HEADER TRANSFERASE/ISOMERASE 27-JAN-16 5HUD
TITLE NON-COVALENT COMPLEX OF AND DAHP SYNTHASE AND CHORISMATE MUTASE FROM
TITLE 2 CORYNEBACTERIUM GLUTAMICUM WITH BOUND TRANSITION STATE ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE (DAHP)
COMPND 3 SYNTHASE;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CHORISMATE MUTASE;
COMPND 8 CHAIN: E, F, G, H;
COMPND 9 EC: 5.4.99.5;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM GLUTAMICUM;
SOURCE 3 ORGANISM_TAXID: 1718;
SOURCE 4 GENE: CGL2178;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: KA13;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM GLUTAMICUM;
SOURCE 10 ORGANISM_TAXID: 1718;
SOURCE 11 GENE: CGL0853;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_VARIANT: KA13
KEYWDS CHORISMATE MUTASE, DAHP SYNTHASE, SHIKIMATE PATHWAY, COMPLEX,
KEYWDS 2 TRANSFERASE/ISOMERASE, TRANSFERASE-ISOMERASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.BURSCHOWSKY,J.B.HEIM,H.V.THORBJOERNSRUD,U.KRENGEL
REVDAT 4 10-JAN-24 5HUD 1 LINK
REVDAT 3 11-JUL-18 5HUD 1 JRNL
REVDAT 2 31-JAN-18 5HUD 1 JRNL
REVDAT 1 02-AUG-17 5HUD 0
JRNL AUTH D.BURSCHOWSKY,H.V.THORBJORNSRUD,J.B.HEIM,
JRNL AUTH 2 J.R.FAHRIG-KAMARAUSKAITE,K.WURTH-RODERER,P.KAST,U.KRENGEL
JRNL TITL INTER-ENZYME ALLOSTERIC REGULATION OF CHORISMATE MUTASE IN
JRNL TITL 2 CORYNEBACTERIUM GLUTAMICUM: STRUCTURAL BASIS OF FEEDBACK
JRNL TITL 3 ACTIVATION BY TRP.
JRNL REF BIOCHEMISTRY V. 57 557 2018
JRNL REFN ISSN 1520-4995
JRNL PMID 29178787
JRNL DOI 10.1021/ACS.BIOCHEM.7B01018
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 170847
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 8846
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11500
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.4010
REMARK 3 BIN FREE R VALUE SET COUNT : 588
REMARK 3 BIN FREE R VALUE : 0.4070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16558
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 871
REMARK 3 SOLVENT ATOMS : 779
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.57000
REMARK 3 B22 (A**2) : -1.03000
REMARK 3 B33 (A**2) : 0.40000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.09000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.238
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.215
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.237
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.127
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.913
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.867
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17692 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 17019 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 23699 ; 1.531 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 39134 ; 0.986 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2138 ; 6.091 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 835 ;35.924 ;23.689
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2915 ;16.337 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 169 ;16.187 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2605 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19615 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3920 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 8570 ; 1.926 ; 3.211
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8569 ; 1.926 ; 3.210
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10699 ; 3.154 ; 4.802
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 10700 ; 3.154 ; 4.802
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9122 ; 2.165 ; 3.602
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 9122 ; 2.165 ; 3.602
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 13000 ; 3.552 ; 5.247
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 19759 ; 5.800 ;25.468
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 19760 ; 5.800 ;25.470
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5HUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000217715.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.97239
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 : AIMLESS, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 190339
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 131.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 2.950
REMARK 200 R MERGE (I) : 0.19900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.7900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.24
REMARK 200 R MERGE FOR SHELL (I) : 1.76300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.440
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: 2W1A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM IMIDAZOLE/MES BUFFER, PH 6.5 30
REMARK 280 MM EACH OF ETHYLENE GLYCOL MIX (DI-ETHYLENE GLYCOL, TRI-ETHYLENE
REMARK 280 GLYCOL, TETRA-ETHYLENE GLYCOL, PENTA-ETHYLENE GLYCOL) 15%
REMARK 280 GLYCEROL 15% PEG 4000 MICRO-SEEDED FROM BADLY DIFFRACTING
REMARK 280 CRYSTALS (APPROX. 8 AA RESOLUTION), IN 100 MM NA-HEPES, PH 7.5,
REMARK 280 200 MM LISO4, 25% PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 55.24050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 50130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 79870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 MET A 11
REMARK 465 SER A 12
REMARK 465 TRP A 13
REMARK 465 THR A 14
REMARK 465 VAL A 15
REMARK 465 ASP A 16
REMARK 465 ILE A 17
REMARK 465 PRO A 18
REMARK 465 LYS A 19
REMARK 465 GLU A 20
REMARK 465 VAL A 21
REMARK 465 LEU A 22
REMARK 465 PRO A 23
REMARK 465 ASP A 24
REMARK 465 LEU A 25
REMARK 465 PRO A 26
REMARK 465 PRO A 27
REMARK 465 LEU A 28
REMARK 465 MET B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 GLY B 10
REMARK 465 MET B 11
REMARK 465 SER B 12
REMARK 465 TRP B 13
REMARK 465 THR B 14
REMARK 465 VAL B 15
REMARK 465 ASP B 16
REMARK 465 ILE B 17
REMARK 465 PRO B 18
REMARK 465 LYS B 19
REMARK 465 GLU B 20
REMARK 465 VAL B 21
REMARK 465 LEU B 22
REMARK 465 PRO B 23
REMARK 465 ASP B 24
REMARK 465 LEU B 25
REMARK 465 PRO B 26
REMARK 465 PRO B 27
REMARK 465 LEU B 28
REMARK 465 MET C 1
REMARK 465 HIS C 2
REMARK 465 HIS C 3
REMARK 465 HIS C 4
REMARK 465 HIS C 5
REMARK 465 HIS C 6
REMARK 465 PRO C 18
REMARK 465 LYS C 19
REMARK 465 GLU C 20
REMARK 465 VAL C 21
REMARK 465 LEU C 22
REMARK 465 PRO C 23
REMARK 465 ASP C 24
REMARK 465 LEU C 25
REMARK 465 PRO C 26
REMARK 465 PRO C 27
REMARK 465 MET D 1
REMARK 465 HIS D 2
REMARK 465 HIS D 3
REMARK 465 HIS D 4
REMARK 465 HIS D 5
REMARK 465 PRO D 18
REMARK 465 LYS D 19
REMARK 465 GLU D 20
REMARK 465 VAL D 21
REMARK 465 LEU D 22
REMARK 465 PRO D 23
REMARK 465 ASP D 24
REMARK 465 LEU D 25
REMARK 465 PRO D 26
REMARK 465 PRO D 27
REMARK 465 MET E 1
REMARK 465 PRO E 2
REMARK 465 SER E 3
REMARK 465 GLY E 4
REMARK 465 THR E 5
REMARK 465 ASP E 6
REMARK 465 MET F 1
REMARK 465 PRO F 2
REMARK 465 SER F 3
REMARK 465 GLY F 4
REMARK 465 THR F 5
REMARK 465 ASP F 6
REMARK 465 ASP F 7
REMARK 465 MET G 1
REMARK 465 PRO G 2
REMARK 465 SER G 3
REMARK 465 GLY G 4
REMARK 465 THR G 5
REMARK 465 ASP G 6
REMARK 465 ASP G 7
REMARK 465 MET H 1
REMARK 465 PRO H 2
REMARK 465 SER H 3
REMARK 465 GLY H 4
REMARK 465 THR H 5
REMARK 465 ASP H 6
REMARK 465 ASP H 7
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 OE2 GLU E 20 O HOH E 201 2.16
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 ASP A 51 106.53 -58.36
REMARK 500 SER A 147 76.66 -174.66
REMARK 500 ASP A 148 53.00 21.64
REMARK 500 CYS A 450 -114.57 -146.60
REMARK 500 GLU B 30 -67.82 -126.17
REMARK 500 LEU B 284 32.43 -97.60
REMARK 500 THR B 295 27.46 -144.55
REMARK 500 CYS B 450 -111.02 -139.70
REMARK 500 LEU C 149 -148.58 -170.89
REMARK 500 ASP C 150 -33.89 143.05
REMARK 500 ASN C 152 40.65 -145.59
REMARK 500 ALA C 167 52.51 -93.14
REMARK 500 ALA C 220 31.89 -96.97
REMARK 500 LEU C 260 -56.19 -129.82
REMARK 500 ASP C 334 51.68 -118.54
REMARK 500 CYS C 450 -108.96 -137.90
REMARK 500 GLU D 30 -136.28 47.21
REMARK 500 GLU D 246 -113.39 29.79
REMARK 500 LEU D 260 -55.37 -132.07
REMARK 500 ASP D 334 54.11 -119.40
REMARK 500 CYS D 450 -112.67 -145.97
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 C 783 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH D 779 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH D 780 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH D 781 DISTANCE = 6.61 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 506 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 97 SG
REMARK 620 2 HIS A 379 NE2 175.5
REMARK 620 3 GLU A 421 OE1 93.7 88.1
REMARK 620 4 GLU A 421 OE2 97.5 80.4 51.2
REMARK 620 5 ASP A 451 OD2 91.3 85.0 149.3 98.1
REMARK 620 6 HOH A 704 O 104.6 78.7 107.1 150.3 100.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 513 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 97 SG
REMARK 620 2 HIS B 379 NE2 177.7
REMARK 620 3 GLU B 421 OE1 96.5 81.7
REMARK 620 4 ASP B 451 OD2 93.7 87.1 145.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 530 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 97 SG
REMARK 620 2 HIS C 379 NE2 175.3
REMARK 620 3 GLU C 421 OE1 98.5 81.2
REMARK 620 4 GLU C 421 OE2 96.3 79.7 54.0
REMARK 620 5 ASP C 451 OD2 95.9 81.6 141.0 88.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN D 525 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 97 SG
REMARK 620 2 HIS D 379 NE2 176.3
REMARK 620 3 GLU D 421 OE1 101.3 79.2
REMARK 620 4 GLU D 421 OE2 98.8 84.5 53.0
REMARK 620 5 ASP D 451 OD2 96.8 84.8 143.5 93.2
REMARK 620 6 HOH D 746 O 91.4 84.9 102.2 154.6 108.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRP A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRP B 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 527
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 528
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 C 529
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN C 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRP C 532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE D 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 D 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 D 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 D 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 527
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRP D 528
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE E 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE E 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE E 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TSA E 108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG F 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE F 108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE F 109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TSA F 110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG G 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG G 109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE G 110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TSA G 111
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TSA H 106
DBREF 5HUD A 11 472 UNP Q8NNL5 Q8NNL5_CORGL 1 462
DBREF 5HUD B 11 472 UNP Q8NNL5 Q8NNL5_CORGL 1 462
DBREF 5HUD C 11 472 UNP Q8NNL5 Q8NNL5_CORGL 1 462
DBREF 5HUD D 11 472 UNP Q8NNL5 Q8NNL5_CORGL 1 462
DBREF 5HUD E 1 90 UNP Q8NS29 Q8NS29_CORGL 14 103
DBREF 5HUD F 1 90 UNP Q8NS29 Q8NS29_CORGL 14 103
DBREF 5HUD G 1 90 UNP Q8NS29 Q8NS29_CORGL 14 103
DBREF 5HUD H 1 90 UNP Q8NS29 Q8NS29_CORGL 14 103
SEQADV 5HUD MET A 1 UNP Q8NNL5 INITIATING METHIONINE
SEQADV 5HUD HIS A 2 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS A 3 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS A 4 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS A 5 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS A 6 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS A 7 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD SER A 8 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD SER A 9 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD GLY A 10 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD MET B 1 UNP Q8NNL5 INITIATING METHIONINE
SEQADV 5HUD HIS B 2 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS B 3 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS B 4 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS B 5 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS B 6 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS B 7 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD SER B 8 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD SER B 9 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD GLY B 10 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD MET C 1 UNP Q8NNL5 INITIATING METHIONINE
SEQADV 5HUD HIS C 2 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS C 3 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS C 4 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS C 5 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS C 6 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS C 7 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD SER C 8 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD SER C 9 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD GLY C 10 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD MET D 1 UNP Q8NNL5 INITIATING METHIONINE
SEQADV 5HUD HIS D 2 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS D 3 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS D 4 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS D 5 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS D 6 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD HIS D 7 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD SER D 8 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD SER D 9 UNP Q8NNL5 EXPRESSION TAG
SEQADV 5HUD GLY D 10 UNP Q8NNL5 EXPRESSION TAG
SEQRES 1 A 472 MET HIS HIS HIS HIS HIS HIS SER SER GLY MET SER TRP
SEQRES 2 A 472 THR VAL ASP ILE PRO LYS GLU VAL LEU PRO ASP LEU PRO
SEQRES 3 A 472 PRO LEU PRO GLU GLY MET GLN GLN GLN PHE GLU ASP THR
SEQRES 4 A 472 ILE SER ARG ASP ALA LYS GLN GLN PRO THR TRP ASP ARG
SEQRES 5 A 472 ALA GLN ALA GLU ASN VAL ARG LYS ILE LEU GLU SER VAL
SEQRES 6 A 472 PRO PRO ILE VAL VAL ALA PRO GLU VAL LEU GLU LEU LYS
SEQRES 7 A 472 GLN LYS LEU ALA ASP VAL ALA ASN GLY LYS ALA PHE LEU
SEQRES 8 A 472 LEU GLN GLY GLY ASP CYS ALA GLU THR PHE GLU SER ASN
SEQRES 9 A 472 THR GLU PRO HIS ILE ARG ALA ASN VAL LYS THR LEU LEU
SEQRES 10 A 472 GLN MET ALA VAL VAL LEU THR TYR GLY ALA SER THR PRO
SEQRES 11 A 472 VAL ILE LYS MET ALA ARG ILE ALA GLY GLN TYR ALA LYS
SEQRES 12 A 472 PRO ARG SER SER ASP LEU ASP GLY ASN GLY LEU PRO ASN
SEQRES 13 A 472 TYR ARG GLY ASP ILE VAL ASN GLY VAL GLU ALA THR PRO
SEQRES 14 A 472 GLU ALA ARG ARG HIS ASP PRO ALA ARG MET ILE ARG ALA
SEQRES 15 A 472 TYR ALA ASN ALA SER ALA ALA MET ASN LEU VAL ARG ALA
SEQRES 16 A 472 LEU THR SER SER GLY THR ALA ASP LEU TYR ARG LEU SER
SEQRES 17 A 472 GLU TRP ASN ARG GLU PHE VAL ALA ASN SER PRO ALA GLY
SEQRES 18 A 472 ALA ARG TYR GLU ALA LEU ALA ARG GLU ILE ASP SER GLY
SEQRES 19 A 472 LEU ARG PHE MET GLU ALA CYS GLY VAL SER ASP GLU SER
SEQRES 20 A 472 LEU ARG ALA ALA ASP ILE TYR CYS SER HIS GLU ALA LEU
SEQRES 21 A 472 LEU VAL ASP TYR GLU ARG SER MET LEU ARG LEU ALA THR
SEQRES 22 A 472 ASP GLU GLU GLY ASN GLU GLU LEU TYR ASP LEU SER ALA
SEQRES 23 A 472 HIS GLN LEU TRP ILE GLY GLU ARG THR ARG GLY MET ASP
SEQRES 24 A 472 ASP PHE HIS VAL ASN PHE ALA SER MET ILE SER ASN PRO
SEQRES 25 A 472 ILE GLY ILE LYS ILE GLY PRO GLY ILE THR PRO GLU GLU
SEQRES 26 A 472 ALA VAL ALA TYR ALA ASP LYS LEU ASP PRO ASN PHE GLU
SEQRES 27 A 472 PRO GLY ARG LEU THR ILE VAL ALA ARG MET GLY HIS ASP
SEQRES 28 A 472 LYS VAL ARG SER VAL LEU PRO GLY VAL ILE GLN ALA VAL
SEQRES 29 A 472 GLU ALA SER GLY HIS LYS VAL ILE TRP GLN SER ASP PRO
SEQRES 30 A 472 MET HIS GLY ASN THR PHE THR ALA SER ASN GLY TYR LYS
SEQRES 31 A 472 THR ARG HIS PHE ASP LYS VAL ILE ASP GLU VAL GLN GLY
SEQRES 32 A 472 PHE PHE GLU VAL HIS ARG ALA LEU GLY THR HIS PRO GLY
SEQRES 33 A 472 GLY ILE HIS ILE GLU PHE THR GLY GLU ASP VAL THR GLU
SEQRES 34 A 472 CYS LEU GLY GLY ALA GLU ASP ILE THR ASP VAL ASP LEU
SEQRES 35 A 472 PRO GLY ARG TYR GLU SER ALA CYS ASP PRO ARG LEU ASN
SEQRES 36 A 472 THR GLN GLN SER LEU GLU LEU ALA PHE LEU VAL ALA GLU
SEQRES 37 A 472 MET LEU ARG ASN
SEQRES 1 B 472 MET HIS HIS HIS HIS HIS HIS SER SER GLY MET SER TRP
SEQRES 2 B 472 THR VAL ASP ILE PRO LYS GLU VAL LEU PRO ASP LEU PRO
SEQRES 3 B 472 PRO LEU PRO GLU GLY MET GLN GLN GLN PHE GLU ASP THR
SEQRES 4 B 472 ILE SER ARG ASP ALA LYS GLN GLN PRO THR TRP ASP ARG
SEQRES 5 B 472 ALA GLN ALA GLU ASN VAL ARG LYS ILE LEU GLU SER VAL
SEQRES 6 B 472 PRO PRO ILE VAL VAL ALA PRO GLU VAL LEU GLU LEU LYS
SEQRES 7 B 472 GLN LYS LEU ALA ASP VAL ALA ASN GLY LYS ALA PHE LEU
SEQRES 8 B 472 LEU GLN GLY GLY ASP CYS ALA GLU THR PHE GLU SER ASN
SEQRES 9 B 472 THR GLU PRO HIS ILE ARG ALA ASN VAL LYS THR LEU LEU
SEQRES 10 B 472 GLN MET ALA VAL VAL LEU THR TYR GLY ALA SER THR PRO
SEQRES 11 B 472 VAL ILE LYS MET ALA ARG ILE ALA GLY GLN TYR ALA LYS
SEQRES 12 B 472 PRO ARG SER SER ASP LEU ASP GLY ASN GLY LEU PRO ASN
SEQRES 13 B 472 TYR ARG GLY ASP ILE VAL ASN GLY VAL GLU ALA THR PRO
SEQRES 14 B 472 GLU ALA ARG ARG HIS ASP PRO ALA ARG MET ILE ARG ALA
SEQRES 15 B 472 TYR ALA ASN ALA SER ALA ALA MET ASN LEU VAL ARG ALA
SEQRES 16 B 472 LEU THR SER SER GLY THR ALA ASP LEU TYR ARG LEU SER
SEQRES 17 B 472 GLU TRP ASN ARG GLU PHE VAL ALA ASN SER PRO ALA GLY
SEQRES 18 B 472 ALA ARG TYR GLU ALA LEU ALA ARG GLU ILE ASP SER GLY
SEQRES 19 B 472 LEU ARG PHE MET GLU ALA CYS GLY VAL SER ASP GLU SER
SEQRES 20 B 472 LEU ARG ALA ALA ASP ILE TYR CYS SER HIS GLU ALA LEU
SEQRES 21 B 472 LEU VAL ASP TYR GLU ARG SER MET LEU ARG LEU ALA THR
SEQRES 22 B 472 ASP GLU GLU GLY ASN GLU GLU LEU TYR ASP LEU SER ALA
SEQRES 23 B 472 HIS GLN LEU TRP ILE GLY GLU ARG THR ARG GLY MET ASP
SEQRES 24 B 472 ASP PHE HIS VAL ASN PHE ALA SER MET ILE SER ASN PRO
SEQRES 25 B 472 ILE GLY ILE LYS ILE GLY PRO GLY ILE THR PRO GLU GLU
SEQRES 26 B 472 ALA VAL ALA TYR ALA ASP LYS LEU ASP PRO ASN PHE GLU
SEQRES 27 B 472 PRO GLY ARG LEU THR ILE VAL ALA ARG MET GLY HIS ASP
SEQRES 28 B 472 LYS VAL ARG SER VAL LEU PRO GLY VAL ILE GLN ALA VAL
SEQRES 29 B 472 GLU ALA SER GLY HIS LYS VAL ILE TRP GLN SER ASP PRO
SEQRES 30 B 472 MET HIS GLY ASN THR PHE THR ALA SER ASN GLY TYR LYS
SEQRES 31 B 472 THR ARG HIS PHE ASP LYS VAL ILE ASP GLU VAL GLN GLY
SEQRES 32 B 472 PHE PHE GLU VAL HIS ARG ALA LEU GLY THR HIS PRO GLY
SEQRES 33 B 472 GLY ILE HIS ILE GLU PHE THR GLY GLU ASP VAL THR GLU
SEQRES 34 B 472 CYS LEU GLY GLY ALA GLU ASP ILE THR ASP VAL ASP LEU
SEQRES 35 B 472 PRO GLY ARG TYR GLU SER ALA CYS ASP PRO ARG LEU ASN
SEQRES 36 B 472 THR GLN GLN SER LEU GLU LEU ALA PHE LEU VAL ALA GLU
SEQRES 37 B 472 MET LEU ARG ASN
SEQRES 1 C 472 MET HIS HIS HIS HIS HIS HIS SER SER GLY MET SER TRP
SEQRES 2 C 472 THR VAL ASP ILE PRO LYS GLU VAL LEU PRO ASP LEU PRO
SEQRES 3 C 472 PRO LEU PRO GLU GLY MET GLN GLN GLN PHE GLU ASP THR
SEQRES 4 C 472 ILE SER ARG ASP ALA LYS GLN GLN PRO THR TRP ASP ARG
SEQRES 5 C 472 ALA GLN ALA GLU ASN VAL ARG LYS ILE LEU GLU SER VAL
SEQRES 6 C 472 PRO PRO ILE VAL VAL ALA PRO GLU VAL LEU GLU LEU LYS
SEQRES 7 C 472 GLN LYS LEU ALA ASP VAL ALA ASN GLY LYS ALA PHE LEU
SEQRES 8 C 472 LEU GLN GLY GLY ASP CYS ALA GLU THR PHE GLU SER ASN
SEQRES 9 C 472 THR GLU PRO HIS ILE ARG ALA ASN VAL LYS THR LEU LEU
SEQRES 10 C 472 GLN MET ALA VAL VAL LEU THR TYR GLY ALA SER THR PRO
SEQRES 11 C 472 VAL ILE LYS MET ALA ARG ILE ALA GLY GLN TYR ALA LYS
SEQRES 12 C 472 PRO ARG SER SER ASP LEU ASP GLY ASN GLY LEU PRO ASN
SEQRES 13 C 472 TYR ARG GLY ASP ILE VAL ASN GLY VAL GLU ALA THR PRO
SEQRES 14 C 472 GLU ALA ARG ARG HIS ASP PRO ALA ARG MET ILE ARG ALA
SEQRES 15 C 472 TYR ALA ASN ALA SER ALA ALA MET ASN LEU VAL ARG ALA
SEQRES 16 C 472 LEU THR SER SER GLY THR ALA ASP LEU TYR ARG LEU SER
SEQRES 17 C 472 GLU TRP ASN ARG GLU PHE VAL ALA ASN SER PRO ALA GLY
SEQRES 18 C 472 ALA ARG TYR GLU ALA LEU ALA ARG GLU ILE ASP SER GLY
SEQRES 19 C 472 LEU ARG PHE MET GLU ALA CYS GLY VAL SER ASP GLU SER
SEQRES 20 C 472 LEU ARG ALA ALA ASP ILE TYR CYS SER HIS GLU ALA LEU
SEQRES 21 C 472 LEU VAL ASP TYR GLU ARG SER MET LEU ARG LEU ALA THR
SEQRES 22 C 472 ASP GLU GLU GLY ASN GLU GLU LEU TYR ASP LEU SER ALA
SEQRES 23 C 472 HIS GLN LEU TRP ILE GLY GLU ARG THR ARG GLY MET ASP
SEQRES 24 C 472 ASP PHE HIS VAL ASN PHE ALA SER MET ILE SER ASN PRO
SEQRES 25 C 472 ILE GLY ILE LYS ILE GLY PRO GLY ILE THR PRO GLU GLU
SEQRES 26 C 472 ALA VAL ALA TYR ALA ASP LYS LEU ASP PRO ASN PHE GLU
SEQRES 27 C 472 PRO GLY ARG LEU THR ILE VAL ALA ARG MET GLY HIS ASP
SEQRES 28 C 472 LYS VAL ARG SER VAL LEU PRO GLY VAL ILE GLN ALA VAL
SEQRES 29 C 472 GLU ALA SER GLY HIS LYS VAL ILE TRP GLN SER ASP PRO
SEQRES 30 C 472 MET HIS GLY ASN THR PHE THR ALA SER ASN GLY TYR LYS
SEQRES 31 C 472 THR ARG HIS PHE ASP LYS VAL ILE ASP GLU VAL GLN GLY
SEQRES 32 C 472 PHE PHE GLU VAL HIS ARG ALA LEU GLY THR HIS PRO GLY
SEQRES 33 C 472 GLY ILE HIS ILE GLU PHE THR GLY GLU ASP VAL THR GLU
SEQRES 34 C 472 CYS LEU GLY GLY ALA GLU ASP ILE THR ASP VAL ASP LEU
SEQRES 35 C 472 PRO GLY ARG TYR GLU SER ALA CYS ASP PRO ARG LEU ASN
SEQRES 36 C 472 THR GLN GLN SER LEU GLU LEU ALA PHE LEU VAL ALA GLU
SEQRES 37 C 472 MET LEU ARG ASN
SEQRES 1 D 472 MET HIS HIS HIS HIS HIS HIS SER SER GLY MET SER TRP
SEQRES 2 D 472 THR VAL ASP ILE PRO LYS GLU VAL LEU PRO ASP LEU PRO
SEQRES 3 D 472 PRO LEU PRO GLU GLY MET GLN GLN GLN PHE GLU ASP THR
SEQRES 4 D 472 ILE SER ARG ASP ALA LYS GLN GLN PRO THR TRP ASP ARG
SEQRES 5 D 472 ALA GLN ALA GLU ASN VAL ARG LYS ILE LEU GLU SER VAL
SEQRES 6 D 472 PRO PRO ILE VAL VAL ALA PRO GLU VAL LEU GLU LEU LYS
SEQRES 7 D 472 GLN LYS LEU ALA ASP VAL ALA ASN GLY LYS ALA PHE LEU
SEQRES 8 D 472 LEU GLN GLY GLY ASP CYS ALA GLU THR PHE GLU SER ASN
SEQRES 9 D 472 THR GLU PRO HIS ILE ARG ALA ASN VAL LYS THR LEU LEU
SEQRES 10 D 472 GLN MET ALA VAL VAL LEU THR TYR GLY ALA SER THR PRO
SEQRES 11 D 472 VAL ILE LYS MET ALA ARG ILE ALA GLY GLN TYR ALA LYS
SEQRES 12 D 472 PRO ARG SER SER ASP LEU ASP GLY ASN GLY LEU PRO ASN
SEQRES 13 D 472 TYR ARG GLY ASP ILE VAL ASN GLY VAL GLU ALA THR PRO
SEQRES 14 D 472 GLU ALA ARG ARG HIS ASP PRO ALA ARG MET ILE ARG ALA
SEQRES 15 D 472 TYR ALA ASN ALA SER ALA ALA MET ASN LEU VAL ARG ALA
SEQRES 16 D 472 LEU THR SER SER GLY THR ALA ASP LEU TYR ARG LEU SER
SEQRES 17 D 472 GLU TRP ASN ARG GLU PHE VAL ALA ASN SER PRO ALA GLY
SEQRES 18 D 472 ALA ARG TYR GLU ALA LEU ALA ARG GLU ILE ASP SER GLY
SEQRES 19 D 472 LEU ARG PHE MET GLU ALA CYS GLY VAL SER ASP GLU SER
SEQRES 20 D 472 LEU ARG ALA ALA ASP ILE TYR CYS SER HIS GLU ALA LEU
SEQRES 21 D 472 LEU VAL ASP TYR GLU ARG SER MET LEU ARG LEU ALA THR
SEQRES 22 D 472 ASP GLU GLU GLY ASN GLU GLU LEU TYR ASP LEU SER ALA
SEQRES 23 D 472 HIS GLN LEU TRP ILE GLY GLU ARG THR ARG GLY MET ASP
SEQRES 24 D 472 ASP PHE HIS VAL ASN PHE ALA SER MET ILE SER ASN PRO
SEQRES 25 D 472 ILE GLY ILE LYS ILE GLY PRO GLY ILE THR PRO GLU GLU
SEQRES 26 D 472 ALA VAL ALA TYR ALA ASP LYS LEU ASP PRO ASN PHE GLU
SEQRES 27 D 472 PRO GLY ARG LEU THR ILE VAL ALA ARG MET GLY HIS ASP
SEQRES 28 D 472 LYS VAL ARG SER VAL LEU PRO GLY VAL ILE GLN ALA VAL
SEQRES 29 D 472 GLU ALA SER GLY HIS LYS VAL ILE TRP GLN SER ASP PRO
SEQRES 30 D 472 MET HIS GLY ASN THR PHE THR ALA SER ASN GLY TYR LYS
SEQRES 31 D 472 THR ARG HIS PHE ASP LYS VAL ILE ASP GLU VAL GLN GLY
SEQRES 32 D 472 PHE PHE GLU VAL HIS ARG ALA LEU GLY THR HIS PRO GLY
SEQRES 33 D 472 GLY ILE HIS ILE GLU PHE THR GLY GLU ASP VAL THR GLU
SEQRES 34 D 472 CYS LEU GLY GLY ALA GLU ASP ILE THR ASP VAL ASP LEU
SEQRES 35 D 472 PRO GLY ARG TYR GLU SER ALA CYS ASP PRO ARG LEU ASN
SEQRES 36 D 472 THR GLN GLN SER LEU GLU LEU ALA PHE LEU VAL ALA GLU
SEQRES 37 D 472 MET LEU ARG ASN
SEQRES 1 E 90 MET PRO SER GLY THR ASP ASP PRO LEU SER ASP ALA GLU
SEQRES 2 E 90 ILE GLN LYS TYR ARG GLU GLU ILE ASN ARG LEU ASP ARG
SEQRES 3 E 90 GLU ILE LEU ASP ALA VAL LYS ARG ARG THR LYS ILE SER
SEQRES 4 E 90 GLN THR ILE GLY LYS THR ARG MET SER SER GLY GLY THR
SEQRES 5 E 90 ARG LEU VAL HIS THR ARG GLU VAL ALA ILE ILE ASN GLN
SEQRES 6 E 90 PHE ARG GLU GLU ILE GLY GLU GLU GLY PRO ALA LEU ALA
SEQRES 7 E 90 GLY ILE LEU LEU ARG MET GLY ARG GLY LYS LEU GLY
SEQRES 1 F 90 MET PRO SER GLY THR ASP ASP PRO LEU SER ASP ALA GLU
SEQRES 2 F 90 ILE GLN LYS TYR ARG GLU GLU ILE ASN ARG LEU ASP ARG
SEQRES 3 F 90 GLU ILE LEU ASP ALA VAL LYS ARG ARG THR LYS ILE SER
SEQRES 4 F 90 GLN THR ILE GLY LYS THR ARG MET SER SER GLY GLY THR
SEQRES 5 F 90 ARG LEU VAL HIS THR ARG GLU VAL ALA ILE ILE ASN GLN
SEQRES 6 F 90 PHE ARG GLU GLU ILE GLY GLU GLU GLY PRO ALA LEU ALA
SEQRES 7 F 90 GLY ILE LEU LEU ARG MET GLY ARG GLY LYS LEU GLY
SEQRES 1 G 90 MET PRO SER GLY THR ASP ASP PRO LEU SER ASP ALA GLU
SEQRES 2 G 90 ILE GLN LYS TYR ARG GLU GLU ILE ASN ARG LEU ASP ARG
SEQRES 3 G 90 GLU ILE LEU ASP ALA VAL LYS ARG ARG THR LYS ILE SER
SEQRES 4 G 90 GLN THR ILE GLY LYS THR ARG MET SER SER GLY GLY THR
SEQRES 5 G 90 ARG LEU VAL HIS THR ARG GLU VAL ALA ILE ILE ASN GLN
SEQRES 6 G 90 PHE ARG GLU GLU ILE GLY GLU GLU GLY PRO ALA LEU ALA
SEQRES 7 G 90 GLY ILE LEU LEU ARG MET GLY ARG GLY LYS LEU GLY
SEQRES 1 H 90 MET PRO SER GLY THR ASP ASP PRO LEU SER ASP ALA GLU
SEQRES 2 H 90 ILE GLN LYS TYR ARG GLU GLU ILE ASN ARG LEU ASP ARG
SEQRES 3 H 90 GLU ILE LEU ASP ALA VAL LYS ARG ARG THR LYS ILE SER
SEQRES 4 H 90 GLN THR ILE GLY LYS THR ARG MET SER SER GLY GLY THR
SEQRES 5 H 90 ARG LEU VAL HIS THR ARG GLU VAL ALA ILE ILE ASN GLN
SEQRES 6 H 90 PHE ARG GLU GLU ILE GLY GLU GLU GLY PRO ALA LEU ALA
SEQRES 7 H 90 GLY ILE LEU LEU ARG MET GLY ARG GLY LYS LEU GLY
HET GOL A 501 6
HET GOL A 502 6
HET PEG A 503 7
HET PEG A 504 7
HET PGE A 505 10
HET MN A 506 1
HET PO4 A 507 5
HET PO4 A 508 5
HET TRP A 509 15
HET GOL B 501 6
HET GOL B 502 6
HET GOL B 503 6
HET GOL B 504 6
HET GOL B 505 6
HET GOL B 506 6
HET GOL B 507 6
HET GOL B 508 6
HET GOL B 509 6
HET GOL B 510 6
HET PEG B 511 7
HET PG4 B 512 13
HET MN B 513 1
HET PO4 B 514 5
HET TRP B 515 15
HET GOL C 501 6
HET GOL C 502 6
HET GOL C 503 6
HET GOL C 504 6
HET GOL C 505 6
HET GOL C 506 6
HET GOL C 507 6
HET GOL C 508 6
HET GOL C 509 6
HET GOL C 510 6
HET GOL C 511 6
HET GOL C 512 6
HET GOL C 513 6
HET GOL C 514 6
HET GOL C 515 6
HET GOL C 516 6
HET GOL C 517 6
HET GOL C 518 6
HET GOL C 519 6
HET GOL C 520 6
HET PEG C 521 7
HET PEG C 522 7
HET PEG C 523 7
HET PGE C 524 10
HET PGE C 525 10
HET PGE C 526 10
HET PGE C 527 10
HET PGE C 528 10
HET PG4 C 529 13
HET MN C 530 1
HET PO4 C 531 5
HET TRP C 532 15
HET GOL D 501 6
HET GOL D 502 6
HET GOL D 503 6
HET GOL D 504 6
HET GOL D 505 6
HET GOL D 506 6
HET GOL D 507 6
HET GOL D 508 6
HET GOL D 509 6
HET GOL D 510 6
HET GOL D 511 6
HET GOL D 512 6
HET GOL D 513 6
HET PEG D 514 7
HET PEG D 515 7
HET PEG D 516 7
HET PEG D 517 7
HET PEG D 518 7
HET PEG D 519 7
HET PGE D 520 10
HET PGE D 521 10
HET PG4 D 522 13
HET PG4 D 523 13
HET PG4 D 524 13
HET MN D 525 1
HET PO4 D 526 5
HET PO4 D 527 5
HET TRP D 528 15
HET GOL E 101 6
HET GOL E 102 6
HET GOL E 103 6
HET GOL E 104 6
HET PGE E 105 10
HET PGE E 106 10
HET PGE E 107 10
HET TSA E 108 16
HET GOL F 101 6
HET GOL F 102 6
HET GOL F 103 6
HET GOL F 104 6
HET GOL F 105 6
HET GOL F 106 6
HET PEG F 107 7
HET PGE F 108 10
HET PGE F 109 10
HET TSA F 110 16
HET GOL G 101 6
HET GOL G 102 6
HET GOL G 103 6
HET GOL G 104 6
HET GOL G 105 6
HET GOL G 106 6
HET PEG G 107 7
HET PEG G 108 7
HET PEG G 109 7
HET PGE G 110 10
HET TSA G 111 16
HET GOL H 101 6
HET GOL H 102 6
HET GOL H 103 6
HET GOL H 104 6
HET GOL H 105 6
HET TSA H 106 16
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM MN MANGANESE (II) ION
HETNAM PO4 PHOSPHATE ION
HETNAM TRP TRYPTOPHAN
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM TSA 8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-
HETNAM 2 TSA DICARBOXYLIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 GOL 66(C3 H8 O3)
FORMUL 11 PEG 16(C4 H10 O3)
FORMUL 13 PGE 14(C6 H14 O4)
FORMUL 14 MN 4(MN 2+)
FORMUL 15 PO4 6(O4 P 3-)
FORMUL 17 TRP 4(C11 H12 N2 O2)
FORMUL 29 PG4 5(C8 H18 O5)
FORMUL 00 TSA 4(C10 H12 O6)
FORMUL 28 HOH *779(H2 O)
HELIX 1 AA1 MET A 32 SER A 41 1 10
HELIX 2 AA2 ASP A 51 SER A 64 1 14
HELIX 3 AA3 VAL A 70 ASN A 86 1 17
HELIX 4 AA4 THR A 105 SER A 128 1 24
HELIX 5 AA5 THR A 168 ARG A 173 1 6
HELIX 6 AA6 ALA A 177 SER A 199 1 23
HELIX 7 AA7 ASP A 203 SER A 218 1 16
HELIX 8 AA8 ALA A 220 CYS A 241 1 22
HELIX 9 AA9 LEU A 261 MET A 268 1 8
HELIX 10 AB1 GLY A 292 ARG A 296 5 5
HELIX 11 AB2 ASP A 300 ILE A 309 1 10
HELIX 12 AB3 THR A 322 ASP A 334 1 13
HELIX 13 AB4 LYS A 352 SER A 367 1 16
HELIX 14 AB5 HIS A 393 GLY A 412 1 20
HELIX 15 AB6 THR A 438 ARG A 445 5 8
HELIX 16 AB7 ASN A 455 ASN A 472 1 18
HELIX 17 AB8 GLU B 30 SER B 41 1 12
HELIX 18 AB9 ASP B 51 GLU B 63 1 13
HELIX 19 AC1 VAL B 70 ASN B 86 1 17
HELIX 20 AC2 THR B 105 SER B 128 1 24
HELIX 21 AC3 ALA B 177 SER B 199 1 23
HELIX 22 AC4 ASP B 203 SER B 218 1 16
HELIX 23 AC5 ALA B 220 CYS B 241 1 22
HELIX 24 AC6 ASP B 245 ALA B 250 5 6
HELIX 25 AC7 LEU B 261 SER B 267 1 7
HELIX 26 AC8 GLY B 292 ARG B 296 5 5
HELIX 27 AC9 ASP B 300 ILE B 309 1 10
HELIX 28 AD1 THR B 322 ASP B 334 1 13
HELIX 29 AD2 GLY B 349 SER B 367 1 19
HELIX 30 AD3 HIS B 393 GLY B 412 1 20
HELIX 31 AD4 THR B 438 LEU B 442 5 5
HELIX 32 AD5 ASN B 455 ASN B 472 1 18
HELIX 33 AD6 SER C 8 ILE C 17 1 10
HELIX 34 AD7 PRO C 29 SER C 41 1 13
HELIX 35 AD8 ASP C 51 GLU C 63 1 13
HELIX 36 AD9 VAL C 70 ASN C 86 1 17
HELIX 37 AE1 THR C 105 SER C 128 1 24
HELIX 38 AE2 THR C 168 ARG C 173 1 6
HELIX 39 AE3 ALA C 177 GLY C 200 1 24
HELIX 40 AE4 ASP C 203 SER C 218 1 16
HELIX 41 AE5 ALA C 220 CYS C 241 1 22
HELIX 42 AE6 LEU C 261 MET C 268 1 8
HELIX 43 AE7 GLY C 292 ARG C 296 5 5
HELIX 44 AE8 ASP C 300 MET C 308 1 9
HELIX 45 AE9 THR C 322 ASP C 334 1 13
HELIX 46 AF1 LYS C 352 SER C 367 1 16
HELIX 47 AF2 HIS C 393 GLY C 412 1 20
HELIX 48 AF3 THR C 438 LEU C 442 5 5
HELIX 49 AF4 ASN C 455 ASN C 472 1 18
HELIX 50 AF5 HIS D 7 ILE D 17 1 11
HELIX 51 AF6 GLY D 31 ARG D 42 1 12
HELIX 52 AF7 ASP D 51 GLU D 63 1 13
HELIX 53 AF8 VAL D 70 ASN D 86 1 17
HELIX 54 AF9 THR D 105 SER D 128 1 24
HELIX 55 AG1 THR D 168 ARG D 173 1 6
HELIX 56 AG2 ALA D 177 SER D 199 1 23
HELIX 57 AG3 ASP D 203 SER D 218 1 16
HELIX 58 AG4 ALA D 220 CYS D 241 1 22
HELIX 59 AG5 ASP D 245 ARG D 249 5 5
HELIX 60 AG6 LEU D 261 MET D 268 1 8
HELIX 61 AG7 GLY D 292 ARG D 296 5 5
HELIX 62 AG8 ASP D 300 SER D 307 1 8
HELIX 63 AG9 THR D 322 ASP D 334 1 13
HELIX 64 AH1 LYS D 352 SER D 367 1 16
HELIX 65 AH2 HIS D 393 GLY D 412 1 20
HELIX 66 AH3 THR D 438 LEU D 442 5 5
HELIX 67 AH4 ASN D 455 ASN D 472 1 18
HELIX 68 AH5 PRO E 8 SER E 49 1 42
HELIX 69 AH6 VAL E 55 GLY E 71 1 17
HELIX 70 AH7 GLU E 73 GLY E 87 1 15
HELIX 71 AH8 LEU F 9 SER F 48 1 40
HELIX 72 AH9 VAL F 55 GLY F 71 1 17
HELIX 73 AI1 GLU F 73 GLY F 87 1 15
HELIX 74 AI2 LEU G 9 SER G 49 1 41
HELIX 75 AI3 VAL G 55 GLY G 71 1 17
HELIX 76 AI4 GLU G 73 GLY G 87 1 15
HELIX 77 AI5 LEU H 9 SER H 49 1 41
HELIX 78 AI6 VAL H 55 GLY H 71 1 17
HELIX 79 AI7 GLU H 73 GLY H 87 1 15
SHEET 1 AA1 9 PHE A 90 GLY A 95 0
SHEET 2 AA1 9 VAL A 131 ARG A 136 1 O MET A 134 N LEU A 92
SHEET 3 AA1 9 ILE A 253 GLU A 258 1 O TYR A 254 N ALA A 135
SHEET 4 AA1 9 GLN A 288 ILE A 291 1 O GLN A 288 N CYS A 255
SHEET 5 AA1 9 ILE A 313 ILE A 317 1 O LYS A 316 N ILE A 291
SHEET 6 AA1 9 LEU A 342 ALA A 346 1 O VAL A 345 N ILE A 315
SHEET 7 AA1 9 ILE A 372 SER A 375 1 O GLN A 374 N ILE A 344
SHEET 8 AA1 9 PRO A 415 GLU A 421 1 O GLY A 417 N SER A 375
SHEET 9 AA1 9 PHE A 90 GLY A 95 1 N LEU A 91 O GLY A 416
SHEET 1 AA2 2 LEU A 269 THR A 273 0
SHEET 2 AA2 2 GLU A 279 ASP A 283 -1 O TYR A 282 N ARG A 270
SHEET 1 AA3 2 PHE A 383 THR A 384 0
SHEET 2 AA3 2 LYS A 390 THR A 391 -1 O THR A 391 N PHE A 383
SHEET 1 AA4 9 PHE B 90 GLY B 95 0
SHEET 2 AA4 9 VAL B 131 ARG B 136 1 O ILE B 132 N LEU B 92
SHEET 3 AA4 9 ILE B 253 GLU B 258 1 O TYR B 254 N ALA B 135
SHEET 4 AA4 9 GLN B 288 ILE B 291 1 O GLN B 288 N CYS B 255
SHEET 5 AA4 9 ILE B 313 ILE B 317 1 O LYS B 316 N ILE B 291
SHEET 6 AA4 9 LEU B 342 ALA B 346 1 O VAL B 345 N ILE B 315
SHEET 7 AA4 9 ILE B 372 SER B 375 1 O ILE B 372 N ILE B 344
SHEET 8 AA4 9 GLY B 417 GLU B 421 1 O HIS B 419 N SER B 375
SHEET 9 AA4 9 PHE B 90 GLY B 95 1 N GLN B 93 O ILE B 418
SHEET 1 AA5 2 LEU B 269 THR B 273 0
SHEET 2 AA5 2 GLU B 279 ASP B 283 -1 O TYR B 282 N ARG B 270
SHEET 1 AA6 2 PHE B 383 THR B 384 0
SHEET 2 AA6 2 LYS B 390 THR B 391 -1 O THR B 391 N PHE B 383
SHEET 1 AA7 9 PHE C 90 GLY C 95 0
SHEET 2 AA7 9 VAL C 131 ARG C 136 1 O ILE C 132 N LEU C 92
SHEET 3 AA7 9 ILE C 253 GLU C 258 1 O TYR C 254 N LYS C 133
SHEET 4 AA7 9 GLN C 288 ILE C 291 1 O GLN C 288 N CYS C 255
SHEET 5 AA7 9 ILE C 313 ILE C 317 1 O GLY C 314 N LEU C 289
SHEET 6 AA7 9 LEU C 342 ALA C 346 1 O VAL C 345 N ILE C 315
SHEET 7 AA7 9 ILE C 372 SER C 375 1 O GLN C 374 N ILE C 344
SHEET 8 AA7 9 GLY C 417 GLU C 421 1 O HIS C 419 N SER C 375
SHEET 9 AA7 9 PHE C 90 GLY C 95 1 N LEU C 91 O ILE C 418
SHEET 1 AA8 2 LEU C 269 THR C 273 0
SHEET 2 AA8 2 GLU C 279 ASP C 283 -1 O TYR C 282 N ARG C 270
SHEET 1 AA9 2 PHE C 383 THR C 384 0
SHEET 2 AA9 2 LYS C 390 THR C 391 -1 O THR C 391 N PHE C 383
SHEET 1 AB1 9 PHE D 90 GLY D 95 0
SHEET 2 AB1 9 VAL D 131 ARG D 136 1 O ILE D 132 N LEU D 92
SHEET 3 AB1 9 ILE D 253 GLU D 258 1 O TYR D 254 N ALA D 135
SHEET 4 AB1 9 GLN D 288 ILE D 291 1 O GLN D 288 N CYS D 255
SHEET 5 AB1 9 ILE D 313 ILE D 317 1 O LYS D 316 N ILE D 291
SHEET 6 AB1 9 LEU D 342 ALA D 346 1 O VAL D 345 N ILE D 315
SHEET 7 AB1 9 ILE D 372 SER D 375 1 O ILE D 372 N ILE D 344
SHEET 8 AB1 9 GLY D 417 GLU D 421 1 O HIS D 419 N SER D 375
SHEET 9 AB1 9 PHE D 90 GLY D 95 1 N LEU D 91 O ILE D 418
SHEET 1 AB2 2 LEU D 269 THR D 273 0
SHEET 2 AB2 2 GLU D 279 ASP D 283 -1 O TYR D 282 N ARG D 270
SHEET 1 AB3 2 THR D 382 THR D 384 0
SHEET 2 AB3 2 LYS D 390 ARG D 392 -1 O THR D 391 N PHE D 383
LINK SG CYS A 97 MN MN A 506 1555 1555 2.53
LINK NE2 HIS A 379 MN MN A 506 1555 1555 2.36
LINK OE1 GLU A 421 MN MN A 506 1555 1555 2.32
LINK OE2 GLU A 421 MN MN A 506 1555 1555 2.71
LINK OD2 ASP A 451 MN MN A 506 1555 1555 2.20
LINK MN MN A 506 O HOH A 704 1555 1555 2.57
LINK SG CYS B 97 MN MN B 513 1555 1555 2.47
LINK NE2 HIS B 379 MN MN B 513 1555 1555 2.29
LINK OE1 GLU B 421 MN MN B 513 1555 1555 2.21
LINK OD2 ASP B 451 MN MN B 513 1555 1555 2.40
LINK SG CYS C 97 MN MN C 530 1555 1555 2.44
LINK NE2 HIS C 379 MN MN C 530 1555 1555 2.41
LINK OE1 GLU C 421 MN MN C 530 1555 1555 2.12
LINK OE2 GLU C 421 MN MN C 530 1555 1555 2.60
LINK OD2 ASP C 451 MN MN C 530 1555 1555 2.47
LINK SG CYS D 97 MN MN D 525 1555 1555 2.35
LINK NE2 HIS D 379 MN MN D 525 1555 1555 2.40
LINK OE1 GLU D 421 MN MN D 525 1555 1555 2.14
LINK OE2 GLU D 421 MN MN D 525 1555 1555 2.63
LINK OD2 ASP D 451 MN MN D 525 1555 1555 2.45
LINK MN MN D 525 O HOH D 746 1555 1555 2.35
SITE 1 AC1 4 THR A 49 ARG A 173 HIS A 174 ASN D 152
SITE 1 AC2 1 GLN A 362
SITE 1 AC3 8 GLU A 73 THR A 197 ALA A 251 ILE A 253
SITE 2 AC3 8 TYR A 254 HIS A 287 HOH A 604 HOH B 606
SITE 1 AC4 8 LYS A 80 PRO A 130 VAL A 131 ILE A 132
SITE 2 AC4 8 LYS A 133 TRP A 509 HOH A 669 HOH A 690
SITE 1 AC5 5 CYS A 97 HIS A 379 GLU A 421 ASP A 451
SITE 2 AC5 5 HOH A 704
SITE 1 AC6 9 GLY A 292 GLU A 293 ARG A 294 LYS A 316
SITE 2 AC6 9 ARG A 347 HIS A 379 HOH A 643 HOH A 657
SITE 3 AC6 9 HOH A 671
SITE 1 AC7 2 ARG A 145 SER A 146
SITE 1 AC8 13 LEU A 117 ALA A 120 VAL A 121 LYS A 133
SITE 2 AC8 13 ALA A 202 LEU A 207 SER A 247 ALA A 250
SITE 3 AC8 13 PEG A 504 HOH A 669 HOH A 672 ALA D 240
SITE 4 AC8 13 CYS D 241
SITE 1 AC9 4 ALA A 71 LEU A 271 LEU A 284 GLU B 106
SITE 1 AD1 6 LYS B 80 LYS B 133 ASP B 252 TRP B 515
SITE 2 AD1 6 HOH B 601 HOH B 641
SITE 1 AD2 4 GLU A 106 ALA B 71 ARG B 270 LEU B 271
SITE 1 AD3 3 ARG B 110 THR B 201 TRP B 210
SITE 1 AD4 2 ASN B 336 PHE B 337
SITE 1 AD5 4 GLY B 153 PRO B 155 GOL B 508 HOH B 612
SITE 1 AD6 5 SER B 307 MET B 308 ILE B 309 ASN B 336
SITE 2 AD6 5 GLU B 338
SITE 1 AD7 5 THR B 49 ASP B 148 ARG B 173 HIS B 174
SITE 2 AD7 5 GOL B 506
SITE 1 AD8 7 ALA B 44 LYS B 45 GLN B 46 GLN B 47
SITE 2 AD8 7 PRO B 48 THR B 49 HOH B 692
SITE 1 AD9 2 ARG B 145 ARG B 294
SITE 1 AE1 7 GLU B 73 THR B 197 ALA B 251 ASP B 252
SITE 2 AE1 7 ILE B 253 TYR B 254 HOH B 610
SITE 1 AE2 4 CYS B 97 HIS B 379 GLU B 421 ASP B 451
SITE 1 AE3 8 GLY B 292 GLU B 293 ARG B 294 LYS B 316
SITE 2 AE3 8 ARG B 347 HIS B 379 HOH B 643 HOH B 686
SITE 1 AE4 10 LEU B 117 LYS B 133 ALA B 202 LEU B 207
SITE 2 AE4 10 SER B 247 ALA B 250 GOL B 502 HOH B 660
SITE 3 AE4 10 ALA C 240 CYS C 241
SITE 1 AE5 3 GLU C 324 ALA C 363 HOH C 667
SITE 1 AE6 6 MET C 298 GLU C 325 ALA C 328 TYR C 329
SITE 2 AE6 6 HOH C 601 HOH C 608
SITE 1 AE7 4 ARG C 145 SER C 146 GOL C 511 HOH C 613
SITE 1 AE8 3 ASN C 336 GOL C 505 HOH C 733
SITE 1 AE9 4 SER C 307 ASN C 336 GLU C 338 GOL C 504
SITE 1 AF1 1 GLU C 276
SITE 1 AF2 4 ARG C 212 VAL C 215 ALA C 216 PGE F 109
SITE 1 AF3 5 ALA C 184 ASN C 185 PGE C 524 PGE C 527
SITE 2 AF3 5 TYR D 183
SITE 1 AF4 3 THR C 49 ASP C 148 HIS C 174
SITE 1 AF5 5 ARG C 145 LEU C 149 ASP C 150 ASN C 156
SITE 2 AF5 5 GOL C 503
SITE 1 AF6 7 VAL C 121 SER C 208 ASN C 211 ARG C 212
SITE 2 AF6 7 ILE C 231 ASP C 232 LEU C 235
SITE 1 AF7 3 GLU C 425 GLU C 447 ARG C 453
SITE 1 AF8 2 HOH C 603 HOH C 673
SITE 1 AF9 5 LYS C 114 GLN C 118 TRP C 210 THR C 456
SITE 2 AF9 5 HOH C 653
SITE 1 AG1 1 HOH C 714
SITE 1 AG2 2 ASP C 252 SER D 198
SITE 1 AG3 1 PEG C 523
SITE 1 AG4 4 GLU C 213 ASN C 217 GOL C 520 HOH C 718
SITE 1 AG5 1 GOL C 519
SITE 1 AG6 8 LYS C 80 ASP C 83 PRO C 130 ILE C 132
SITE 2 AG6 8 HOH C 612 HOH C 629 HOH C 703 HOH C 725
SITE 1 AG7 1 GOL C 518
SITE 1 AG8 5 ILE C 180 GOL C 509 ILE D 180 ARG D 181
SITE 2 AG8 5 PO4 D 527
SITE 1 AG9 5 GLU C 106 HOH C 650 VAL D 70 ALA D 71
SITE 2 AG9 5 LEU D 271
SITE 1 AH1 7 ALA C 71 ARG C 270 LEU C 271 HOH C 719
SITE 2 AH1 7 HOH C 729 GLU D 106 HOH D 648
SITE 1 AH2 4 PHE C 101 ARG C 181 ASN C 185 GOL C 509
SITE 1 AH3 4 TRP C 13 HOH C 768 GOL F 101 PEG F 107
SITE 1 AH4 1 HOH C 722
SITE 1 AH5 5 CYS C 97 HIS C 379 GLU C 421 ASP C 451
SITE 2 AH5 5 HOH C 758
SITE 1 AH6 9 GLY C 292 GLU C 293 ARG C 294 LYS C 316
SITE 2 AH6 9 ARG C 347 HIS C 379 HOH C 676 HOH C 704
SITE 3 AH6 9 HOH C 720
SITE 1 AH7 12 ALA B 240 CYS B 241 LEU C 117 ALA C 120
SITE 2 AH7 12 VAL C 121 LYS C 133 ALA C 202 LEU C 207
SITE 3 AH7 12 SER C 247 ALA C 250 ALA C 251 HOH C 652
SITE 1 AH8 3 GLU D 324 PEG D 519 HOH D 622
SITE 1 AH9 8 LYS D 45 GLU D 293 ARG D 294 THR D 295
SITE 2 AH9 8 ARG D 296 GLY D 297 ASP D 300 HOH D 608
SITE 1 AI1 5 ARG D 145 SER D 146 SER D 147 ASN D 156
SITE 2 AI1 5 GOL D 504
SITE 1 AI2 6 SER D 147 LEU D 149 ASP D 150 GLY D 151
SITE 2 AI2 6 ASN D 156 GOL D 503
SITE 1 AI3 6 SER C 199 ARG C 206 PRO D 72 GLU D 76
SITE 2 AI3 6 PG4 D 524 HOH D 699
SITE 1 AI4 6 SER D 307 MET D 308 ILE D 309 PRO D 335
SITE 2 AI4 6 ASN D 336 GLU D 338
SITE 1 AI5 4 GLN D 46 ARG D 145 SER D 146 ARG D 158
SITE 1 AI6 7 ASP D 96 ALA D 98 SER D 103 HIS D 108
SITE 2 AI6 7 GLU D 447 ARG D 453 HOH D 632
SITE 1 AI7 4 ARG A 173 THR D 49 ASP D 148 HIS D 174
SITE 1 AI8 3 MET D 11 THR D 14 PEG D 515
SITE 1 AI9 6 GLU D 76 LYS D 80 ASP D 252 TYR D 254
SITE 2 AI9 6 GOL D 513 PG4 D 522
SITE 1 AJ1 3 GLN D 362 ALA D 363 HOH D 706
SITE 1 AJ2 8 LYS D 80 LYS D 133 ALA D 251 ASP D 252
SITE 2 AJ2 8 GOL D 511 TRP D 528 HOH D 601 HOH D 606
SITE 1 AJ3 3 PRO C 72 THR D 201 ARG D 206
SITE 1 AJ4 1 GOL D 510
SITE 1 AJ5 3 GLU D 276 HOH D 664 HOH D 736
SITE 1 AJ6 1 ALA D 216
SITE 1 AJ7 3 GLN D 79 PHE D 337 GLU D 338
SITE 1 AJ8 2 GLU D 324 GOL D 501
SITE 1 AJ9 2 HIS D 6 PEG G 109
SITE 1 AK1 11 ARG C 249 HOH C 609 GLU D 73 GLU D 76
SITE 2 AK1 11 ARG D 194 THR D 197 ALA D 251 ASP D 252
SITE 3 AK1 11 ILE D 253 TYR D 254 GOL D 511
SITE 1 AK2 3 LYS D 45 GLU D 293 ARG D 296
SITE 1 AK3 10 ARG C 110 THR C 201 ARG C 206 TRP C 210
SITE 2 AK3 10 PRO D 72 THR D 273 ASP D 274 GLU D 275
SITE 3 AK3 10 GOL D 505 HOH D 695
SITE 1 AK4 5 CYS D 97 HIS D 379 GLU D 421 ASP D 451
SITE 2 AK4 5 HOH D 746
SITE 1 AK5 8 GLY D 292 GLU D 293 ARG D 294 LYS D 316
SITE 2 AK5 8 ARG D 347 HIS D 379 HOH D 646 HOH D 723
SITE 1 AK6 6 PGE C 524 PHE D 101 ARG D 181 ASN D 185
SITE 2 AK6 6 HOH D 620 HOH D 627
SITE 1 AK7 9 CYS A 241 LEU D 117 LYS D 133 ALA D 202
SITE 2 AK7 9 LEU D 207 SER D 247 ALA D 250 GOL D 513
SITE 3 AK7 9 HOH D 641
SITE 1 AK8 4 LEU E 9 SER E 10 SER F 49 GOL F 106
SITE 1 AK9 6 LYS E 33 LYS E 37 GOL E 103 PGE E 105
SITE 2 AK9 6 PEG F 107 HOH F 204
SITE 1 AL1 4 LYS E 37 GOL E 102 PGE E 105 HOH E 205
SITE 1 AL2 2 ARG E 18 THR F 57
SITE 1 AL3 3 GOL E 102 GOL E 103 PGE E 106
SITE 1 AL4 1 PGE E 105
SITE 1 AL5 4 ASP E 30 ARG E 34 HOH E 224 GLU F 27
SITE 1 AL6 13 ARG E 35 SER E 39 ILE E 42 ARG E 46
SITE 2 AL6 13 LEU E 54 VAL E 55 ARG E 58 GLU E 59
SITE 3 AL6 13 ILE E 62 LEU E 82 ARG E 86 HOH E 206
SITE 4 AL6 13 ARG F 18
SITE 1 AL7 5 PGE C 528 ARG E 26 LYS E 33 GLU F 69
SITE 2 AL7 5 PEG F 107
SITE 1 AL8 5 ASN E 22 ARG F 58 ALA F 61 GLN F 65
SITE 2 AL8 5 HOH F 207
SITE 1 AL9 4 ARG C 409 ARG F 53 ARG F 86 LYS F 88
SITE 1 AM1 1 GOL F 105
SITE 1 AM2 1 GOL F 104
SITE 1 AM3 2 GOL E 101 SER F 48
SITE 1 AM4 4 PGE C 528 GOL E 102 GOL F 101 HOH F 213
SITE 1 AM5 1 HOH F 229
SITE 1 AM6 1 GOL C 508
SITE 1 AM7 13 ARG E 18 ARG F 35 SER F 39 ILE F 42
SITE 2 AM7 13 ARG F 46 LEU F 54 VAL F 55 ARG F 58
SITE 3 AM7 13 GLU F 59 LEU F 82 ARG F 86 HOH F 208
SITE 4 AM7 13 HOH F 210
SITE 1 AM8 4 ASP G 30 LYS G 33 ARG G 34 PEG G 109
SITE 1 AM9 3 PEG G 107 PGE G 110 HOH G 216
SITE 1 AN1 4 LEU G 9 SER G 10 SER H 49 GOL H 105
SITE 1 AN2 1 PGE G 110
SITE 1 AN3 4 ARG G 26 LYS G 33 HOH G 223 GLU H 69
SITE 1 AN4 4 ARG G 58 ALA G 61 GLN G 65 ASN H 22
SITE 1 AN5 5 LYS G 33 THR G 36 GLN G 40 GOL G 102
SITE 2 AN5 5 HOH G 210
SITE 1 AN6 3 PGE D 521 GOL G 101 PGE G 110
SITE 1 AN7 3 GOL G 102 GOL G 104 PEG G 109
SITE 1 AN8 13 ARG G 35 SER G 39 ILE G 42 ARG G 46
SITE 2 AN8 13 LEU G 54 VAL G 55 ARG G 58 GLU G 59
SITE 3 AN8 13 ILE G 62 LEU G 82 ARG G 86 HOH G 209
SITE 4 AN8 13 ARG H 18
SITE 1 AN9 9 GLN D 402 ARG D 409 ASN D 472 ARG H 53
SITE 2 AN9 9 ARG H 86 GLY H 87 LYS H 88 GLY H 90
SITE 3 AN9 9 GOL H 103
SITE 1 AO1 7 ASN G 22 ARG H 58 ALA H 61 GLN H 65
SITE 2 AO1 7 HOH H 219 HOH H 226 HOH H 229
SITE 1 AO2 7 GLN H 40 GLY H 85 ARG H 86 GLY H 87
SITE 2 AO2 7 GOL H 101 HOH H 201 HOH H 203
SITE 1 AO3 1 GLU H 68
SITE 1 AO4 1 GOL G 103
SITE 1 AO5 13 ARG G 18 ARG H 35 SER H 39 ILE H 42
SITE 2 AO5 13 ARG H 46 LEU H 54 VAL H 55 GLU H 59
SITE 3 AO5 13 ILE H 62 LEU H 82 ARG H 86 HOH H 206
SITE 4 AO5 13 HOH H 228
CRYST1 117.622 110.481 134.652 90.00 101.41 90.00 P 1 21 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 0.008502 0.000000 0.001716 0.00000
SCALE2 0.000000 0.009051 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007576 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
