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HEADER HYDROLASE 02-OCT-17 6EMI
TITLE CRYSTAL STRUCTURE OF A VARIANT OF HUMAN BUTYRYLCHOLINESTERASE
TITLE 2 EXPRESSED IN BACTERIA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE
COMPND 5 ESTERASE II,PSEUDOCHOLINESTERASE;
COMPND 6 EC: 3.1.1.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: A AND B CHAINS WERE NUMBERED ACCORDING TO THE SEQUENCE
COMPND 10 OF THE PHYSIOLOGICAL HUMAN BUTYRYLCHOLINAESTERASE.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCHE, CHE1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA-BETA HYDROLASE, PROKARYOTIC EXPRESSION, DIMERIC FORM, DISULFIDE
KEYWDS 2 BOND., HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.BRAZZOLOTTO,A.IGERT,V.GUILLON,G.SANTONI,F.NACHON
REVDAT 1 08-NOV-17 6EMI 0
JRNL AUTH X.BRAZZOLOTTO,A.IGERT,V.GUILLON,G.SANTONI,F.NACHON
JRNL TITL BACTERIAL EXPRESSION OF HUMAN BUTYRYLCHOLINESTERASE AS A
JRNL TITL 2 TOOL FOR NERVE AGENT BIOSCAVENGERS DEVELOPMENT.
JRNL REF MOLECULES V. 22 2017
JRNL REFN ESSN 1420-3049
JRNL PMID 29077024
JRNL DOI 10.3390/MOLECULES22111828
REMARK 2
REMARK 2 RESOLUTION. 2.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 50941
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2576
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 68.6477 - 6.4867 0.96 2744 137 0.1934 0.2198
REMARK 3 2 6.4867 - 5.1492 0.99 2740 144 0.2174 0.2402
REMARK 3 3 5.1492 - 4.4985 0.99 2726 151 0.1844 0.1986
REMARK 3 4 4.4985 - 4.0872 0.98 2679 160 0.1852 0.1887
REMARK 3 5 4.0872 - 3.7943 0.99 2713 119 0.1939 0.2530
REMARK 3 6 3.7943 - 3.5706 0.99 2703 138 0.2048 0.2552
REMARK 3 7 3.5706 - 3.3918 0.99 2678 152 0.2159 0.2311
REMARK 3 8 3.3918 - 3.2441 0.99 2682 158 0.2278 0.3127
REMARK 3 9 3.2441 - 3.1193 0.99 2660 158 0.2352 0.2971
REMARK 3 10 3.1193 - 3.0116 0.99 2698 149 0.2415 0.2628
REMARK 3 11 3.0116 - 2.9174 0.98 2662 162 0.2455 0.3044
REMARK 3 12 2.9174 - 2.8341 0.98 2679 123 0.2597 0.2669
REMARK 3 13 2.8341 - 2.7594 0.99 2645 141 0.2575 0.3388
REMARK 3 14 2.7594 - 2.6921 0.98 2694 154 0.2772 0.3015
REMARK 3 15 2.6921 - 2.6309 0.98 2696 136 0.2844 0.2977
REMARK 3 16 2.6309 - 2.5749 0.98 2647 122 0.2942 0.3408
REMARK 3 17 2.5749 - 2.5234 0.98 2619 132 0.2823 0.3275
REMARK 3 18 2.5234 - 2.4758 0.98 2700 140 0.3004 0.3241
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.190
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 8853
REMARK 3 ANGLE : 0.531 11939
REMARK 3 CHIRALITY : 0.043 1237
REMARK 3 PLANARITY : 0.004 1541
REMARK 3 DIHEDRAL : 12.448 6209
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 6EMI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200006817.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.074
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51072
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.476
REMARK 200 RESOLUTION RANGE LOW (A) : 65.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.11630
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.53030
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: PHASER
REMARK 200 STARTING MODEL: 1P0I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM ACETATE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 79.92000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.58500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 79.92000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.58500
REMARK 290 SMTRY3 4 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: DIMERIC
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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 152.66428
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 121.85891
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 GLY A -2
REMARK 465 ALA A -1
REMARK 465 MET A 0
REMARK 465 GLU A 1
REMARK 465 ASP A 2
REMARK 465 GLY B -2
REMARK 465 ALA B -1
REMARK 465 MET B 0
REMARK 465 GLU B 1
REMARK 465 ASP B 2
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 PHE A 278 CZ
REMARK 480 GLU B 255 CG CD OE1 OE2
REMARK 480 GLU B 259 CG
REMARK 480 LYS B 348 CD CE NZ
REMARK 480 LYS B 355 CD CE NZ
REMARK 480 PHE B 525 CZ
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 OD2 ASP B 378 O HOH B 701 2.17
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 PHE A 43 -3.39 75.51
REMARK 500 ALA A 162 72.25 -158.22
REMARK 500 ARG A 191 46.39 -145.33
REMARK 500 SER A 198 -121.09 57.47
REMARK 500 ASP A 297 -77.00 -112.76
REMARK 500 ASP A 324 76.38 -117.41
REMARK 500 PHE A 398 -60.48 -138.56
REMARK 500 ASN A 485 24.00 -70.50
REMARK 500 THR A 496 -76.45 -86.43
REMARK 500 GLU A 506 -79.73 -74.45
REMARK 500 ALA B 58 68.72 -114.44
REMARK 500 PHE B 153 17.92 -144.00
REMARK 500 ALA B 162 72.77 -159.93
REMARK 500 ARG B 191 48.94 -144.60
REMARK 500 SER B 198 -121.38 59.84
REMARK 500 PRO B 281 -75.59 -67.11
REMARK 500 ASP B 297 -70.35 -110.09
REMARK 500 GLU B 377 -4.65 81.49
REMARK 500 PHE B 398 -62.65 -138.68
REMARK 500 PRO B 480 42.51 -82.93
REMARK 500 GLU B 506 -67.74 -93.38
REMARK 500 SER B 507 -99.06 -109.70
REMARK 500 SER B 508 70.13 95.15
REMARK 500 LYS B 513 70.17 56.65
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 EDO A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 B 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 B 624
DBREF 6EMI A 1 529 UNP P06276 CHLE_HUMAN 29 557
DBREF 6EMI B 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 6EMI GLY A -2 UNP P06276 EXPRESSION TAG
SEQADV 6EMI ALA A -1 UNP P06276 EXPRESSION TAG
SEQADV 6EMI MET A 0 UNP P06276 EXPRESSION TAG
SEQADV 6EMI THR A 7 UNP P06276 ALA 35 ENGINEERED MUTATION
SEQADV 6EMI PRO A 48 UNP P06276 SER 76 ENGINEERED MUTATION
SEQADV 6EMI GLY A 54 UNP P06276 ASP 82 ENGINEERED MUTATION
SEQADV 6EMI MET A 66 UNP P06276 CYS 94 ENGINEERED MUTATION
SEQADV 6EMI THR A 71 UNP P06276 GLN 99 ENGINEERED MUTATION
SEQADV 6EMI MET A 110 UNP P06276 LEU 138 ENGINEERED MUTATION
SEQADV 6EMI VAL A 111 UNP P06276 ILE 139 ENGINEERED MUTATION
SEQADV 6EMI PRO A 126 UNP P06276 HIS 154 ENGINEERED MUTATION
SEQADV 6EMI LYS A 176 UNP P06276 GLN 204 ENGINEERED MUTATION
SEQADV 6EMI ASP A 180 UNP P06276 LYS 208 ENGINEERED MUTATION
SEQADV 6EMI ASP A 188 UNP P06276 ASN 216 ENGINEERED MUTATION
SEQADV 6EMI ASN A 190 UNP P06276 LYS 218 ENGINEERED MUTATION
SEQADV 6EMI ARG A 191 UNP P06276 SER 219 ENGINEERED MUTATION
SEQADV 6EMI PRO A 215 UNP P06276 SER 243 ENGINEERED MUTATION
SEQADV 6EMI ALA A 227 UNP P06276 PHE 255 ENGINEERED MUTATION
SEQADV 6EMI MET A 234 UNP P06276 THR 262 ENGINEERED MUTATION
SEQADV 6EMI PRO A 236 UNP P06276 LEU 264 ENGINEERED MUTATION
SEQADV 6EMI GLU A 237 UNP P06276 TYR 265 ENGINEERED MUTATION
SEQADV 6EMI LEU A 250 UNP P06276 THR 278 ENGINEERED MUTATION
SEQADV 6EMI ASP A 274 UNP P06276 LEU 302 ENGINEERED MUTATION
SEQADV 6EMI SER A 283 UNP P06276 GLY 311 ENGINEERED MUTATION
SEQADV 6EMI THR A 305 UNP P06276 ILE 333 ENGINEERED MUTATION
SEQADV 6EMI ASP A 342 UNP P06276 ASN 370 ENGINEERED MUTATION
SEQADV 6EMI VAL A 356 UNP P06276 ILE 384 ENGINEERED MUTATION
SEQADV 6EMI ASN A 360 UNP P06276 GLY 388 ENGINEERED MUTATION
SEQADV 6EMI GLU A 377 UNP P06276 VAL 405 ENGINEERED MUTATION
SEQADV 6EMI GLU A 379 UNP P06276 ASP 407 ENGINEERED MUTATION
SEQADV 6EMI ASP A 380 UNP P06276 GLN 408 ENGINEERED MUTATION
SEQADV 6EMI ASP A 387 UNP P06276 GLU 415 ENGINEERED MUTATION
SEQADV 6EMI ALA A 390 UNP P06276 GLY 418 ENGINEERED MUTATION
SEQADV 6EMI GLU A 391 UNP P06276 ASP 419 ENGINEERED MUTATION
SEQADV 6EMI PHE A 397 UNP P06276 ASN 425 ENGINEERED MUTATION
SEQADV 6EMI ALA A 406 UNP P06276 THR 434 ENGINEERED MUTATION
SEQADV 6EMI TYR A 409 UNP P06276 PHE 437 ENGINEERED MUTATION
SEQADV 6EMI ALA A 410 UNP P06276 SER 438 ENGINEERED MUTATION
SEQADV 6EMI HIS A 412 UNP P06276 TRP 440 ENGINEERED MUTATION
SEQADV 6EMI TYR A 417 UNP P06276 PHE 445 ENGINEERED MUTATION
SEQADV 6EMI LEU A 454 UNP P06276 ASP 482 ENGINEERED MUTATION
SEQADV 6EMI GLU A 459 UNP P06276 ALA 487 ENGINEERED MUTATION
SEQADV 6EMI GLU A 466 UNP P06276 SER 494 ENGINEERED MUTATION
SEQADV 6EMI MET A 468 UNP P06276 VAL 496 ENGINEERED MUTATION
SEQADV 6EMI ARG A 469 UNP P06276 LYS 497 ENGINEERED MUTATION
SEQADV 6EMI GLN A 489 UNP P06276 SER 517 ENGINEERED MUTATION
SEQADV 6EMI PRO A 495 UNP P06276 SER 523 ENGINEERED MUTATION
SEQADV 6EMI SER A 508 UNP P06276 THR 536 ENGINEERED MUTATION
SEQADV 6EMI HIS A 518 UNP P06276 GLN 546 ENGINEERED MUTATION
SEQADV 6EMI ASN A 523 UNP P06276 THR 551 ENGINEERED MUTATION
SEQADV 6EMI GLY B -2 UNP P06276 EXPRESSION TAG
SEQADV 6EMI ALA B -1 UNP P06276 EXPRESSION TAG
SEQADV 6EMI MET B 0 UNP P06276 EXPRESSION TAG
SEQADV 6EMI THR B 7 UNP P06276 ALA 35 ENGINEERED MUTATION
SEQADV 6EMI PRO B 48 UNP P06276 SER 76 ENGINEERED MUTATION
SEQADV 6EMI GLY B 54 UNP P06276 ASP 82 ENGINEERED MUTATION
SEQADV 6EMI MET B 66 UNP P06276 CYS 94 ENGINEERED MUTATION
SEQADV 6EMI THR B 71 UNP P06276 GLN 99 ENGINEERED MUTATION
SEQADV 6EMI MET B 110 UNP P06276 LEU 138 ENGINEERED MUTATION
SEQADV 6EMI VAL B 111 UNP P06276 ILE 139 ENGINEERED MUTATION
SEQADV 6EMI PRO B 126 UNP P06276 HIS 154 ENGINEERED MUTATION
SEQADV 6EMI LYS B 176 UNP P06276 GLN 204 ENGINEERED MUTATION
SEQADV 6EMI ASP B 180 UNP P06276 LYS 208 ENGINEERED MUTATION
SEQADV 6EMI ASP B 188 UNP P06276 ASN 216 ENGINEERED MUTATION
SEQADV 6EMI ASN B 190 UNP P06276 LYS 218 ENGINEERED MUTATION
SEQADV 6EMI ARG B 191 UNP P06276 SER 219 ENGINEERED MUTATION
SEQADV 6EMI PRO B 215 UNP P06276 SER 243 ENGINEERED MUTATION
SEQADV 6EMI ALA B 227 UNP P06276 PHE 255 ENGINEERED MUTATION
SEQADV 6EMI MET B 234 UNP P06276 THR 262 ENGINEERED MUTATION
SEQADV 6EMI PRO B 236 UNP P06276 LEU 264 ENGINEERED MUTATION
SEQADV 6EMI GLU B 237 UNP P06276 TYR 265 ENGINEERED MUTATION
SEQADV 6EMI LEU B 250 UNP P06276 THR 278 ENGINEERED MUTATION
SEQADV 6EMI ASP B 274 UNP P06276 LEU 302 ENGINEERED MUTATION
SEQADV 6EMI SER B 283 UNP P06276 GLY 311 ENGINEERED MUTATION
SEQADV 6EMI THR B 305 UNP P06276 ILE 333 ENGINEERED MUTATION
SEQADV 6EMI ASP B 342 UNP P06276 ASN 370 ENGINEERED MUTATION
SEQADV 6EMI VAL B 356 UNP P06276 ILE 384 ENGINEERED MUTATION
SEQADV 6EMI ASN B 360 UNP P06276 GLY 388 ENGINEERED MUTATION
SEQADV 6EMI GLU B 377 UNP P06276 VAL 405 ENGINEERED MUTATION
SEQADV 6EMI GLU B 379 UNP P06276 ASP 407 ENGINEERED MUTATION
SEQADV 6EMI ASP B 380 UNP P06276 GLN 408 ENGINEERED MUTATION
SEQADV 6EMI ASP B 387 UNP P06276 GLU 415 ENGINEERED MUTATION
SEQADV 6EMI ALA B 390 UNP P06276 GLY 418 ENGINEERED MUTATION
SEQADV 6EMI GLU B 391 UNP P06276 ASP 419 ENGINEERED MUTATION
SEQADV 6EMI PHE B 397 UNP P06276 ASN 425 ENGINEERED MUTATION
SEQADV 6EMI ALA B 406 UNP P06276 THR 434 ENGINEERED MUTATION
SEQADV 6EMI TYR B 409 UNP P06276 PHE 437 ENGINEERED MUTATION
SEQADV 6EMI ALA B 410 UNP P06276 SER 438 ENGINEERED MUTATION
SEQADV 6EMI HIS B 412 UNP P06276 TRP 440 ENGINEERED MUTATION
SEQADV 6EMI TYR B 417 UNP P06276 PHE 445 ENGINEERED MUTATION
SEQADV 6EMI LEU B 454 UNP P06276 ASP 482 ENGINEERED MUTATION
SEQADV 6EMI GLU B 459 UNP P06276 ALA 487 ENGINEERED MUTATION
SEQADV 6EMI GLU B 466 UNP P06276 SER 494 ENGINEERED MUTATION
SEQADV 6EMI MET B 468 UNP P06276 VAL 496 ENGINEERED MUTATION
SEQADV 6EMI ARG B 469 UNP P06276 LYS 497 ENGINEERED MUTATION
SEQADV 6EMI GLN B 489 UNP P06276 SER 517 ENGINEERED MUTATION
SEQADV 6EMI PRO B 495 UNP P06276 SER 523 ENGINEERED MUTATION
SEQADV 6EMI SER B 508 UNP P06276 THR 536 ENGINEERED MUTATION
SEQADV 6EMI HIS B 518 UNP P06276 GLN 546 ENGINEERED MUTATION
SEQADV 6EMI ASN B 523 UNP P06276 THR 551 ENGINEERED MUTATION
SEQRES 1 A 532 GLY ALA MET GLU ASP ASP ILE ILE ILE THR THR LYS ASN
SEQRES 2 A 532 GLY LYS VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY
SEQRES 3 A 532 THR VAL THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO
SEQRES 4 A 532 PRO LEU GLY ARG LEU ARG PHE LYS LYS PRO GLN PRO LEU
SEQRES 5 A 532 THR LYS TRP SER GLY ILE TRP ASN ALA THR LYS TYR ALA
SEQRES 6 A 532 ASN SER CYS MET GLN ASN ILE ASP THR SER PHE PRO GLY
SEQRES 7 A 532 PHE HIS GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU
SEQRES 8 A 532 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA
SEQRES 9 A 532 PRO LYS PRO LYS ASN ALA THR VAL MET VAL TRP ILE TYR
SEQRES 10 A 532 GLY GLY GLY PHE GLN THR GLY THR SER SER LEU PRO VAL
SEQRES 11 A 532 TYR ASP GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE
SEQRES 12 A 532 VAL VAL SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE
SEQRES 13 A 532 LEU ALA LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET
SEQRES 14 A 532 GLY LEU PHE ASP GLN GLN LEU ALA LEU LYS TRP VAL GLN
SEQRES 15 A 532 ASP ASN ILE ALA ALA PHE GLY GLY ASP PRO ASN ARG VAL
SEQRES 16 A 532 THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER
SEQRES 17 A 532 LEU HIS LEU LEU SER PRO GLY SER HIS PRO LEU PHE THR
SEQRES 18 A 532 ARG ALA ILE LEU GLN SER GLY SER ALA ASN ALA PRO TRP
SEQRES 19 A 532 ALA VAL MET SER PRO GLU GLU ALA ARG ASN ARG THR LEU
SEQRES 20 A 532 ASN LEU ALA LYS LEU LEU GLY CYS SER ARG GLU ASN GLU
SEQRES 21 A 532 THR GLU ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN
SEQRES 22 A 532 GLU ILE LEU ASP ASN GLU ALA PHE VAL VAL PRO TYR SER
SEQRES 23 A 532 THR PRO LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY
SEQRES 24 A 532 ASP PHE LEU THR ASP MET PRO ASP THR LEU LEU GLU LEU
SEQRES 25 A 532 GLY GLN PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN
SEQRES 26 A 532 LYS ASP GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO
SEQRES 27 A 532 GLY PHE SER LYS ASP ASN ASP SER ILE ILE THR ARG LYS
SEQRES 28 A 532 GLU PHE GLN GLU GLY LEU LYS VAL PHE PHE PRO ASN VAL
SEQRES 29 A 532 SER GLU PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR
SEQRES 30 A 532 ASP TRP GLU ASP GLU ASP ARG PRO GLU ASN TYR ARG ASP
SEQRES 31 A 532 ALA LEU ALA GLU VAL VAL GLY ASP TYR PHE PHE ILE CYS
SEQRES 32 A 532 PRO ALA LEU GLU PHE ALA LYS LYS TYR ALA GLU HIS GLY
SEQRES 33 A 532 ASN ASN ALA TYR PHE TYR TYR PHE GLU HIS ARG SER SER
SEQRES 34 A 532 LYS LEU PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY
SEQRES 35 A 532 TYR GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG
SEQRES 36 A 532 ARG LEU ASN TYR THR LYS GLU GLU GLU ILE LEU SER ARG
SEQRES 37 A 532 GLU ILE MET ARG ARG TRP ALA ASN PHE ALA LYS TYR GLY
SEQRES 38 A 532 ASN PRO ASN GLU THR GLN ASN ASN SER THR GLN TRP PRO
SEQRES 39 A 532 VAL PHE LYS PRO THR GLU GLN LYS TYR LEU THR LEU ASN
SEQRES 40 A 532 THR GLU SER SER ARG ILE MET THR LYS LEU ARG ALA GLN
SEQRES 41 A 532 HIS CYS ARG PHE TRP ASN SER PHE PHE PRO LYS VAL
SEQRES 1 B 532 GLY ALA MET GLU ASP ASP ILE ILE ILE THR THR LYS ASN
SEQRES 2 B 532 GLY LYS VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY
SEQRES 3 B 532 THR VAL THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO
SEQRES 4 B 532 PRO LEU GLY ARG LEU ARG PHE LYS LYS PRO GLN PRO LEU
SEQRES 5 B 532 THR LYS TRP SER GLY ILE TRP ASN ALA THR LYS TYR ALA
SEQRES 6 B 532 ASN SER CYS MET GLN ASN ILE ASP THR SER PHE PRO GLY
SEQRES 7 B 532 PHE HIS GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU
SEQRES 8 B 532 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA
SEQRES 9 B 532 PRO LYS PRO LYS ASN ALA THR VAL MET VAL TRP ILE TYR
SEQRES 10 B 532 GLY GLY GLY PHE GLN THR GLY THR SER SER LEU PRO VAL
SEQRES 11 B 532 TYR ASP GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE
SEQRES 12 B 532 VAL VAL SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE
SEQRES 13 B 532 LEU ALA LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET
SEQRES 14 B 532 GLY LEU PHE ASP GLN GLN LEU ALA LEU LYS TRP VAL GLN
SEQRES 15 B 532 ASP ASN ILE ALA ALA PHE GLY GLY ASP PRO ASN ARG VAL
SEQRES 16 B 532 THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER
SEQRES 17 B 532 LEU HIS LEU LEU SER PRO GLY SER HIS PRO LEU PHE THR
SEQRES 18 B 532 ARG ALA ILE LEU GLN SER GLY SER ALA ASN ALA PRO TRP
SEQRES 19 B 532 ALA VAL MET SER PRO GLU GLU ALA ARG ASN ARG THR LEU
SEQRES 20 B 532 ASN LEU ALA LYS LEU LEU GLY CYS SER ARG GLU ASN GLU
SEQRES 21 B 532 THR GLU ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN
SEQRES 22 B 532 GLU ILE LEU ASP ASN GLU ALA PHE VAL VAL PRO TYR SER
SEQRES 23 B 532 THR PRO LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY
SEQRES 24 B 532 ASP PHE LEU THR ASP MET PRO ASP THR LEU LEU GLU LEU
SEQRES 25 B 532 GLY GLN PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN
SEQRES 26 B 532 LYS ASP GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO
SEQRES 27 B 532 GLY PHE SER LYS ASP ASN ASP SER ILE ILE THR ARG LYS
SEQRES 28 B 532 GLU PHE GLN GLU GLY LEU LYS VAL PHE PHE PRO ASN VAL
SEQRES 29 B 532 SER GLU PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR
SEQRES 30 B 532 ASP TRP GLU ASP GLU ASP ARG PRO GLU ASN TYR ARG ASP
SEQRES 31 B 532 ALA LEU ALA GLU VAL VAL GLY ASP TYR PHE PHE ILE CYS
SEQRES 32 B 532 PRO ALA LEU GLU PHE ALA LYS LYS TYR ALA GLU HIS GLY
SEQRES 33 B 532 ASN ASN ALA TYR PHE TYR TYR PHE GLU HIS ARG SER SER
SEQRES 34 B 532 LYS LEU PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY
SEQRES 35 B 532 TYR GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG
SEQRES 36 B 532 ARG LEU ASN TYR THR LYS GLU GLU GLU ILE LEU SER ARG
SEQRES 37 B 532 GLU ILE MET ARG ARG TRP ALA ASN PHE ALA LYS TYR GLY
SEQRES 38 B 532 ASN PRO ASN GLU THR GLN ASN ASN SER THR GLN TRP PRO
SEQRES 39 B 532 VAL PHE LYS PRO THR GLU GLN LYS TYR LEU THR LEU ASN
SEQRES 40 B 532 THR GLU SER SER ARG ILE MET THR LYS LEU ARG ALA GLN
SEQRES 41 B 532 HIS CYS ARG PHE TRP ASN SER PHE PHE PRO LYS VAL
HET EDO A 601 4
HET EDO A 602 4
HET EDO A 603 4
HET PEG A 604 7
HET CL A 605 1
HET CL A 606 1
HET CL A 607 1
HET CL A 608 1
HET CL A 609 1
HET PGE A 610 10
HET PGE A 611 10
HET PGE A 612 10
HET PGE A 613 10
HET PGE A 614 10
HET PGE A 615 10
HET EDO B 601 4
HET EDO B 602 4
HET EDO B 603 4
HET EDO B 604 4
HET EDO B 605 4
HET EDO B 606 4
HET EDO B 607 4
HET EDO B 608 4
HET EDO B 609 4
HET EDO B 610 4
HET EDO B 611 4
HET EDO B 612 4
HET EDO B 613 4
HET EDO B 614 4
HET PEG B 615 7
HET PEG B 616 7
HET PEG B 617 7
HET CL B 618 1
HET CL B 619 1
HET PGE B 620 10
HET PGE B 621 10
HET PGE B 622 10
HET PG4 B 623 13
HET PG4 B 624 13
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM CL CHLORIDE ION
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 17(C2 H6 O2)
FORMUL 6 PEG 4(C4 H10 O3)
FORMUL 7 CL 7(CL 1-)
FORMUL 12 PGE 9(C6 H14 O4)
FORMUL 40 PG4 2(C8 H18 O5)
FORMUL 42 HOH *376(H2 O)
HELIX 1 AA1 LEU A 38 ARG A 42 5 5
HELIX 2 AA2 PHE A 76 MET A 81 1 6
HELIX 3 AA3 LEU A 125 ASP A 129 5 5
HELIX 4 AA4 GLY A 130 ARG A 138 1 9
HELIX 5 AA5 GLY A 149 LEU A 154 1 6
HELIX 6 AA6 ASN A 165 ILE A 182 1 18
HELIX 7 AA7 ALA A 183 PHE A 185 5 3
HELIX 8 AA8 SER A 198 LEU A 209 1 12
HELIX 9 AA9 SER A 210 PHE A 217 5 8
HELIX 10 AB1 SER A 235 LEU A 250 1 16
HELIX 11 AB2 ASN A 256 LYS A 267 1 12
HELIX 12 AB3 ASP A 268 ASP A 274 1 7
HELIX 13 AB4 ASN A 275 VAL A 279 5 5
HELIX 14 AB5 MET A 302 LEU A 309 1 8
HELIX 15 AB6 GLY A 326 TYR A 332 1 7
HELIX 16 AB7 THR A 346 PHE A 358 1 13
HELIX 17 AB8 SER A 362 TYR A 373 1 12
HELIX 18 AB9 GLU A 383 PHE A 398 1 16
HELIX 19 AC1 PHE A 398 HIS A 412 1 15
HELIX 20 AC2 PRO A 431 GLY A 435 5 5
HELIX 21 AC3 GLU A 441 PHE A 446 1 6
HELIX 22 AC4 GLY A 447 ASN A 455 5 9
HELIX 23 AC5 THR A 457 GLY A 478 1 22
HELIX 24 AC6 ARG A 515 PHE A 525 1 11
HELIX 25 AC7 PHE A 526 VAL A 529 5 4
HELIX 26 AC8 LEU B 38 ARG B 42 5 5
HELIX 27 AC9 PHE B 76 MET B 81 1 6
HELIX 28 AD1 LEU B 125 ASP B 129 5 5
HELIX 29 AD2 GLY B 130 ARG B 138 1 9
HELIX 30 AD3 GLY B 149 LEU B 154 1 6
HELIX 31 AD4 ASN B 165 ILE B 182 1 18
HELIX 32 AD5 ALA B 183 PHE B 185 5 3
HELIX 33 AD6 SER B 198 LEU B 209 1 12
HELIX 34 AD7 SER B 210 PHE B 217 5 8
HELIX 35 AD8 SER B 235 LEU B 250 1 16
HELIX 36 AD9 ASN B 256 LYS B 267 1 12
HELIX 37 AE1 ASP B 268 GLU B 276 1 9
HELIX 38 AE2 ALA B 277 VAL B 279 5 3
HELIX 39 AE3 MET B 302 LEU B 309 1 8
HELIX 40 AE4 GLY B 326 VAL B 331 1 6
HELIX 41 AE5 THR B 346 PHE B 358 1 13
HELIX 42 AE6 SER B 362 TYR B 373 1 12
HELIX 43 AE7 GLU B 383 PHE B 398 1 16
HELIX 44 AE8 PHE B 398 HIS B 412 1 15
HELIX 45 AE9 PRO B 431 GLY B 435 5 5
HELIX 46 AF1 GLU B 441 PHE B 446 1 6
HELIX 47 AF2 GLY B 447 ASN B 455 5 9
HELIX 48 AF3 THR B 457 GLY B 478 1 22
HELIX 49 AF4 ARG B 515 PHE B 525 1 11
HELIX 50 AF5 PHE B 526 VAL B 529 5 4
SHEET 1 AA1 3 ILE A 5 THR A 7 0
SHEET 2 AA1 3 LYS A 12 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 AA1 3 ILE A 55 ASN A 57 1 O TRP A 56 N LYS A 12
SHEET 1 AA211 MET A 16 VAL A 20 0
SHEET 2 AA211 GLY A 23 PRO A 32 -1 O GLY A 23 N VAL A 20
SHEET 3 AA211 TYR A 94 PRO A 100 -1 O ILE A 99 N THR A 26
SHEET 4 AA211 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 AA211 ALA A 107 ILE A 113 1 N MET A 110 O ILE A 140
SHEET 6 AA211 GLY A 187 GLU A 197 1 O THR A 193 N VAL A 111
SHEET 7 AA211 ARG A 219 GLN A 223 1 O ILE A 221 N LEU A 194
SHEET 8 AA211 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AA211 ALA A 416 PHE A 421 1 O PHE A 421 N VAL A 321
SHEET 10 AA211 LYS A 499 LEU A 503 1 O LEU A 501 N PHE A 418
SHEET 11 AA211 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 AA3 3 ILE B 5 THR B 7 0
SHEET 2 AA3 3 LYS B 12 ARG B 14 -1 O VAL B 13 N ILE B 6
SHEET 3 AA3 3 ILE B 55 ASN B 57 1 O TRP B 56 N LYS B 12
SHEET 1 AA411 MET B 16 THR B 19 0
SHEET 2 AA411 THR B 24 PRO B 32 -1 O ALA B 27 N MET B 16
SHEET 3 AA411 TYR B 94 PRO B 100 -1 O LEU B 95 N ILE B 31
SHEET 4 AA411 ILE B 140 MET B 144 -1 O SER B 143 N ASN B 96
SHEET 5 AA411 ALA B 107 ILE B 113 1 N TRP B 112 O VAL B 142
SHEET 6 AA411 GLY B 187 GLU B 197 1 O ASP B 188 N ALA B 107
SHEET 7 AA411 ARG B 219 GLN B 223 1 O ILE B 221 N LEU B 194
SHEET 8 AA411 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 9 AA411 ALA B 416 PHE B 421 1 O PHE B 421 N VAL B 321
SHEET 10 AA411 LYS B 499 LEU B 503 1 O LEU B 503 N TYR B 420
SHEET 11 AA411 ILE B 510 THR B 512 -1 O MET B 511 N TYR B 500
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.04
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.04
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.03
SSBOND 4 CYS B 252 CYS B 263 1555 1555 2.03
SSBOND 5 CYS B 400 CYS B 519 1555 1555 2.03
CISPEP 1 ALA A 101 PRO A 102 0 2.60
CISPEP 2 ALA B 101 PRO B 102 0 -0.44
SITE 1 AC1 5 ALA A 227 ALA A 229 VAL A 233 MET A 302
SITE 2 AC1 5 ASP A 304
SITE 1 AC2 4 LEU A 18 TRP A 98 ASP A 129 LYS A 131
SITE 1 AC3 1 THR A 512
SITE 1 AC4 7 ASN A 10 TYR A 33 PRO A 48 LEU A 49
SITE 2 AC4 7 TRP A 177 ASP A 180 ASN A 181
SITE 1 AC5 1 HOH A 740
SITE 1 AC6 1 ARG A 138
SITE 1 AC7 2 GLY A 30 LYS A 60
SITE 1 AC8 1 ARG A 254
SITE 1 AC9 10 ASN A 159 GLU A 161 THR A 258 LYS A 314
SITE 2 AC9 10 THR A 315 GLN A 316 GLY A 413 ASN A 414
SITE 3 AC9 10 ASN A 415 HOH A 726
SITE 1 AD1 6 GLY A 116 GLY A 117 SER A 198 TRP A 231
SITE 2 AD1 6 SER A 287 PHE A 329
SITE 1 AD2 5 TRP A 82 GLY A 116 SER A 198 HIS A 438
SITE 2 AD2 5 HOH A 734
SITE 1 AD3 2 SER A 53 ILE A 55
SITE 1 AD4 7 TRP A 56 LYS A 60 TYR A 61 ALA A 62
SITE 2 AD4 7 ASN A 63 ASP A 87 TYR A 94
SITE 1 AD5 3 GLU A 352 LYS A 355 GLU A 363
SITE 1 AD6 5 LEU B 18 TYR B 61 TRP B 98 ASP B 129
SITE 2 AD6 5 LYS B 131
SITE 1 AD7 5 TYR B 33 PRO B 48 LEU B 49 TRP B 177
SITE 2 AD7 5 ASP B 180
SITE 1 AD8 3 LYS B 60 ASN B 63 ASP B 87
SITE 1 AD9 4 HIS B 77 MET B 81 VAL B 127 EDO B 612
SITE 1 AE1 4 LYS B 323 ASP B 324 GLU B 391 HOH B 830
SITE 1 AE2 4 GLY B 115 GLY B 116 GLU B 197 EDO B 613
SITE 1 AE3 2 TYR B 417 VAL B 492
SITE 1 AE4 2 TRP B 56 HOH B 738
SITE 1 AE5 3 ALA B 410 GLY B 413 ASN B 414
SITE 1 AE6 2 ARG B 135 ARG B 465
SITE 1 AE7 5 GLN B 172 GLY B 212 GLN B 484 PEG B 616
SITE 2 AE7 5 HOH B 705
SITE 1 AE8 3 MET B 81 PRO B 126 EDO B 604
SITE 1 AE9 6 GLY B 116 GLY B 117 SER B 198 PHE B 329
SITE 2 AE9 6 EDO B 606 PGE B 622
SITE 1 AF1 3 HIS B 77 LYS B 427 PRO B 429
SITE 1 AF2 10 GLY B 158 ASN B 159 THR B 218 ARG B 219
SITE 2 AF2 10 ASN B 256 GLU B 257 THR B 258 THR B 315
SITE 3 AF2 10 GLN B 316 HOH B 739
SITE 1 AF3 9 LEU B 209 SER B 210 PRO B 211 GLY B 212
SITE 2 AF3 9 ASP B 297 PHE B 298 THR B 300 EDO B 611
SITE 3 AF3 9 HOH B 705
SITE 1 AF4 3 ARG B 265 ASN B 266 LYS B 267
SITE 1 AF5 1 ASP B 387
SITE 1 AF6 2 ASN B 106 HOH B 874
SITE 1 AF7 5 SER B 53 ILE B 55 TRP B 56 ASN B 57
SITE 2 AF7 5 PG4 B 623
SITE 1 AF8 7 HIS B 372 TYR B 373 THR B 374 ASP B 375
SITE 2 AF8 7 GLU B 391 ARG B 515 HIS B 518
SITE 1 AF9 7 GLY B 116 GLY B 117 SER B 198 TRP B 231
SITE 2 AF9 7 LEU B 286 SER B 287 EDO B 613
SITE 1 AG1 13 LEU B 29 GLY B 30 TRP B 56 ASN B 57
SITE 2 AG1 13 ALA B 58 THR B 59 LYS B 60 ALA B 62
SITE 3 AG1 13 ASP B 91 TYR B 94 PGE B 620 HOH B 706
SITE 4 AG1 13 HOH B 738
SITE 1 AG2 4 ARG B 509 ILE B 510 MET B 511 THR B 512
CRYST1 159.840 75.170 122.070 90.00 93.37 90.00 C 1 2 1 8
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 0.006256 0.000000 0.000368 0.00000
SCALE2 0.000000 0.013303 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008206 0.00000
TER 4214 VAL A 529
TER 8425 VAL B 529
MASTER 451 0 39 50 28 0 59 6 9015 2 222 82
END |