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HEADER HYDROLASE 25-AUG-13 4MEB
TITLE CRYSTAL STRUCTURE OF ACIF-D158S
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PREDICTED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 25-349;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACINETOBACTER SP. RUH2624;
SOURCE 3 ORGANISM_TAXID: 575564;
SOURCE 4 GENE: HMPREF0014_00517, ZP_05823503;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMQ70
KEYWDS ALPHA/BETA HYDROLASE FOLD, EPOXIDE HYDROLASE, SECRETED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.BRIDGES,C.D.BAHL,D.R.MADDEN
REVDAT 1 05-FEB-14 4MEB 0
JRNL AUTH C.D.BAHL,K.L.HVORECNY,A.A.BRIDGES,A.E.BALLOK,J.M.BOMBERGER,
JRNL AUTH 2 K.C.CADY,G.A.O'TOOLE JR.,D.R.MADDEN
JRNL TITL SIGNATURE MOTIFS IDENTIFY AN ACINETOBACTER CIF VIRULENCE
JRNL TITL 2 FACTOR WITH EPOXIDE HYDROLASE ACTIVITY.
JRNL REF J.BIOL.CHEM. 2014
JRNL REFN ESSN 1083-351X
JRNL DOI 10.1074/JBC.M113.518092
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 40962
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 2057
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 40.8580 - 4.9298 0.88 2543 89 0.1813 0.1942
REMARK 3 2 4.9298 - 3.9139 0.92 2451 197 0.1158 0.1503
REMARK 3 3 3.9139 - 3.4195 0.94 2612 99 0.1361 0.1627
REMARK 3 4 3.4195 - 3.1069 0.95 2561 127 0.1597 0.2089
REMARK 3 5 3.1069 - 2.8843 0.96 2555 177 0.1579 0.1953
REMARK 3 6 2.8843 - 2.7143 0.96 2625 100 0.1601 0.2105
REMARK 3 7 2.7143 - 2.5784 0.97 2620 124 0.1614 0.1918
REMARK 3 8 2.5784 - 2.4662 0.97 2538 189 0.1528 0.2099
REMARK 3 9 2.4662 - 2.3712 0.98 2645 108 0.1563 0.1864
REMARK 3 10 2.3712 - 2.2894 0.98 2671 113 0.1497 0.2426
REMARK 3 11 2.2894 - 2.2178 0.98 2560 203 0.1566 0.1889
REMARK 3 12 2.2178 - 2.1544 0.98 2641 112 0.1589 0.2356
REMARK 3 13 2.1544 - 2.0977 0.98 2672 105 0.1667 0.2525
REMARK 3 14 2.0977 - 2.0465 0.98 2568 171 0.1766 0.2436
REMARK 3 15 2.0465 - 2.0000 0.98 2643 143 0.1833 0.2418
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 35.38
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.180
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) : 0.79810
REMARK 3 B22 (A**2) : -0.64370
REMARK 3 B33 (A**2) : -0.15440
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -2.11530
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 : 0.007 5298
REMARK 3 ANGLE : 1.027 7186
REMARK 3 CHIRALITY : 0.078 752
REMARK 3 PLANARITY : 0.005 925
REMARK 3 DIHEDRAL : 11.772 1955
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 25:348)
REMARK 3 ORIGIN FOR THE GROUP (A): -35.5518 -10.0658 -20.0123
REMARK 3 T TENSOR
REMARK 3 T11: 0.0359 T22: 0.0096
REMARK 3 T33: 0.0255 T12: 0.0073
REMARK 3 T13: 0.0067 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.2543 L22: 0.4164
REMARK 3 L33: 0.4749 L12: 0.0665
REMARK 3 L13: 0.0725 L23: 0.1898
REMARK 3 S TENSOR
REMARK 3 S11: 0.0199 S12: 0.0410 S13: 0.0098
REMARK 3 S21: -0.0019 S22: 0.0118 S23: -0.0342
REMARK 3 S31: -0.0388 S32: 0.0323 S33: -0.0189
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 25:348)
REMARK 3 ORIGIN FOR THE GROUP (A): -72.9692 -20.4373 -23.9949
REMARK 3 T TENSOR
REMARK 3 T11: 0.0390 T22: 0.0769
REMARK 3 T33: 0.0558 T12: 0.0298
REMARK 3 T13: -0.0142 T23: -0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 0.6168 L22: 0.4134
REMARK 3 L33: 0.4143 L12: 0.0944
REMARK 3 L13: 0.0748 L23: 0.0608
REMARK 3 S TENSOR
REMARK 3 S11: -0.0050 S12: -0.0161 S13: 0.0165
REMARK 3 S21: 0.0219 S22: -0.0330 S23: 0.0854
REMARK 3 S31: -0.0159 S32: -0.0594 S33: 0.0232
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 4MEB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-13.
REMARK 100 THE RCSB ID CODE IS RCSB081802.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL CUT MONOCHROMATOR
REMARK 200 OPTICS : TOROIDAL FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS-PACKAGE
REMARK 200 DATA SCALING SOFTWARE : XDS-PACKAGE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40969
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 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: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 4MEA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 250 MM MONOPOTASSIUM PHOSPHATE, 100 MM
REMARK 280 SODIUM CITRATE, 20% PEG 4000, PH 4.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 21.25550
REMARK 290 SMTRY3 2 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: 3970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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 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 LYS A 349
REMARK 465 HIS A 350
REMARK 465 HIS A 351
REMARK 465 HIS A 352
REMARK 465 HIS A 353
REMARK 465 HIS A 354
REMARK 465 HIS A 355
REMARK 465 LYS B 349
REMARK 465 HIS B 350
REMARK 465 HIS B 351
REMARK 465 HIS B 352
REMARK 465 HIS B 353
REMARK 465 HIS B 354
REMARK 465 HIS B 355
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 SER A 80 -72.76 -146.46
REMARK 500 SER A 158 -130.76 54.84
REMARK 500 ASP A 182 -62.14 57.80
REMARK 500 ASP A 223 77.27 -159.77
REMARK 500 ASN A 301 -114.84 72.48
REMARK 500 ASP A 326 19.43 57.32
REMARK 500 ASN A 335 62.20 -151.74
REMARK 500 SER B 80 -67.04 -153.74
REMARK 500 TYR B 130 31.34 -96.51
REMARK 500 SER B 158 -125.87 55.08
REMARK 500 ASP B 182 -62.77 58.83
REMARK 500 ASP B 223 78.85 -154.27
REMARK 500 ASN B 283 47.14 -103.51
REMARK 500 LYS B 285 42.39 -56.29
REMARK 500 ASN B 301 -113.71 71.01
REMARK 500 ASN B 335 59.22 -158.23
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 PO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MEA RELATED DB: PDB
REMARK 900 WILD TYPE PROTEIN
REMARK 900 RELATED ID: 3KD2 RELATED DB: PDB
REMARK 900 HOMOLOGUE FROM PSEUDOMONAS AERUGINOSA PA14
DBREF 4MEB A 25 349 UNP D0BWK6 D0BWK6_9GAMM 25 349
DBREF 4MEB B 25 349 UNP D0BWK6 D0BWK6_9GAMM 25 349
SEQADV 4MEB SER A 158 UNP D0BWK6 ASP 158 ENGINEERED MUTATION
SEQADV 4MEB HIS A 350 UNP D0BWK6 EXPRESSION TAG
SEQADV 4MEB HIS A 351 UNP D0BWK6 EXPRESSION TAG
SEQADV 4MEB HIS A 352 UNP D0BWK6 EXPRESSION TAG
SEQADV 4MEB HIS A 353 UNP D0BWK6 EXPRESSION TAG
SEQADV 4MEB HIS A 354 UNP D0BWK6 EXPRESSION TAG
SEQADV 4MEB HIS A 355 UNP D0BWK6 EXPRESSION TAG
SEQADV 4MEB SER B 158 UNP D0BWK6 ASP 158 ENGINEERED MUTATION
SEQADV 4MEB HIS B 350 UNP D0BWK6 EXPRESSION TAG
SEQADV 4MEB HIS B 351 UNP D0BWK6 EXPRESSION TAG
SEQADV 4MEB HIS B 352 UNP D0BWK6 EXPRESSION TAG
SEQADV 4MEB HIS B 353 UNP D0BWK6 EXPRESSION TAG
SEQADV 4MEB HIS B 354 UNP D0BWK6 EXPRESSION TAG
SEQADV 4MEB HIS B 355 UNP D0BWK6 EXPRESSION TAG
SEQRES 1 A 331 GLU TYR ASP PRO ASN LEU LYS SER ILE ASP THR PRO PRO
SEQRES 2 A 331 ALA VAL SER GLN GLN MET PHE ASN LYS VAL LYS SER ASN
SEQRES 3 A 331 GLY LEU GLY GLN TYR ALA TYR ALA LYS GLY LEU SER SER
SEQRES 4 A 331 LYS PHE ILE GLU SER GLU GLY VAL LYS LEU HIS TYR VAL
SEQRES 5 A 331 GLU GLY GLY SER LYS GLY THR PRO ILE VAL PHE ILE HIS
SEQRES 6 A 331 GLY PHE GLY SER THR TRP LYS MET TRP GLU PRO VAL MET
SEQRES 7 A 331 LEU SER TYR MET LYS ASP HIS LYS VAL ILE ALA ILE ASP
SEQRES 8 A 331 LEU PRO GLY LEU GLY GLN SER GLY PRO ILE LEU ASN ASP
SEQRES 9 A 331 ASP TYR SER ALA GLU ASN THR SER LYS ILE LEU ILE GLY
SEQRES 10 A 331 ALA ILE LYS LYS ILE ALA GLY LYS GLY PRO ILE TYR TYR
SEQRES 11 A 331 VAL SER HIS SER LEU GLY ASN THR ALA SER TYR PRO LEU
SEQRES 12 A 331 VAL ALA ASN ASN GLN GLY TYR ILE LYS LYS ALA VAL PHE
SEQRES 13 A 331 MET ASP SER PRO ILE PRO ASP ARG ALA MET PHE GLU TYR
SEQRES 14 A 331 PRO GLY TYR THR ALA ASP GLY PRO GLY LEU GLY TRP HIS
SEQRES 15 A 331 PHE GLY TYR PHE SER PHE GLY ASP ILE ALA GLU LYS GLN
SEQRES 16 A 331 ILE ALA ASN ASP PRO ASN LEU PHE PHE SER TYR PHE ILE
SEQRES 17 A 331 LYS THR TYR ALA GLY LYS LYS GLU ILE PHE THR PRO GLU
SEQRES 18 A 331 LEU LEU ALA GLU LEU ILE GLU PRO TYR SER THR ARG ASP
SEQRES 19 A 331 LYS LEU LYS ALA ALA PHE GLY TYR TYR ARG SER HIS ALA
SEQRES 20 A 331 ASP SER ILE ARG GLN ASN GLU ALA LEU LEU ALA ASN GLY
SEQRES 21 A 331 LYS LYS LEU THR ILE PRO SER MET ALA LEU THR GLY GLN
SEQRES 22 A 331 LYS GLY VAL ASN ASP VAL LEU VAL LYS GLU MET ARG ALA
SEQRES 23 A 331 ARG PHE VAL ALA ASP PRO ALA GLN TYR THR ALA ILE ILE
SEQRES 24 A 331 LEU PRO ASP THR GLY HIS TRP MET VAL GLU GLU ASN ALA
SEQRES 25 A 331 GLU GLY VAL GLU LYS SER LEU SER ASN PHE LEU PHE LYS
SEQRES 26 A 331 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 331 GLU TYR ASP PRO ASN LEU LYS SER ILE ASP THR PRO PRO
SEQRES 2 B 331 ALA VAL SER GLN GLN MET PHE ASN LYS VAL LYS SER ASN
SEQRES 3 B 331 GLY LEU GLY GLN TYR ALA TYR ALA LYS GLY LEU SER SER
SEQRES 4 B 331 LYS PHE ILE GLU SER GLU GLY VAL LYS LEU HIS TYR VAL
SEQRES 5 B 331 GLU GLY GLY SER LYS GLY THR PRO ILE VAL PHE ILE HIS
SEQRES 6 B 331 GLY PHE GLY SER THR TRP LYS MET TRP GLU PRO VAL MET
SEQRES 7 B 331 LEU SER TYR MET LYS ASP HIS LYS VAL ILE ALA ILE ASP
SEQRES 8 B 331 LEU PRO GLY LEU GLY GLN SER GLY PRO ILE LEU ASN ASP
SEQRES 9 B 331 ASP TYR SER ALA GLU ASN THR SER LYS ILE LEU ILE GLY
SEQRES 10 B 331 ALA ILE LYS LYS ILE ALA GLY LYS GLY PRO ILE TYR TYR
SEQRES 11 B 331 VAL SER HIS SER LEU GLY ASN THR ALA SER TYR PRO LEU
SEQRES 12 B 331 VAL ALA ASN ASN GLN GLY TYR ILE LYS LYS ALA VAL PHE
SEQRES 13 B 331 MET ASP SER PRO ILE PRO ASP ARG ALA MET PHE GLU TYR
SEQRES 14 B 331 PRO GLY TYR THR ALA ASP GLY PRO GLY LEU GLY TRP HIS
SEQRES 15 B 331 PHE GLY TYR PHE SER PHE GLY ASP ILE ALA GLU LYS GLN
SEQRES 16 B 331 ILE ALA ASN ASP PRO ASN LEU PHE PHE SER TYR PHE ILE
SEQRES 17 B 331 LYS THR TYR ALA GLY LYS LYS GLU ILE PHE THR PRO GLU
SEQRES 18 B 331 LEU LEU ALA GLU LEU ILE GLU PRO TYR SER THR ARG ASP
SEQRES 19 B 331 LYS LEU LYS ALA ALA PHE GLY TYR TYR ARG SER HIS ALA
SEQRES 20 B 331 ASP SER ILE ARG GLN ASN GLU ALA LEU LEU ALA ASN GLY
SEQRES 21 B 331 LYS LYS LEU THR ILE PRO SER MET ALA LEU THR GLY GLN
SEQRES 22 B 331 LYS GLY VAL ASN ASP VAL LEU VAL LYS GLU MET ARG ALA
SEQRES 23 B 331 ARG PHE VAL ALA ASP PRO ALA GLN TYR THR ALA ILE ILE
SEQRES 24 B 331 LEU PRO ASP THR GLY HIS TRP MET VAL GLU GLU ASN ALA
SEQRES 25 B 331 GLU GLY VAL GLU LYS SER LEU SER ASN PHE LEU PHE LYS
SEQRES 26 B 331 HIS HIS HIS HIS HIS HIS
HET PO4 A 401 5
HET GOL A 402 6
HET PO4 B 401 5
HET PO4 B 402 5
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 PO4 3(O4 P 3-)
FORMUL 4 GOL C3 H8 O3
FORMUL 7 HOH *562(H2 O)
HELIX 1 1 PRO A 36 ASN A 50 1 15
HELIX 2 2 LEU A 52 ALA A 56 5 5
HELIX 3 3 THR A 94 MET A 97 5 4
HELIX 4 4 TRP A 98 MET A 106 1 9
HELIX 5 5 SER A 131 GLY A 148 1 18
HELIX 6 6 SER A 158 ASN A 171 1 14
HELIX 7 7 ASP A 187 GLU A 192 5 6
HELIX 8 8 GLY A 204 PHE A 210 1 7
HELIX 9 9 ASP A 214 ASP A 223 1 10
HELIX 10 10 ASP A 223 ALA A 236 1 14
HELIX 11 11 LYS A 238 PHE A 242 5 5
HELIX 12 12 THR A 243 GLU A 252 1 10
HELIX 13 13 PRO A 253 SER A 255 5 3
HELIX 14 14 THR A 256 SER A 269 1 14
HELIX 15 15 SER A 269 ASN A 283 1 15
HELIX 16 16 ASP A 302 PHE A 312 1 11
HELIX 17 17 ASP A 315 ALA A 317 5 3
HELIX 18 18 TRP A 330 PHE A 348 1 19
HELIX 19 19 PRO B 36 ASN B 50 1 15
HELIX 20 20 LEU B 52 ALA B 56 5 5
HELIX 21 21 THR B 94 MET B 97 5 4
HELIX 22 22 TRP B 98 MET B 106 1 9
HELIX 23 23 SER B 131 GLY B 148 1 18
HELIX 24 24 SER B 158 ASN B 170 1 13
HELIX 25 25 ASP B 187 GLU B 192 5 6
HELIX 26 26 GLY B 204 PHE B 210 1 7
HELIX 27 27 ASP B 214 ASP B 223 1 10
HELIX 28 28 ASP B 223 ALA B 236 1 14
HELIX 29 29 LYS B 238 PHE B 242 5 5
HELIX 30 30 THR B 243 GLU B 252 1 10
HELIX 31 31 PRO B 253 SER B 255 5 3
HELIX 32 32 THR B 256 SER B 269 1 14
HELIX 33 33 SER B 269 ASN B 283 1 15
HELIX 34 34 ASP B 302 PHE B 312 1 11
HELIX 35 35 ASP B 315 ALA B 317 5 3
HELIX 36 36 TRP B 330 PHE B 348 1 19
SHEET 1 A 8 SER A 62 SER A 68 0
SHEET 2 A 8 VAL A 71 GLY A 78 -1 O LEU A 73 N ILE A 66
SHEET 3 A 8 VAL A 111 ILE A 114 -1 O ALA A 113 N VAL A 76
SHEET 4 A 8 ILE A 85 ILE A 88 1 N PHE A 87 O ILE A 112
SHEET 5 A 8 ILE A 152 HIS A 157 1 O VAL A 155 N VAL A 86
SHEET 6 A 8 ILE A 175 MET A 181 1 O LYS A 176 N ILE A 152
SHEET 7 A 8 SER A 291 GLY A 296 1 O MET A 292 N PHE A 180
SHEET 8 A 8 TYR A 319 LEU A 324 1 O LEU A 324 N THR A 295
SHEET 1 B 2 TYR A 196 THR A 197 0
SHEET 2 B 2 GLY A 200 PRO A 201 -1 O GLY A 200 N THR A 197
SHEET 1 C 8 LEU B 61 SER B 68 0
SHEET 2 C 8 VAL B 71 GLY B 78 -1 O LEU B 73 N ILE B 66
SHEET 3 C 8 VAL B 111 ILE B 114 -1 O VAL B 111 N GLY B 78
SHEET 4 C 8 ILE B 85 ILE B 88 1 N PHE B 87 O ILE B 112
SHEET 5 C 8 ILE B 152 HIS B 157 1 O VAL B 155 N VAL B 86
SHEET 6 C 8 ILE B 175 MET B 181 1 O LYS B 176 N ILE B 152
SHEET 7 C 8 SER B 291 GLY B 296 1 O MET B 292 N PHE B 180
SHEET 8 C 8 TYR B 319 LEU B 324 1 O LEU B 324 N THR B 295
SHEET 1 D 2 TYR B 196 THR B 197 0
SHEET 2 D 2 GLY B 200 PRO B 201 -1 O GLY B 200 N THR B 197
CISPEP 1 GLY A 150 PRO A 151 0 -0.61
CISPEP 2 GLY B 150 PRO B 151 0 1.55
SITE 1 AC1 7 SER A 158 SER A 183 HIS A 206 PHE A 207
SITE 2 AC1 7 TYR A 267 HOH A 559 HOH A 650
SITE 1 AC2 7 LYS A 48 TYR A 55 GLU A 252 THR A 256
SITE 2 AC2 7 LYS A 259 HOH A 584 HOH A 729
SITE 1 AC3 4 ASP B 214 GLU B 217 ARG B 257 LYS B 261
SITE 1 AC4 9 SER B 158 LEU B 159 SER B 183 PRO B 184
SITE 2 AC4 9 HIS B 206 PHE B 207 TYR B 267 HOH B 684
SITE 3 AC4 9 HOH B 688
CRYST1 86.109 42.511 86.907 90.00 98.38 90.00 P 1 21 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 0.011613 0.000000 0.001712 0.00000
SCALE2 0.000000 0.023523 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011631 0.00000
TER 2579 PHE A 348
TER 5132 PHE B 348
MASTER 307 0 4 36 20 0 8 6 5647 2 21 52
END |