
TITLE 2 HYDROCARBON (PAH)-DEGRADING BACTERIUM CYCLOCLASTICUS ZANKLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE HYDROLASE CCSP0084;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CYCLOCLASTICUS SP. P1;
SOURCE 3 ORGANISM_COMMON: CYCLOCLASTICUS ZANCLES;
SOURCE 4 ORGANISM_TAXID: 385025;
SOURCE 5 GENE: Q91_2195;
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: P15TV LIC
KEYWDS ALPHA AND BETA PROTEINS, ALPHA/BETA HYDROLASE FOLD, ALPHA/BETA-
KEYWDS 2 HYDROLASES SUPERFAMILY, CARBON-CARBON BOND HYDROLASE FAMILY, SERINE
KEYWDS 3 HYDROLASE, ESTERASE, META-CLEAVAGE PRODUCT (MCP) HYDROLASE,
KEYWDS 4 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,X.XU,A.DONG,H.CUI,M.ALCAIDE,J.TORNES,C.GERTLER,
AUTHOR 2 M.M.YAKIMOV,P.N.GOLYSHIN,M.FERRER,A.SAVCHENKO
REVDAT 1 26-JUN-13 4I3F 0
JRNL AUTH M.ALCAIDE,J.TORNES,P.J.STOGIOS,X.XU,C.GERTLER,R.DI LEO,
JRNL AUTH 2 R.BARGIELA,A.LAFRAYA,M.E.GUAZZARONI,N.LOPEZ-CORTES,
JRNL AUTH 3 T.N.CHERNIKOVA,O.V.GOLYSHINA,T.Y.NECHITAYLO,I.PLUMEIER,
JRNL AUTH 4 D.H.PIEPER,M.M.YAKIMOV,A.SAVCHENKO,P.N.GOLYSHIN,M.FERRER
JRNL TITL SINGLE RESIDUES DICTATE THE CO-EVOLUTION OF DUAL ESTERASES -
JRNL TITL 2 MCP HYDROLASES FROM THE ALPHA/BETA HYDROLASE FAMILY.
JRNL REF BIOCHEM.J. 2013
JRNL REFN ESSN 1470-8728
JRNL PMID 23750508
JRNL DOI 10.1042/BJ20130552
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 28176
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1368
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 19.6077 - 4.5691 0.99 2708 80 0.1458 0.1756
REMARK 3 2 4.5691 - 3.6342 0.99 2670 78 0.1124 0.1552
REMARK 3 3 3.6342 - 3.1770 0.98 2645 84 0.1270 0.1798
REMARK 3 4 3.1770 - 2.8875 0.98 2714 601 0.1492 0.2135
REMARK 3 5 2.8875 - 2.6811 0.97 2621 75 0.1521 0.1690
REMARK 3 6 2.6811 - 2.5234 0.96 2579 89 0.1430 0.1859
REMARK 3 7 2.5234 - 2.3972 0.96 2623 70 0.1430 0.1586
REMARK 3 8 2.3972 - 2.2930 0.95 2573 65 0.1485 0.1794
REMARK 3 9 2.2930 - 2.2049 0.95 2639 70 0.1483 0.1610
REMARK 3 10 2.2049 - 2.1289 0.94 2583 61 0.1443 0.1770
REMARK 3 11 2.1289 - 2.0624 0.94 2551 66 0.1387 0.1850
REMARK 3 12 2.0624 - 2.0035 0.93 2555 61 0.1430 0.1986
REMARK 3 13 2.0035 - 1.9508 0.93 2557 66 0.1575 0.1985
REMARK 3 14 1.9508 - 1.9033 0.93 2513 63 0.1721 0.2038
REMARK 3 15 1.9033 - 1.8600 0.92 2593 51 0.1672 0.2399
REMARK 3 16 1.8600 - 1.8205 0.92 2489 68 0.1782 0.2554
REMARK 3 17 1.8205 - 1.7841 0.91 2466 62 0.1845 0.2390
REMARK 3 18 1.7841 - 1.7504 0.91 2503 61 0.1974 0.2657
REMARK 3 19 1.7504 - 1.7192 0.90 2467 75 0.1898 0.2253
REMARK 3 20 1.7192 - 1.6901 0.90 2473 70 0.1970 0.2885
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.290
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 : 0.008 2345
REMARK 3 ANGLE : 1.028 3189
REMARK 3 CHIRALITY : 0.074 339
REMARK 3 PLANARITY : 0.005 425
REMARK 3 DIHEDRAL : 13.781 854
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain A and resi 0:131
REMARK 3 ORIGIN FOR THE GROUP (A): -19.5875 -2.6933 11.3796
REMARK 3 T TENSOR
REMARK 3 T11: 0.0898 T22: 0.1000
REMARK 3 T33: 0.0751 T12: 0.0254
REMARK 3 T13: -0.0105 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.6622 L22: 1.4863
REMARK 3 L33: 2.3018 L12: 0.3575
REMARK 3 L13: 0.8712 L23: 0.0557
REMARK 3 S TENSOR
REMARK 3 S11: -0.0402 S12: 0.0893 S13: 0.1286
REMARK 3 S21: -0.1136 S22: -0.0640 S23: 0.0800
REMARK 3 S31: -0.1610 S32: -0.0728 S33: 0.0928
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain A and resi 132:189
REMARK 3 ORIGIN FOR THE GROUP (A): -35.0298 -12.7745 23.2488
REMARK 3 T TENSOR
REMARK 3 T11: 0.1628 T22: 0.2283
REMARK 3 T33: 0.2118 T12: -0.0106
REMARK 3 T13: -0.0132 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 3.8967 L22: 1.0895
REMARK 3 L33: 4.6012 L12: 0.5676
REMARK 3 L13: 0.6049 L23: 0.6614
REMARK 3 S TENSOR
REMARK 3 S11: -0.0165 S12: 0.0964 S13: 0.4878
REMARK 3 S21: -0.1035 S22: -0.0452 S23: 0.1875
REMARK 3 S31: -0.3502 S32: -0.7579 S33: 0.0515
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain A and resi 190:282
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1985 -11.0932 23.1885
REMARK 3 T TENSOR
REMARK 3 T11: 0.0720 T22: 0.0715
REMARK 3 T33: 0.0735 T12: 0.0033
REMARK 3 T13: 0.0009 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 1.6430 L22: 0.5940
REMARK 3 L33: 1.6644 L12: 0.3077
REMARK 3 L13: 0.4226 L23: -0.1645
REMARK 3 S TENSOR
REMARK 3 S11: 0.0186 S12: 0.0999 S13: -0.0412
REMARK 3 S21: -0.0650 S22: -0.0058 S23: -0.0338
REMARK 3 S31: 0.1229 S32: 0.0046 S33: -0.0086
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 4I3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-12.
REMARK 100 THE RCSB ID CODE IS RCSB076254.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31991
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610
REMARK 200 RESOLUTION RANGE LOW (A) : 19.610
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.35700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.PHASER)
REMARK 200 STARTING MODEL: 1CR6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 0.2 M MAGNESIUM
REMARK 280 CHLORIDE, 25% PEG3350. , VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 40.77150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.84550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 40.77150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.84550
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
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 CYS A 70 70.24 -154.07
REMARK 500 SER A 104 -115.09 50.37
REMARK 500 LYS A 122 -97.69 -105.06
REMARK 500 VAL A 189 -38.32 -135.17
REMARK 500 LYS A 264 62.57 -117.88
REMARK 500
REMARK 500 REMARK: NULL
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 NA A 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 119 OE2
REMARK 620 2 HOH A 762 O 131.6
REMARK 620 3 HOH A 494 O 78.8 94.0
REMARK 620 4 HOH A 557 O 84.5 96.6 163.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 304
DBREF 4I3F A -20 282 PDB 4I3F 4I3F -20 282
SEQRES 1 A 303 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 303 ARG GLU ASN LEU TYR PHE GLN GLY MET GLN THR SER ASN
SEQRES 3 A 303 ILE GLN THR GLY SER PHE ASN THR PHE LEU ASN GLU ALA
SEQRES 4 A 303 GLY THR ASP LYS ASP THR SER ILE LEU LEU LEU HIS GLY
SEQRES 5 A 303 SER GLY PRO GLY ALA ASN ALA MET SER ASN TRP GLN TYR
SEQRES 6 A 303 ALA LEU PRO PHE LEU ALA GLU ASN TYR HIS CYS LEU ALA
SEQRES 7 A 303 PRO ASP ILE ALA GLY PHE GLY LEU SER GLN HIS ASN CYS
SEQRES 8 A 303 PRO PRO ASN GLY THR SER HIS TRP ILE ASP ILE TRP VAL
SEQRES 9 A 303 GLN GLN GLN ILE ASP LEU LEU ASP ALA LYS GLY ILE GLU
SEQRES 10 A 303 GLN THR HIS ILE VAL GLY ASN SER MET GLY GLY GLY VAL
SEQRES 11 A 303 THR LEU HIS LEU LEU ASN ARG HIS PRO GLU ARG PHE LYS
SEQRES 12 A 303 LYS ALA VAL LEU MET GLY PRO VAL GLY ALA PRO PHE ALA
SEQRES 13 A 303 PRO THR GLU GLY LEU THR LYS GLY TRP GLU PHE TYR LYS
SEQRES 14 A 303 ASP PRO SER LYS GLU ALA LEU GLU TYR LEU ILE THR LYS
SEQRES 15 A 303 PHE LEU PHE ASP PRO SER LEU LEU GLY ASN ASP ILE ALA
SEQRES 16 A 303 SER ILE ALA ALA GLN ARG PHE ASP ASN VAL MET LYS ASP
SEQRES 17 A 303 GLU VAL ARG LEU GLN PHE GLU ALA MET PHE SER GLY GLY
SEQRES 18 A 303 THR LYS LYS GLY ILE ASP ALA PHE VAL LEU SER ASP ASP
SEQRES 19 A 303 GLU LEU ASN ASN ILE SER HIS GLN MET LEU VAL THR HIS
SEQRES 20 A 303 ALA ARG GLU ASP PHE PHE ILE PRO LEU ASN ASN ALA TYR
SEQRES 21 A 303 TYR LEU ILE ASP ARG ILE PRO ASN ALA GLN LEU HIS VAL
SEQRES 22 A 303 PHE ASP HIS CYS GLY HIS TRP VAL GLN ILE GLU LYS LYS
SEQRES 23 A 303 LYS ALA PHE ASN ASN LEU THR LYS LEU PHE PHE ASP GLY
SEQRES 24 A 303 MET PHE ASP ASP
HET CL A 301 1
HET CL A 302 1
HET NA A 303 1
HET PEG A 304 7
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 2 CL 2(CL 1-)
FORMUL 4 NA NA 1+
FORMUL 5 PEG C4 H10 O3
FORMUL 6 HOH *413(H2 O)
HELIX 1 1 ASN A 37 GLN A 43 1 7
HELIX 2 2 TYR A 44 ALA A 50 1 7
HELIX 3 3 GLY A 74 LYS A 93 1 20
HELIX 4 4 SER A 104 HIS A 117 1 14
HELIX 5 5 THR A 137 GLU A 145 1 9
HELIX 6 6 PHE A 146 ASP A 149 5 4
HELIX 7 7 SER A 151 PHE A 162 1 12
HELIX 8 8 ASP A 165 GLY A 170 5 6
HELIX 9 9 ASP A 172 LYS A 186 1 15
HELIX 10 10 LYS A 186 PHE A 197 1 12
HELIX 11 11 GLY A 200 VAL A 209 1 10
HELIX 12 12 SER A 211 ASN A 217 1 7
HELIX 13 13 LEU A 235 ILE A 245 1 11
HELIX 14 14 TRP A 259 LYS A 264 1 6
HELIX 15 15 LYS A 264 GLY A 278 1 15
SHEET 1 A 8 GLN A 2 THR A 8 0
SHEET 2 A 8 PHE A 11 ALA A 18 -1 O THR A 13 N ILE A 6
SHEET 3 A 8 HIS A 54 PRO A 58 -1 O ALA A 57 N ASN A 16
SHEET 4 A 8 SER A 25 LEU A 29 1 N LEU A 28 O LEU A 56
SHEET 5 A 8 THR A 98 ASN A 103 1 O VAL A 101 N LEU A 29
SHEET 6 A 8 PHE A 121 MET A 127 1 O VAL A 125 N ILE A 100
SHEET 7 A 8 MET A 222 ALA A 227 1 O THR A 225 N LEU A 126
SHEET 8 A 8 ALA A 248 PHE A 253 1 O GLN A 249 N VAL A 224
LINK OE2 GLU A 119 NA NA A 303 1555 1555 2.35
LINK NA NA A 303 O HOH A 762 1555 1555 2.75
LINK NA NA A 303 O HOH A 494 1555 1555 2.85
LINK NA NA A 303 O BHOH A 557 1555 1555 3.14
SITE 1 AC1 7 GLY A 31 GLY A 33 ASN A 41 TRP A 259
SITE 2 AC1 7 HOH A 680 HOH A 682 HOH A 739
SITE 1 AC2 2 SER A 32 SER A 104
SITE 1 AC3 4 HIS A 117 GLU A 119 HOH A 494 HOH A 762
SITE 1 AC4 4 SER A 10 THR A 20 HOH A 470 HOH A 633
CRYST1 81.543 49.691 67.995 90.00 105.89 90.00 C 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 0.012263 0.000000 0.003491 0.00000
SCALE2 0.000000 0.020124 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015291 0.00000
TER 2273 ASP A 282
MASTER 334 0 4 15 8 0 5 6 2654 1 12 24
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