| content |
HEADER HYDROLASE 16-JUL-15 5CML
TITLE CRYSTAL STRUCTURE OF THE ESTERASE DOMAIN FROM RHODOTHERMUS MARINUS
TITLE 2 RMAR_1206 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OSMC FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-255;
COMPND 5 SYNONYM: ESTERASE RMAR_1206;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOTHERMUS MARINUS;
SOURCE 3 ORGANISM_TAXID: 29549;
SOURCE 4 GENE: RMAR_1206;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: AI;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDEST17
KEYWDS SERINE ESTERASE OSMC THERMOPHILE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.MARLES-WRIGHT,C.WARDROPE,M.-B.V.JENSEN,L.E.HORSFALL,P.D.TOGNERI,
AUTHOR 2 S.J.ROSSER
REVDAT 1 27-JUL-16 5CML 0
JRNL AUTH J.MARLES-WRIGHT,C.WARDROPE,M.-B.V.JENSEN,L.E.HORSFALL,
JRNL AUTH 2 P.D.TOGNERI
JRNL TITL CHARACTERISATION OF A NOVEL FAMILY OF CARBOXYL ESTERASES
JRNL TITL 2 WITH OSMC DOMAINS FROM EXTREMOPHILIC AND MESOPHILIC BACTERIA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 69880
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3544
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 44.6427 - 4.5482 0.97 2693 136 0.1608 0.1800
REMARK 3 2 4.5482 - 3.6106 0.97 2632 145 0.1402 0.1514
REMARK 3 3 3.6106 - 3.1543 0.97 2607 149 0.1421 0.1515
REMARK 3 4 3.1543 - 2.8660 0.97 2612 133 0.1513 0.2035
REMARK 3 5 2.8660 - 2.6606 0.98 2602 155 0.1461 0.1706
REMARK 3 6 2.6606 - 2.5037 0.99 2681 133 0.1384 0.1811
REMARK 3 7 2.5037 - 2.3784 0.99 2661 142 0.1235 0.1632
REMARK 3 8 2.3784 - 2.2748 1.00 2666 139 0.1219 0.1793
REMARK 3 9 2.2748 - 2.1873 1.00 2674 141 0.1230 0.1542
REMARK 3 10 2.1873 - 2.1118 1.00 2659 147 0.1231 0.1743
REMARK 3 11 2.1118 - 2.0458 1.00 2685 151 0.1251 0.1699
REMARK 3 12 2.0458 - 1.9873 1.00 2616 170 0.1289 0.1696
REMARK 3 13 1.9873 - 1.9350 1.00 2687 130 0.1262 0.1886
REMARK 3 14 1.9350 - 1.8877 1.00 2655 133 0.1243 0.1757
REMARK 3 15 1.8877 - 1.8448 1.00 2646 135 0.1266 0.1724
REMARK 3 16 1.8448 - 1.8056 1.00 2686 157 0.1339 0.1957
REMARK 3 17 1.8056 - 1.7695 1.00 2654 137 0.1344 0.1910
REMARK 3 18 1.7695 - 1.7361 1.00 2706 122 0.1406 0.1669
REMARK 3 19 1.7361 - 1.7051 1.00 2657 150 0.1472 0.2178
REMARK 3 20 1.7051 - 1.6762 1.00 2652 141 0.1609 0.2047
REMARK 3 21 1.6762 - 1.6491 1.00 2646 162 0.1736 0.2474
REMARK 3 22 1.6491 - 1.6237 1.00 2674 115 0.1974 0.2552
REMARK 3 23 1.6237 - 1.5999 1.00 2653 139 0.2231 0.2968
REMARK 3 24 1.5999 - 1.5773 1.00 2660 150 0.2561 0.3017
REMARK 3 25 1.5773 - 1.5560 0.97 2572 132 0.2945 0.3251
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.500
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 : 0.010 3710
REMARK 3 ANGLE : 1.179 5032
REMARK 3 CHIRALITY : 0.047 579
REMARK 3 PLANARITY : 0.006 659
REMARK 3 DIHEDRAL : 13.245 1355
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 5CML COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211869.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
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 : SINGLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69888
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560
REMARK 200 RESOLUTION RANGE LOW (A) : 44.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.72500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.880
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2FUK, 3TRD, 3PF9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 15 MG/ML WAS CRYSTALLIZED
REMARK 280 BY SITTING DROP VAPOUR DIFFUSION WITH 100 NL DROPS OF PROTEIN
REMARK 280 SUPPLEMENTED WITH 100 NL OF MOTHER LIQUOR COMPRISING 0.2 M
REMARK 280 AMMONIUM CITRATE DIBASIC, PH 5.0, 20 % W/V PEG 3350 (HAMPTON PEG/
REMARK 280 ION HT96 SCREEN D12), DROPS WERE EQUILIBRATED AGAINST 70 UL OF
REMARK 280 MOTHER LIQUOR FOR ONE MONTH BEFORE CRYSTALS APPEARED., VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 37.03450
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLU A 71
REMARK 465 SER A 72
REMARK 465 GLU A 73
REMARK 465 GLY A 74
REMARK 465 ASP A 75
REMARK 465 PHE A 76
REMARK 465 SER A 77
REMARK 465 GLU A 78
REMARK 465 THR A 79
REMARK 465 THR A 80
REMARK 465 PHE A 81
REMARK 465 ILE A 151
REMARK 465 LYS A 152
REMARK 465 ARG A 254
REMARK 465 ARG A 255
REMARK 465 LEU A 256
REMARK 465 GLY A 257
REMARK 465 HIS A 258
REMARK 465 HIS A 259
REMARK 465 HIS A 260
REMARK 465 HIS A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 MET B 1
REMARK 465 GLU B 71
REMARK 465 SER B 72
REMARK 465 GLU B 73
REMARK 465 GLY B 74
REMARK 465 ASP B 75
REMARK 465 PHE B 76
REMARK 465 SER B 77
REMARK 465 GLU B 78
REMARK 465 THR B 79
REMARK 465 THR B 80
REMARK 465 PHE B 81
REMARK 465 ALA B 82
REMARK 465 THR B 83
REMARK 465 ASP B 149
REMARK 465 THR B 150
REMARK 465 ILE B 151
REMARK 465 LYS B 152
REMARK 465 THR B 153
REMARK 465 VAL B 154
REMARK 465 GLY B 155
REMARK 465 LYS B 169
REMARK 465 LYS B 170
REMARK 465 GLN B 171
REMARK 465 PHE B 172
REMARK 465 LEU B 173
REMARK 465 GLU B 174
REMARK 465 ARG B 254
REMARK 465 ARG B 255
REMARK 465 LEU B 256
REMARK 465 GLY B 257
REMARK 465 HIS B 258
REMARK 465 HIS B 259
REMARK 465 HIS B 260
REMARK 465 HIS B 261
REMARK 465 HIS B 262
REMARK 465 HIS B 263
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 401 O HOH A 539 2.00
REMARK 500 O HOH A 488 O HOH B 500 2.19
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 TYR A 99 -121.80 -133.20
REMARK 500 SER A 109 -129.63 60.26
REMARK 500 ASN A 180 107.66 68.92
REMARK 500 ASP A 225 -101.92 51.14
REMARK 500 ASP B 25 108.71 -46.69
REMARK 500 TYR B 99 -115.57 -131.00
REMARK 500 SER B 109 -127.10 60.59
REMARK 500 ASN B 180 110.54 75.98
REMARK 500 ASP B 225 -94.06 48.09
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 PGE A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 301
DBREF 5CML A 1 255 UNP D0MHY8 D0MHY8_RHOM4 1 255
DBREF 5CML B 1 255 UNP D0MHY8 D0MHY8_RHOM4 1 255
SEQADV 5CML LEU A 256 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML GLY A 257 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML HIS A 258 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML HIS A 259 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML HIS A 260 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML HIS A 261 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML HIS A 262 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML HIS A 263 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML LEU B 256 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML GLY B 257 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML HIS B 258 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML HIS B 259 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML HIS B 260 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML HIS B 261 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML HIS B 262 UNP D0MHY8 EXPRESSION TAG
SEQADV 5CML HIS B 263 UNP D0MHY8 EXPRESSION TAG
SEQRES 1 A 263 MET GLN ILE LYS THR VAL THR PHE GLU ASN ASN ARG GLY
SEQRES 2 A 263 GLU ARG LEU ALA ALA ARG LEU ASP LEU PRO VAL ASP THR
SEQRES 3 A 263 GLN PRO VAL ALA TYR ALA LEU PHE ALA HIS CYS PHE THR
SEQRES 4 A 263 CYS SER LYS ASN LEU LYS ALA VAL THR THR ILE SER ARG
SEQRES 5 A 263 ALA LEU THR THR GLN GLY TYR ALA VAL LEU ARG PHE ASP
SEQRES 6 A 263 PHE THR GLY LEU GLY GLU SER GLU GLY ASP PHE SER GLU
SEQRES 7 A 263 THR THR PHE ALA THR ASN PHE GLU ASP LEU ARG ALA ALA
SEQRES 8 A 263 CYS ARG PHE LEU SER ALA GLN TYR GLU PRO PRO ALA LEU
SEQRES 9 A 263 LEU ILE GLY HIS SER LEU GLY GLY ALA ALA VAL LEU ALA
SEQRES 10 A 263 VAL ALA GLY GLU PHE PRO GLU VAL LYS ALA VAL ALA THR
SEQRES 11 A 263 ILE GLY ALA PRO CYS ASP PRO ALA HIS VAL ARG HIS LEU
SEQRES 12 A 263 LEU ARG PRO ALA LEU ASP THR ILE LYS THR VAL GLY GLU
SEQRES 13 A 263 ALA VAL VAL ASP LEU GLY GLY ARG PRO PHE ARG ILE LYS
SEQRES 14 A 263 LYS GLN PHE LEU GLU GLU LEU GLU ARG VAL ASN LEU GLU
SEQRES 15 A 263 ASP GLN VAL ARG THR MET ARG ARG PRO LEU LEU LEU PHE
SEQRES 16 A 263 HIS SER PRO THR ASP GLN ILE VAL GLY ILE GLU ASN ALA
SEQRES 17 A 263 ALA CYS LEU PHE GLN ALA ALA ARG HIS PRO LYS SER PHE
SEQRES 18 A 263 VAL SER LEU ASP GLN ALA ASP HIS LEU LEU SER ASN SER
SEQRES 19 A 263 ASP ASP ALA ALA PHE VAL GLY GLU VAL LEU GLY ALA TRP
SEQRES 20 A 263 ALA ARG ARG TYR VAL GLY ARG ARG LEU GLY HIS HIS HIS
SEQRES 21 A 263 HIS HIS HIS
SEQRES 1 B 263 MET GLN ILE LYS THR VAL THR PHE GLU ASN ASN ARG GLY
SEQRES 2 B 263 GLU ARG LEU ALA ALA ARG LEU ASP LEU PRO VAL ASP THR
SEQRES 3 B 263 GLN PRO VAL ALA TYR ALA LEU PHE ALA HIS CYS PHE THR
SEQRES 4 B 263 CYS SER LYS ASN LEU LYS ALA VAL THR THR ILE SER ARG
SEQRES 5 B 263 ALA LEU THR THR GLN GLY TYR ALA VAL LEU ARG PHE ASP
SEQRES 6 B 263 PHE THR GLY LEU GLY GLU SER GLU GLY ASP PHE SER GLU
SEQRES 7 B 263 THR THR PHE ALA THR ASN PHE GLU ASP LEU ARG ALA ALA
SEQRES 8 B 263 CYS ARG PHE LEU SER ALA GLN TYR GLU PRO PRO ALA LEU
SEQRES 9 B 263 LEU ILE GLY HIS SER LEU GLY GLY ALA ALA VAL LEU ALA
SEQRES 10 B 263 VAL ALA GLY GLU PHE PRO GLU VAL LYS ALA VAL ALA THR
SEQRES 11 B 263 ILE GLY ALA PRO CYS ASP PRO ALA HIS VAL ARG HIS LEU
SEQRES 12 B 263 LEU ARG PRO ALA LEU ASP THR ILE LYS THR VAL GLY GLU
SEQRES 13 B 263 ALA VAL VAL ASP LEU GLY GLY ARG PRO PHE ARG ILE LYS
SEQRES 14 B 263 LYS GLN PHE LEU GLU GLU LEU GLU ARG VAL ASN LEU GLU
SEQRES 15 B 263 ASP GLN VAL ARG THR MET ARG ARG PRO LEU LEU LEU PHE
SEQRES 16 B 263 HIS SER PRO THR ASP GLN ILE VAL GLY ILE GLU ASN ALA
SEQRES 17 B 263 ALA CYS LEU PHE GLN ALA ALA ARG HIS PRO LYS SER PHE
SEQRES 18 B 263 VAL SER LEU ASP GLN ALA ASP HIS LEU LEU SER ASN SER
SEQRES 19 B 263 ASP ASP ALA ALA PHE VAL GLY GLU VAL LEU GLY ALA TRP
SEQRES 20 B 263 ALA ARG ARG TYR VAL GLY ARG ARG LEU GLY HIS HIS HIS
SEQRES 21 B 263 HIS HIS HIS
HET PGE A 301 24
HET PGE B 301 24
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 3 PGE 2(C6 H14 O4)
FORMUL 5 HOH *280(H2 O)
HELIX 1 AA1 CYS A 37 SER A 41 5 5
HELIX 2 AA2 LEU A 44 GLN A 57 1 14
HELIX 3 AA3 ASN A 84 TYR A 99 1 16
HELIX 4 AA4 SER A 109 ALA A 119 1 11
HELIX 5 AA5 GLY A 120 PHE A 122 5 3
HELIX 6 AA6 ASP A 136 HIS A 142 1 7
HELIX 7 AA7 LYS A 170 ASN A 180 1 11
HELIX 8 AA8 ASN A 180 MET A 188 1 9
HELIX 9 AA9 ILE A 205 ALA A 215 1 11
HELIX 10 AB1 ASN A 233 GLY A 253 1 21
HELIX 11 AB2 CYS B 37 SER B 41 5 5
HELIX 12 AB3 LEU B 44 GLN B 57 1 14
HELIX 13 AB4 PHE B 85 TYR B 99 1 15
HELIX 14 AB5 SER B 109 ALA B 119 1 11
HELIX 15 AB6 GLY B 120 PHE B 122 5 3
HELIX 16 AB7 ASP B 136 HIS B 142 1 7
HELIX 17 AB8 LEU B 176 ASN B 180 1 5
HELIX 18 AB9 ASN B 180 MET B 188 1 9
HELIX 19 AC1 ILE B 205 ALA B 215 1 11
HELIX 20 AC2 ASN B 233 GLY B 253 1 21
SHEET 1 AA1 8 GLN A 2 GLU A 9 0
SHEET 2 AA1 8 ARG A 15 LEU A 22 -1 O LEU A 16 N PHE A 8
SHEET 3 AA1 8 TYR A 59 ASP A 65 -1 O VAL A 61 N ASP A 21
SHEET 4 AA1 8 ALA A 30 HIS A 36 1 N ALA A 32 O LEU A 62
SHEET 5 AA1 8 LEU A 104 HIS A 108 1 O ILE A 106 N LEU A 33
SHEET 6 AA1 8 ALA A 127 ILE A 131 1 O ALA A 129 N LEU A 105
SHEET 7 AA1 8 LEU A 192 HIS A 196 1 O PHE A 195 N THR A 130
SHEET 8 AA1 8 LYS A 219 SER A 223 1 O VAL A 222 N LEU A 194
SHEET 1 AA2 3 LEU A 144 PRO A 146 0
SHEET 2 AA2 3 GLU A 156 VAL A 159 -1 O VAL A 158 N ARG A 145
SHEET 3 AA2 3 PHE A 166 LYS A 169 -1 O PHE A 166 N VAL A 159
SHEET 1 AA3 8 ILE B 3 GLU B 9 0
SHEET 2 AA3 8 ARG B 15 ASP B 21 -1 O LEU B 16 N PHE B 8
SHEET 3 AA3 8 TYR B 59 ASP B 65 -1 O ARG B 63 N ARG B 19
SHEET 4 AA3 8 ALA B 30 HIS B 36 1 N ALA B 32 O LEU B 62
SHEET 5 AA3 8 LEU B 104 HIS B 108 1 O ILE B 106 N LEU B 33
SHEET 6 AA3 8 ALA B 127 ILE B 131 1 O ALA B 129 N LEU B 105
SHEET 7 AA3 8 LEU B 192 HIS B 196 1 O PHE B 195 N THR B 130
SHEET 8 AA3 8 LYS B 219 SER B 223 1 O VAL B 222 N LEU B 194
SHEET 1 AA4 3 LEU B 144 PRO B 146 0
SHEET 2 AA4 3 ALA B 157 VAL B 159 -1 O VAL B 158 N ARG B 145
SHEET 3 AA4 3 PHE B 166 ILE B 168 -1 O PHE B 166 N VAL B 159
SSBOND 1 CYS A 135 CYS A 210 1555 1555 2.03
SSBOND 2 CYS B 135 CYS B 210 1555 1555 2.08
CISPEP 1 HIS A 217 PRO A 218 0 -0.73
CISPEP 2 HIS B 217 PRO B 218 0 -1.57
SITE 1 AC1 6 HIS A 217 HOH A 483 ALA B 209 PHE B 212
SITE 2 AC1 6 PHE B 221 PGE B 301
SITE 1 AC2 6 ALA A 209 GLN A 213 PHE A 221 PGE A 301
SITE 2 AC2 6 HIS B 217 HOH B 453
CRYST1 60.325 74.069 60.953 90.00 113.47 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 0.016577 0.000000 0.007198 0.00000
SCALE2 0.000000 0.013501 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017886 0.00000
TER 3733 GLY A 253
TER 7252 GLY B 253
MASTER 328 0 2 20 22 0 4 6 3884 2 52 42
END |