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HEADER HYDROLASE 24-FEB-21 7NN3
TITLE A CARBOHYDRATE ESTERASE FAMILY 15 (CE15) GLUCURONOYL ESTERASE FROM
TITLE 2 CALDICELLULOSIRUPTOR KRISTJANSONII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-XYLANASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.2.1.8;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CALDICELLULOSIRUPTOR KRISTJANSSONII (STRAIN
SOURCE 3 ATCC 700853 / DSM 12137 / I77R1B);
SOURCE 4 ORGANISM_TAXID: 632335;
SOURCE 5 STRAIN: ATCC 700853 / DSM 12137 / I77R1B;
SOURCE 6 GENE: CALKR_2245;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KRSKA,S.MAZURKEWICH,J.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
REVDAT 1 07-JUL-21 7NN3 0
JRNL AUTH D.KRSKA,S.MAZURKEWICH,H.A.BROWN,Y.THEIBICH,J.N.POULSEN,
JRNL AUTH 2 A.L.MORRIS,N.M.KOROPATKIN,L.LO LEGGIO,J.LARSBRINK
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF A MULTIMODULAR
JRNL TITL 2 HYPERTHERMOSTABLE XYLANASE-GLUCURONOYL ESTERASE FROM
JRNL TITL 3 CALDICELLULOSIRUPTOR KRISTJANSONII .
JRNL REF BIOCHEMISTRY 2021
JRNL REFN ISSN 0006-2960
JRNL PMID 34180241
JRNL DOI 10.1021/ACS.BIOCHEM.1C00305
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.344
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 145194
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.377
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 48.6200 - 4.5528 0.94 10336 145 0.1271 0.1408
REMARK 3 2 4.5528 - 3.6140 0.97 10317 143 0.1220 0.1604
REMARK 3 3 3.6140 - 3.1573 0.96 10133 142 0.1582 0.2019
REMARK 3 4 3.1573 - 2.8687 0.98 10352 144 0.1739 0.2423
REMARK 3 5 2.8687 - 2.6631 0.98 10265 144 0.1822 0.2460
REMARK 3 6 2.6631 - 2.5061 0.99 10317 144 0.1731 0.1936
REMARK 3 7 2.5061 - 2.3806 0.99 10378 145 0.1776 0.2326
REMARK 3 8 2.3806 - 2.2769 0.99 10377 145 0.1793 0.2293
REMARK 3 9 2.2769 - 2.1893 0.98 10266 143 0.1980 0.2600
REMARK 3 10 2.1893 - 2.1137 0.99 10335 145 0.2108 0.2445
REMARK 3 11 2.1137 - 2.0476 0.99 10343 144 0.2229 0.2602
REMARK 3 12 2.0476 - 1.9891 0.99 10342 144 0.2363 0.2476
REMARK 3 13 1.9891 - 1.9367 0.98 10279 144 0.2622 0.3137
REMARK 3 14 1.9367 - 1.8895 0.88 9154 128 0.3136 0.3324
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) : 0.216
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.268
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.14
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 : 0.007 12521
REMARK 3 ANGLE : 0.796 17006
REMARK 3 CHIRALITY : 0.055 1758
REMARK 3 PLANARITY : 0.005 2224
REMARK 3 DIHEDRAL : 12.874 7160
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 7NN3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-FEB-21.
REMARK 100 THE DEPOSITION ID IS D_1292113766.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 145210
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.889
REMARK 200 RESOLUTION RANGE LOW (A) : 48.637
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.07681
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.0300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.82670
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: AUTO-RICKSHAW
REMARK 200 STARTING MODEL: 6EHN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M BIS
REMARK 280 -TRIS, AND 25% POLYETHYLENE GLYCOL 3350. PROTEIN AT 51.1 MG/ML.,
REMARK 280 PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 49.52900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.19700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.45050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.19700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.52900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.45050
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, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 SER A 11
REMARK 465 TYR A 395
REMARK 465 ARG A 396
REMARK 465 ASN A 397
REMARK 465 ALA A 398
REMARK 465 ASP A 399
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 SER B 11
REMARK 465 SER B 12
REMARK 465 GLU B 13
REMARK 465 ASN B 14
REMARK 465 LEU B 15
REMARK 465 TYR B 16
REMARK 465 PHE B 17
REMARK 465 GLN B 18
REMARK 465 GLY B 19
REMARK 465 HIS B 20
REMARK 465 ILE B 21
REMARK 465 THR B 393
REMARK 465 LEU B 394
REMARK 465 TYR B 395
REMARK 465 ARG B 396
REMARK 465 ASN B 397
REMARK 465 ALA B 398
REMARK 465 ASP B 399
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 SER C 3
REMARK 465 SER C 4
REMARK 465 HIS C 5
REMARK 465 HIS C 6
REMARK 465 HIS C 7
REMARK 465 HIS C 8
REMARK 465 HIS C 9
REMARK 465 HIS C 10
REMARK 465 SER C 11
REMARK 465 SER C 12
REMARK 465 GLU C 13
REMARK 465 ASN C 14
REMARK 465 LEU C 15
REMARK 465 TYR C 16
REMARK 465 PHE C 17
REMARK 465 GLN C 18
REMARK 465 GLY C 19
REMARK 465 HIS C 20
REMARK 465 ILE C 21
REMARK 465 LEU C 394
REMARK 465 TYR C 395
REMARK 465 ARG C 396
REMARK 465 ASN C 397
REMARK 465 ALA C 398
REMARK 465 ASP C 399
REMARK 465 MET D 1
REMARK 465 GLY D 2
REMARK 465 SER D 3
REMARK 465 SER D 4
REMARK 465 HIS D 5
REMARK 465 HIS D 6
REMARK 465 HIS D 7
REMARK 465 HIS D 8
REMARK 465 HIS D 9
REMARK 465 HIS D 10
REMARK 465 SER D 11
REMARK 465 THR D 393
REMARK 465 LEU D 394
REMARK 465 TYR D 395
REMARK 465 ARG D 396
REMARK 465 ASN D 397
REMARK 465 ALA D 398
REMARK 465 ASP D 399
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 MET A 57 -59.76 -142.56
REMARK 500 SER A 210 -121.45 63.01
REMARK 500 PHE A 274 -164.04 -119.46
REMARK 500 ASN A 315 70.62 64.95
REMARK 500 ALA A 342 81.18 -155.64
REMARK 500 SER A 347 -144.81 -120.92
REMARK 500 MET B 57 -64.28 -138.10
REMARK 500 LEU B 117 73.90 -108.39
REMARK 500 SER B 210 -122.12 66.23
REMARK 500 PHE B 274 -162.40 -119.85
REMARK 500 ASN B 315 71.22 66.61
REMARK 500 ALA B 342 84.73 -154.85
REMARK 500 ASP B 345 -111.47 -85.76
REMARK 500 MET C 57 -61.44 -142.98
REMARK 500 LEU C 117 72.59 -102.49
REMARK 500 SER C 210 -117.92 60.39
REMARK 500 PHE C 274 -164.34 -120.27
REMARK 500 ASN C 315 72.26 61.58
REMARK 500 ALA C 342 88.70 -151.54
REMARK 500 ASP C 345 -114.54 -86.87
REMARK 500 GLN D 37 -35.32 -130.45
REMARK 500 MET D 57 -63.69 -144.62
REMARK 500 SER D 210 -124.63 66.65
REMARK 500 PHE D 274 -168.80 -115.97
REMARK 500 ASN D 315 71.04 66.07
REMARK 500 ALA D 342 78.80 -153.15
REMARK 500 SER D 347 -149.14 -122.27
REMARK 500 SER D 347 -149.01 -125.31
REMARK 500 THR D 372 -39.28 60.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 752 DISTANCE = 6.59 ANGSTROMS
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 410
DBREF 7NN3 A 22 399 UNP E4S6E9 E4S6E9_CALKI 1340 1717
DBREF 7NN3 B 22 399 UNP E4S6E9 E4S6E9_CALKI 1340 1717
DBREF 7NN3 C 22 399 UNP E4S6E9 E4S6E9_CALKI 1340 1717
DBREF 7NN3 D 22 399 UNP E4S6E9 E4S6E9_CALKI 1340 1717
SEQADV 7NN3 MET A 1 UNP E4S6E9 INITIATING METHIONINE
SEQADV 7NN3 GLY A 2 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER A 3 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER A 4 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS A 5 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS A 6 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS A 7 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS A 8 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS A 9 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS A 10 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER A 11 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER A 12 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 GLU A 13 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 ASN A 14 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 LEU A 15 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 TYR A 16 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 PHE A 17 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 GLN A 18 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 GLY A 19 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS A 20 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 ILE A 21 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 MET B 1 UNP E4S6E9 INITIATING METHIONINE
SEQADV 7NN3 GLY B 2 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER B 3 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER B 4 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS B 5 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS B 6 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS B 7 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS B 8 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS B 9 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS B 10 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER B 11 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER B 12 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 GLU B 13 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 ASN B 14 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 LEU B 15 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 TYR B 16 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 PHE B 17 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 GLN B 18 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 GLY B 19 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS B 20 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 ILE B 21 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 MET C 1 UNP E4S6E9 INITIATING METHIONINE
SEQADV 7NN3 GLY C 2 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER C 3 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER C 4 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS C 5 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS C 6 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS C 7 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS C 8 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS C 9 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS C 10 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER C 11 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER C 12 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 GLU C 13 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 ASN C 14 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 LEU C 15 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 TYR C 16 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 PHE C 17 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 GLN C 18 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 GLY C 19 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS C 20 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 ILE C 21 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 MET D 1 UNP E4S6E9 INITIATING METHIONINE
SEQADV 7NN3 GLY D 2 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER D 3 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER D 4 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS D 5 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS D 6 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS D 7 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS D 8 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS D 9 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS D 10 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER D 11 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 SER D 12 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 GLU D 13 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 ASN D 14 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 LEU D 15 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 TYR D 16 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 PHE D 17 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 GLN D 18 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 GLY D 19 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 HIS D 20 UNP E4S6E9 EXPRESSION TAG
SEQADV 7NN3 ILE D 21 UNP E4S6E9 EXPRESSION TAG
SEQRES 1 A 399 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 A 399 ASN LEU TYR PHE GLN GLY HIS ILE GLU THR LEU PRO ASP
SEQRES 3 A 399 SER PHE THR PHE TYR ASP GLY THR LYS VAL GLN ARG LEU
SEQRES 4 A 399 SER ASP TRP PRO LYS ARG ALA GLN GLU LEU LYS ASP LEU
SEQRES 5 A 399 TYR GLN PHE TYR MET TYR GLY TYR LYS PRO ASP THR SER
SEQRES 6 A 399 VAL GLU ASP VAL THR TYR SER VAL ASN GLY ASN THR LEU
SEQRES 7 A 399 THR ILE THR VAL LYS VAL GLY ASP LYS GLN ALA SER PHE
SEQRES 8 A 399 ASN ALA THR VAL ARG LEU PRO GLN ALA ASN SER GLY TYR
SEQRES 9 A 399 GLN PRO PRO TYR PRO VAL ILE ILE SER LEU GLY TYR LEU
SEQRES 10 A 399 ALA GLY PHE ASN TRP GLN THR TRP GLN PHE ILE ASP TYR
SEQRES 11 A 399 SER THR ASN ALA VAL ASN ARG GLY TYR ALA VAL ILE SER
SEQRES 12 A 399 PHE MET PRO ASN ASP VAL ALA ARG ASP ASP SER SER TYR
SEQRES 13 A 399 THR GLY ALA PHE TYR THR LEU TYR PRO HIS SER ASN LYS
SEQRES 14 A 399 VAL GLU ASN ASP THR GLY VAL LEU MET ALA TRP ALA TRP
SEQRES 15 A 399 GLY ALA SER LYS ILE LEU ASP ALA LEU GLU LYS GLY ALA
SEQRES 16 A 399 ILE PRO GLU ILE ASP ALA LYS LYS ALA ILE VAL THR GLY
SEQRES 17 A 399 PHE SER ARG TYR GLY LYS ALA ALA LEU VAL ALA GLY ALA
SEQRES 18 A 399 PHE ASP GLU ARG PHE ALA VAL VAL ASN PRO HIS ALA SER
SEQRES 19 A 399 GLY GLN GLY GLY ALA ALA SER PHE ARG TYR SER PHE ALA
SEQRES 20 A 399 GLY LYS GLN TYR SER TRP GLY VAL ALA GLY ASN ALA GLU
SEQRES 21 A 399 ALA PHE SER ASN LEU GLN GLY ASN THR GLU GLY HIS TRP
SEQRES 22 A 399 PHE ASN ALA VAL PHE ARG GLU PHE LYS ASP PRO ARG GLN
SEQRES 23 A 399 LEU PRO PHE ASP GLN HIS GLU LEU ILE ALA LEU CYS ALA
SEQRES 24 A 399 PRO ARG THR VAL LEU ILE THR GLY GLY TYR SER ASP TRP
SEQRES 25 A 399 GLY THR ASN PRO GLU GLY THR TRP VAL SER PHE VAL GLY
SEQRES 26 A 399 ALA ARG LYS VAL TYR GLU PHE LEU GLY VAL ALA ASP ARG
SEQRES 27 A 399 ILE GLY PHE ALA LEU ARG ASP GLY SER HIS ALA ILE THR
SEQRES 28 A 399 GLU GLU ASP VAL ASN ASN LEU LEU ASP PHE CYS ASP TRP
SEQRES 29 A 399 GLN LEU ARG GLY ILE GLN PRO THR LYS ASP PHE SER THR
SEQRES 30 A 399 SER ARG PHE ALA ILE ASP PRO ALA TRP ASP THR ILE SER
SEQRES 31 A 399 VAL PRO THR LEU TYR ARG ASN ALA ASP
SEQRES 1 B 399 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 B 399 ASN LEU TYR PHE GLN GLY HIS ILE GLU THR LEU PRO ASP
SEQRES 3 B 399 SER PHE THR PHE TYR ASP GLY THR LYS VAL GLN ARG LEU
SEQRES 4 B 399 SER ASP TRP PRO LYS ARG ALA GLN GLU LEU LYS ASP LEU
SEQRES 5 B 399 TYR GLN PHE TYR MET TYR GLY TYR LYS PRO ASP THR SER
SEQRES 6 B 399 VAL GLU ASP VAL THR TYR SER VAL ASN GLY ASN THR LEU
SEQRES 7 B 399 THR ILE THR VAL LYS VAL GLY ASP LYS GLN ALA SER PHE
SEQRES 8 B 399 ASN ALA THR VAL ARG LEU PRO GLN ALA ASN SER GLY TYR
SEQRES 9 B 399 GLN PRO PRO TYR PRO VAL ILE ILE SER LEU GLY TYR LEU
SEQRES 10 B 399 ALA GLY PHE ASN TRP GLN THR TRP GLN PHE ILE ASP TYR
SEQRES 11 B 399 SER THR ASN ALA VAL ASN ARG GLY TYR ALA VAL ILE SER
SEQRES 12 B 399 PHE MET PRO ASN ASP VAL ALA ARG ASP ASP SER SER TYR
SEQRES 13 B 399 THR GLY ALA PHE TYR THR LEU TYR PRO HIS SER ASN LYS
SEQRES 14 B 399 VAL GLU ASN ASP THR GLY VAL LEU MET ALA TRP ALA TRP
SEQRES 15 B 399 GLY ALA SER LYS ILE LEU ASP ALA LEU GLU LYS GLY ALA
SEQRES 16 B 399 ILE PRO GLU ILE ASP ALA LYS LYS ALA ILE VAL THR GLY
SEQRES 17 B 399 PHE SER ARG TYR GLY LYS ALA ALA LEU VAL ALA GLY ALA
SEQRES 18 B 399 PHE ASP GLU ARG PHE ALA VAL VAL ASN PRO HIS ALA SER
SEQRES 19 B 399 GLY GLN GLY GLY ALA ALA SER PHE ARG TYR SER PHE ALA
SEQRES 20 B 399 GLY LYS GLN TYR SER TRP GLY VAL ALA GLY ASN ALA GLU
SEQRES 21 B 399 ALA PHE SER ASN LEU GLN GLY ASN THR GLU GLY HIS TRP
SEQRES 22 B 399 PHE ASN ALA VAL PHE ARG GLU PHE LYS ASP PRO ARG GLN
SEQRES 23 B 399 LEU PRO PHE ASP GLN HIS GLU LEU ILE ALA LEU CYS ALA
SEQRES 24 B 399 PRO ARG THR VAL LEU ILE THR GLY GLY TYR SER ASP TRP
SEQRES 25 B 399 GLY THR ASN PRO GLU GLY THR TRP VAL SER PHE VAL GLY
SEQRES 26 B 399 ALA ARG LYS VAL TYR GLU PHE LEU GLY VAL ALA ASP ARG
SEQRES 27 B 399 ILE GLY PHE ALA LEU ARG ASP GLY SER HIS ALA ILE THR
SEQRES 28 B 399 GLU GLU ASP VAL ASN ASN LEU LEU ASP PHE CYS ASP TRP
SEQRES 29 B 399 GLN LEU ARG GLY ILE GLN PRO THR LYS ASP PHE SER THR
SEQRES 30 B 399 SER ARG PHE ALA ILE ASP PRO ALA TRP ASP THR ILE SER
SEQRES 31 B 399 VAL PRO THR LEU TYR ARG ASN ALA ASP
SEQRES 1 C 399 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 C 399 ASN LEU TYR PHE GLN GLY HIS ILE GLU THR LEU PRO ASP
SEQRES 3 C 399 SER PHE THR PHE TYR ASP GLY THR LYS VAL GLN ARG LEU
SEQRES 4 C 399 SER ASP TRP PRO LYS ARG ALA GLN GLU LEU LYS ASP LEU
SEQRES 5 C 399 TYR GLN PHE TYR MET TYR GLY TYR LYS PRO ASP THR SER
SEQRES 6 C 399 VAL GLU ASP VAL THR TYR SER VAL ASN GLY ASN THR LEU
SEQRES 7 C 399 THR ILE THR VAL LYS VAL GLY ASP LYS GLN ALA SER PHE
SEQRES 8 C 399 ASN ALA THR VAL ARG LEU PRO GLN ALA ASN SER GLY TYR
SEQRES 9 C 399 GLN PRO PRO TYR PRO VAL ILE ILE SER LEU GLY TYR LEU
SEQRES 10 C 399 ALA GLY PHE ASN TRP GLN THR TRP GLN PHE ILE ASP TYR
SEQRES 11 C 399 SER THR ASN ALA VAL ASN ARG GLY TYR ALA VAL ILE SER
SEQRES 12 C 399 PHE MET PRO ASN ASP VAL ALA ARG ASP ASP SER SER TYR
SEQRES 13 C 399 THR GLY ALA PHE TYR THR LEU TYR PRO HIS SER ASN LYS
SEQRES 14 C 399 VAL GLU ASN ASP THR GLY VAL LEU MET ALA TRP ALA TRP
SEQRES 15 C 399 GLY ALA SER LYS ILE LEU ASP ALA LEU GLU LYS GLY ALA
SEQRES 16 C 399 ILE PRO GLU ILE ASP ALA LYS LYS ALA ILE VAL THR GLY
SEQRES 17 C 399 PHE SER ARG TYR GLY LYS ALA ALA LEU VAL ALA GLY ALA
SEQRES 18 C 399 PHE ASP GLU ARG PHE ALA VAL VAL ASN PRO HIS ALA SER
SEQRES 19 C 399 GLY GLN GLY GLY ALA ALA SER PHE ARG TYR SER PHE ALA
SEQRES 20 C 399 GLY LYS GLN TYR SER TRP GLY VAL ALA GLY ASN ALA GLU
SEQRES 21 C 399 ALA PHE SER ASN LEU GLN GLY ASN THR GLU GLY HIS TRP
SEQRES 22 C 399 PHE ASN ALA VAL PHE ARG GLU PHE LYS ASP PRO ARG GLN
SEQRES 23 C 399 LEU PRO PHE ASP GLN HIS GLU LEU ILE ALA LEU CYS ALA
SEQRES 24 C 399 PRO ARG THR VAL LEU ILE THR GLY GLY TYR SER ASP TRP
SEQRES 25 C 399 GLY THR ASN PRO GLU GLY THR TRP VAL SER PHE VAL GLY
SEQRES 26 C 399 ALA ARG LYS VAL TYR GLU PHE LEU GLY VAL ALA ASP ARG
SEQRES 27 C 399 ILE GLY PHE ALA LEU ARG ASP GLY SER HIS ALA ILE THR
SEQRES 28 C 399 GLU GLU ASP VAL ASN ASN LEU LEU ASP PHE CYS ASP TRP
SEQRES 29 C 399 GLN LEU ARG GLY ILE GLN PRO THR LYS ASP PHE SER THR
SEQRES 30 C 399 SER ARG PHE ALA ILE ASP PRO ALA TRP ASP THR ILE SER
SEQRES 31 C 399 VAL PRO THR LEU TYR ARG ASN ALA ASP
SEQRES 1 D 399 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 D 399 ASN LEU TYR PHE GLN GLY HIS ILE GLU THR LEU PRO ASP
SEQRES 3 D 399 SER PHE THR PHE TYR ASP GLY THR LYS VAL GLN ARG LEU
SEQRES 4 D 399 SER ASP TRP PRO LYS ARG ALA GLN GLU LEU LYS ASP LEU
SEQRES 5 D 399 TYR GLN PHE TYR MET TYR GLY TYR LYS PRO ASP THR SER
SEQRES 6 D 399 VAL GLU ASP VAL THR TYR SER VAL ASN GLY ASN THR LEU
SEQRES 7 D 399 THR ILE THR VAL LYS VAL GLY ASP LYS GLN ALA SER PHE
SEQRES 8 D 399 ASN ALA THR VAL ARG LEU PRO GLN ALA ASN SER GLY TYR
SEQRES 9 D 399 GLN PRO PRO TYR PRO VAL ILE ILE SER LEU GLY TYR LEU
SEQRES 10 D 399 ALA GLY PHE ASN TRP GLN THR TRP GLN PHE ILE ASP TYR
SEQRES 11 D 399 SER THR ASN ALA VAL ASN ARG GLY TYR ALA VAL ILE SER
SEQRES 12 D 399 PHE MET PRO ASN ASP VAL ALA ARG ASP ASP SER SER TYR
SEQRES 13 D 399 THR GLY ALA PHE TYR THR LEU TYR PRO HIS SER ASN LYS
SEQRES 14 D 399 VAL GLU ASN ASP THR GLY VAL LEU MET ALA TRP ALA TRP
SEQRES 15 D 399 GLY ALA SER LYS ILE LEU ASP ALA LEU GLU LYS GLY ALA
SEQRES 16 D 399 ILE PRO GLU ILE ASP ALA LYS LYS ALA ILE VAL THR GLY
SEQRES 17 D 399 PHE SER ARG TYR GLY LYS ALA ALA LEU VAL ALA GLY ALA
SEQRES 18 D 399 PHE ASP GLU ARG PHE ALA VAL VAL ASN PRO HIS ALA SER
SEQRES 19 D 399 GLY GLN GLY GLY ALA ALA SER PHE ARG TYR SER PHE ALA
SEQRES 20 D 399 GLY LYS GLN TYR SER TRP GLY VAL ALA GLY ASN ALA GLU
SEQRES 21 D 399 ALA PHE SER ASN LEU GLN GLY ASN THR GLU GLY HIS TRP
SEQRES 22 D 399 PHE ASN ALA VAL PHE ARG GLU PHE LYS ASP PRO ARG GLN
SEQRES 23 D 399 LEU PRO PHE ASP GLN HIS GLU LEU ILE ALA LEU CYS ALA
SEQRES 24 D 399 PRO ARG THR VAL LEU ILE THR GLY GLY TYR SER ASP TRP
SEQRES 25 D 399 GLY THR ASN PRO GLU GLY THR TRP VAL SER PHE VAL GLY
SEQRES 26 D 399 ALA ARG LYS VAL TYR GLU PHE LEU GLY VAL ALA ASP ARG
SEQRES 27 D 399 ILE GLY PHE ALA LEU ARG ASP GLY SER HIS ALA ILE THR
SEQRES 28 D 399 GLU GLU ASP VAL ASN ASN LEU LEU ASP PHE CYS ASP TRP
SEQRES 29 D 399 GLN LEU ARG GLY ILE GLN PRO THR LYS ASP PHE SER THR
SEQRES 30 D 399 SER ARG PHE ALA ILE ASP PRO ALA TRP ASP THR ILE SER
SEQRES 31 D 399 VAL PRO THR LEU TYR ARG ASN ALA ASP
HET PGE A 401 24
HET EDO A 402 10
HET EDO A 403 10
HET PEG A 404 17
HET EDO A 405 10
HET EDO A 406 10
HET EDO A 407 10
HET EDO A 408 10
HET EDO B 401 10
HET PEG B 402 17
HET PEG B 403 17
HET EDO B 404 10
HET EDO B 405 10
HET PEG B 406 17
HET ACT B 407 7
HET EDO C 401 10
HET EDO C 402 10
HET EDO C 403 10
HET EDO C 404 10
HET PGE C 405 24
HET EDO C 406 10
HET EDO C 407 10
HET EDO C 408 10
HET EDO C 409 10
HET EDO D 401 10
HET EDO D 402 10
HET EDO D 403 10
HET EDO D 404 10
HET PEG D 405 17
HET PEG D 406 17
HET EDO D 407 10
HET EDO D 408 10
HET PEG D 409 17
HET EDO D 410 10
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM ACT ACETATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 PGE 2(C6 H14 O4)
FORMUL 6 EDO 24(C2 H6 O2)
FORMUL 8 PEG 7(C4 H10 O3)
FORMUL 19 ACT C2 H3 O2 1-
FORMUL 39 HOH *1138(H2 O)
HELIX 1 AA1 ASN A 14 GLN A 18 5 5
HELIX 2 AA2 ARG A 38 SER A 40 5 3
HELIX 3 AA3 ASP A 41 MET A 57 1 17
HELIX 4 AA4 ASP A 63 GLU A 67 5 5
HELIX 5 AA5 GLN A 99 GLY A 103 5 5
HELIX 6 AA6 TYR A 130 ARG A 137 1 8
HELIX 7 AA7 MET A 145 ALA A 150 1 6
HELIX 8 AA8 GLY A 158 TYR A 164 1 7
HELIX 9 AA9 GLY A 175 LYS A 193 1 19
HELIX 10 AB1 SER A 210 ASP A 223 1 14
HELIX 11 AB2 ALA A 261 GLY A 267 1 7
HELIX 12 AB3 GLU A 270 PHE A 274 5 5
HELIX 13 AB4 VAL A 277 PHE A 281 5 5
HELIX 14 AB5 ASP A 283 LEU A 287 5 5
HELIX 15 AB6 ASP A 290 LEU A 297 1 8
HELIX 16 AB7 ASP A 311 THR A 314 5 4
HELIX 17 AB8 ASN A 315 LEU A 333 1 19
HELIX 18 AB9 VAL A 335 ASP A 337 5 3
HELIX 19 AC1 THR A 351 GLY A 368 1 18
HELIX 20 AC2 SER B 40 MET B 57 1 18
HELIX 21 AC3 GLN B 99 GLY B 103 5 5
HELIX 22 AC4 TYR B 130 ARG B 137 1 8
HELIX 23 AC5 MET B 145 ALA B 150 1 6
HELIX 24 AC6 GLY B 158 TYR B 164 1 7
HELIX 25 AC7 LYS B 169 ASP B 173 5 5
HELIX 26 AC8 GLY B 175 LYS B 193 1 19
HELIX 27 AC9 SER B 210 ASP B 223 1 14
HELIX 28 AD1 ALA B 261 GLY B 267 1 7
HELIX 29 AD2 GLU B 270 PHE B 274 5 5
HELIX 30 AD3 VAL B 277 PHE B 281 5 5
HELIX 31 AD4 ASP B 283 LEU B 287 5 5
HELIX 32 AD5 ASP B 290 LEU B 297 1 8
HELIX 33 AD6 ASP B 311 THR B 314 5 4
HELIX 34 AD7 ASN B 315 LEU B 333 1 19
HELIX 35 AD8 VAL B 335 ASP B 337 5 3
HELIX 36 AD9 THR B 351 GLY B 368 1 18
HELIX 37 AE1 ARG C 38 SER C 40 5 3
HELIX 38 AE2 ASP C 41 MET C 57 1 17
HELIX 39 AE3 ASP C 63 SER C 65 5 3
HELIX 40 AE4 GLN C 99 GLY C 103 5 5
HELIX 41 AE5 TYR C 130 ARG C 137 1 8
HELIX 42 AE6 MET C 145 ALA C 150 1 6
HELIX 43 AE7 GLY C 158 TYR C 164 1 7
HELIX 44 AE8 LYS C 169 ASP C 173 5 5
HELIX 45 AE9 GLY C 175 LYS C 193 1 19
HELIX 46 AF1 SER C 210 ASP C 223 1 14
HELIX 47 AF2 ALA C 261 GLY C 267 1 7
HELIX 48 AF3 GLU C 270 PHE C 274 5 5
HELIX 49 AF4 VAL C 277 PHE C 281 5 5
HELIX 50 AF5 ASP C 283 LEU C 287 5 5
HELIX 51 AF6 ASP C 290 LEU C 297 1 8
HELIX 52 AF7 ASP C 311 THR C 314 5 4
HELIX 53 AF8 ASN C 315 LEU C 333 1 19
HELIX 54 AF9 VAL C 335 ASP C 337 5 3
HELIX 55 AG1 THR C 351 GLY C 368 1 18
HELIX 56 AG2 ASN D 14 GLN D 18 5 5
HELIX 57 AG3 SER D 40 MET D 57 1 18
HELIX 58 AG4 ASP D 63 GLU D 67 5 5
HELIX 59 AG5 GLN D 99 GLY D 103 5 5
HELIX 60 AG6 TYR D 130 ARG D 137 1 8
HELIX 61 AG7 MET D 145 ALA D 150 1 6
HELIX 62 AG8 GLY D 158 TYR D 164 1 7
HELIX 63 AG9 GLY D 175 LYS D 193 1 19
HELIX 64 AH1 SER D 210 ASP D 223 1 14
HELIX 65 AH2 ALA D 261 GLY D 267 1 7
HELIX 66 AH3 GLU D 270 PHE D 274 5 5
HELIX 67 AH4 VAL D 277 PHE D 281 5 5
HELIX 68 AH5 ASP D 283 LEU D 287 5 5
HELIX 69 AH6 ASP D 290 LEU D 297 1 8
HELIX 70 AH7 ASP D 311 THR D 314 5 4
HELIX 71 AH8 ASN D 315 LEU D 333 1 19
HELIX 72 AH9 VAL D 335 ASP D 337 5 3
HELIX 73 AI1 THR D 351 GLY D 368 1 18
SHEET 1 AA1 9 ASP A 68 ASN A 74 0
SHEET 2 AA1 9 THR A 77 VAL A 84 -1 O THR A 79 N SER A 72
SHEET 3 AA1 9 LYS A 87 ARG A 96 -1 O ALA A 93 N LEU A 78
SHEET 4 AA1 9 ALA A 140 PHE A 144 -1 O SER A 143 N THR A 94
SHEET 5 AA1 9 TYR A 108 LEU A 114 1 N ILE A 111 O ALA A 140
SHEET 6 AA1 9 ILE A 199 PHE A 209 1 O ILE A 205 N ILE A 112
SHEET 7 AA1 9 VAL A 228 HIS A 232 1 O ASN A 230 N VAL A 206
SHEET 8 AA1 9 THR A 302 GLY A 308 1 O LEU A 304 N VAL A 229
SHEET 9 AA1 9 ILE A 339 ARG A 344 1 O ALA A 342 N ILE A 305
SHEET 1 AA2 2 ALA A 118 PHE A 120 0
SHEET 2 AA2 2 PHE A 127 ASP A 129 -1 O ILE A 128 N GLY A 119
SHEET 1 AA3 2 GLN A 250 TYR A 251 0
SHEET 2 AA3 2 GLY A 254 VAL A 255 -1 O GLY A 254 N TYR A 251
SHEET 1 AA4 9 ASP B 68 ASN B 74 0
SHEET 2 AA4 9 THR B 77 VAL B 84 -1 O THR B 79 N SER B 72
SHEET 3 AA4 9 LYS B 87 ARG B 96 -1 O ALA B 93 N LEU B 78
SHEET 4 AA4 9 ALA B 140 PHE B 144 -1 O SER B 143 N THR B 94
SHEET 5 AA4 9 TYR B 108 LEU B 114 1 N ILE B 111 O ALA B 140
SHEET 6 AA4 9 ILE B 199 PHE B 209 1 O ILE B 205 N ILE B 112
SHEET 7 AA4 9 VAL B 228 HIS B 232 1 O ASN B 230 N VAL B 206
SHEET 8 AA4 9 THR B 302 GLY B 308 1 O LEU B 304 N VAL B 229
SHEET 9 AA4 9 ILE B 339 ARG B 344 1 O GLY B 340 N VAL B 303
SHEET 1 AA5 2 ALA B 118 ASN B 121 0
SHEET 2 AA5 2 GLN B 126 ASP B 129 -1 O ILE B 128 N GLY B 119
SHEET 1 AA6 2 GLN B 250 TYR B 251 0
SHEET 2 AA6 2 GLY B 254 VAL B 255 -1 O GLY B 254 N TYR B 251
SHEET 1 AA7 9 GLU C 67 ASN C 74 0
SHEET 2 AA7 9 THR C 77 VAL C 84 -1 O THR C 81 N THR C 70
SHEET 3 AA7 9 LYS C 87 ARG C 96 -1 O ALA C 93 N LEU C 78
SHEET 4 AA7 9 ALA C 140 PHE C 144 -1 O SER C 143 N THR C 94
SHEET 5 AA7 9 TYR C 108 LEU C 114 1 N PRO C 109 O ALA C 140
SHEET 6 AA7 9 ILE C 199 PHE C 209 1 O ILE C 205 N ILE C 112
SHEET 7 AA7 9 VAL C 228 HIS C 232 1 O ASN C 230 N VAL C 206
SHEET 8 AA7 9 THR C 302 GLY C 308 1 O LEU C 304 N VAL C 229
SHEET 9 AA7 9 ILE C 339 ARG C 344 1 O ALA C 342 N ILE C 305
SHEET 1 AA8 2 ALA C 118 ASN C 121 0
SHEET 2 AA8 2 GLN C 126 ASP C 129 -1 O GLN C 126 N ASN C 121
SHEET 1 AA9 2 GLN C 250 TYR C 251 0
SHEET 2 AA9 2 GLY C 254 VAL C 255 -1 O GLY C 254 N TYR C 251
SHEET 1 AB1 9 ASP D 68 ASN D 74 0
SHEET 2 AB1 9 THR D 77 VAL D 84 -1 O THR D 77 N ASN D 74
SHEET 3 AB1 9 LYS D 87 ARG D 96 -1 O PHE D 91 N ILE D 80
SHEET 4 AB1 9 ALA D 140 PHE D 144 -1 O SER D 143 N THR D 94
SHEET 5 AB1 9 TYR D 108 LEU D 114 1 N PRO D 109 O ALA D 140
SHEET 6 AB1 9 ILE D 199 PHE D 209 1 O ILE D 205 N ILE D 112
SHEET 7 AB1 9 VAL D 228 HIS D 232 1 O ASN D 230 N VAL D 206
SHEET 8 AB1 9 THR D 302 GLY D 308 1 O LEU D 304 N VAL D 229
SHEET 9 AB1 9 ILE D 339 ARG D 344 1 O GLY D 340 N VAL D 303
SHEET 1 AB2 2 ALA D 118 PHE D 120 0
SHEET 2 AB2 2 PHE D 127 ASP D 129 -1 O ILE D 128 N GLY D 119
SHEET 1 AB3 2 GLN D 250 TYR D 251 0
SHEET 2 AB3 2 GLY D 254 VAL D 255 -1 O GLY D 254 N TYR D 251
CISPEP 1 PRO A 106 PRO A 107 0 -1.20
CISPEP 2 ALA A 299 PRO A 300 0 4.52
CISPEP 3 PRO B 106 PRO B 107 0 -2.81
CISPEP 4 ALA B 299 PRO B 300 0 3.95
CISPEP 5 PRO C 106 PRO C 107 0 -1.82
CISPEP 6 ALA C 299 PRO C 300 0 2.79
CISPEP 7 PRO D 106 PRO D 107 0 0.57
CISPEP 8 ALA D 299 PRO D 300 0 5.90
SITE 1 AC1 4 GLU A 13 SER A 252 EDO A 402 TRP B 125
SITE 1 AC2 6 TYR A 251 SER A 252 TRP A 253 ARG A 379
SITE 2 AC2 6 PGE A 401 HOH A 715
SITE 1 AC3 3 PHE A 127 ASP A 129 HOH A 743
SITE 1 AC4 1 HOH A 766
SITE 1 AC5 6 TRP A 253 SER A 310 ASP A 345 GLY A 346
SITE 2 AC5 6 ARG A 379 TRP C 253
SITE 1 AC6 2 GLN A 370 HOH A 531
SITE 1 AC7 5 GLN A 266 ARG A 279 GLU A 280 PHE A 281
SITE 2 AC7 5 LYS A 282
SITE 1 AC8 1 HOH A 694
SITE 1 AC9 5 ASN B 121 TRP B 122 GLN B 123 HOH B 516
SITE 2 AC9 5 HIS D 348
SITE 1 AD1 5 ARG B 327 LYS B 328 GLU B 331 ALA B 336
SITE 2 AD1 5 HOH B 657
SITE 1 AD2 2 PHE B 55 TYR B 56
SITE 1 AD3 2 GLN B 370 HOH B 523
SITE 1 AD4 3 SER B 72 ASN B 74 HOH B 534
SITE 1 AD5 2 ARG B 285 GLN B 286
SITE 1 AD6 2 LYS B 193 HOH B 519
SITE 1 AD7 5 GLY C 248 HOH C 700 ASN D 74 THR D 79
SITE 2 AD7 5 EDO D 402
SITE 1 AD8 4 HIS A 348 ASN C 121 TRP C 122 HOH C 562
SITE 1 AD9 4 ALA C 227 THR C 302 ARG C 338 HOH C 528
SITE 1 AE1 1 SER C 102
SITE 1 AE2 2 ASP C 51 LEU C 52
SITE 1 AE3 5 VAL A 255 ARG C 379 HOH C 501 HOH C 519
SITE 2 AE3 5 HOH C 522
SITE 1 AE4 6 TRP A 312 ARG C 344 ASP C 345 GLU C 353
SITE 2 AE4 6 ARG C 379 HOH C 522
SITE 1 AE5 5 GLN C 47 ASP C 51 GLN C 54 LYS C 61
SITE 2 AE5 5 HOH C 619
SITE 1 AE6 2 LEU C 366 ARG C 367
SITE 1 AE7 6 ASP A 374 THR A 377 ARG D 151 ASP D 153
SITE 2 AE7 6 HOH D 574 HOH D 577
SITE 1 AE8 4 EDO C 401 SER D 72 THR D 79 HOH D 558
SITE 1 AE9 2 ARG D 379 HOH D 747
SITE 1 AF1 2 PHE D 127 HOH D 529
SITE 1 AF2 1 LEU D 52
SITE 1 AF3 4 SER D 263 GLN D 266 GLY D 267 ARG D 279
SITE 1 AF4 4 PRO D 165 HIS D 166 SER D 167 ASN D 172
SITE 1 AF5 3 LEU D 191 GLU D 192 ALA D 201
SITE 1 AF6 12 LYS D 61 THR D 64 ALA D 181 TRP D 182
SITE 2 AF6 12 SER D 185 LYS D 186 VAL D 218 ALA D 219
SITE 3 AF6 12 PHE D 222 ASP D 223 HOH D 548 HOH D 589
SITE 1 AF7 1 HOH D 552
CRYST1 99.058 116.901 160.394 90.00 90.00 90.00 P 21 21 21 16
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 0.010095 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008554 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006235 0.00000
TER 3059 LEU A 394
TER 6005 PRO B 392
TER 8959 THR C 393
TER 12019 PRO D 392
MASTER 514 0 34 73 52 0 46 613199 4 414 124
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