HEADER OXIDOREDUCTASE 06-MAR-12 4E1G
TITLE X-RAY CRYSTAL STRUCTURE OF ALPHA-LINOLENIC ACID BOUND TO THE
TITLE 2 CYCLOOXYGENASE CHANNEL OF CYCLOOXYGENASE-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-604;
COMPND 5 SYNONYM: CYCLOOXYGENASE-2, COX-2, GLUCOCORTICOID-REGULATED
COMPND 6 INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, MACROPHAGE ACTIVATION-
COMPND 7 ASSOCIATED MARKER PROTEIN P71/73, PES-2, PHS II, PROSTAGLANDIN H2
COMPND 8 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PROSTAGLANDIN-ENDOPEROXIDE
COMPND 9 SYNTHASE 2, TIS10 PROTEIN;
COMPND 10 EC: 1.14.99.1;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 STRAIN: WILD TYPE;
SOURCE 6 GENE: COX-2, COX2, PGHS-B, PTGS2, TIS10;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS MONOTOPIC MEMBRANE PROTEIN, BIOLOGICAL DIMER, OXIDOREDUCTASE, COX-2,
KEYWDS 2 N-GLYCOSYLATION, MEMBRANE OF ER
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.VECCHIO,M.G.MALKOWSKI
REVDAT 3 01-AUG-12 4E1G 1 JRNL
REVDAT 2 13-JUN-12 4E1G 1 JRNL
REVDAT 1 25-APR-12 4E1G 0
JRNL AUTH A.J.VECCHIO,B.J.ORLANDO,R.NANDAGIRI,M.G.MALKOWSKI
JRNL TITL INVESTIGATING SUBSTRATE PROMISCUITY IN CYCLOOXYGENASE-2: THE
JRNL TITL 2 ROLE OF ARG-120 AND RESIDUES LINING THE HYDROPHOBIC GROOVE.
JRNL REF J.BIOL.CHEM. V. 287 24619 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22637474
JRNL DOI 10.1074/JBC.M112.372243
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 79080
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4154
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5579
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 289
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8840
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 335
REMARK 3 SOLVENT ATOMS : 746
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.41000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : -0.56000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.172
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.101
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.250
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9517 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12954 ; 2.044 ; 2.001
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1118 ; 6.327 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 440 ;37.343 ;23.841
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1486 ;14.697 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;14.417 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1381 ; 0.148 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7317 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 5541 ; 1.037 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9005 ; 1.757 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3976 ; 3.243 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3939 ; 4.852 ; 4.500
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 : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 33 A 114
REMARK 3 ORIGIN FOR THE GROUP (A): 55.7541 45.6869 63.8335
REMARK 3 T TENSOR
REMARK 3 T11: .0350 T22: .1527
REMARK 3 T33: .1883 T12: -.0394
REMARK 3 T13: -.0381 T23: -.0652
REMARK 3 L TENSOR
REMARK 3 L11: .6320 L22: 1.0370
REMARK 3 L33: .8200 L12: -.6482
REMARK 3 L13: .0323 L23: .4310
REMARK 3 S TENSOR
REMARK 3 S11: -.0526 S12: -.0470 S13: .2179
REMARK 3 S21: -.0423 S22: .1793 S23: -.2238
REMARK 3 S31: -.1111 S32: .3047 S33: -.1268
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 115 A 226
REMARK 3 ORIGIN FOR THE GROUP (A): 37.3441 35.8213 66.9008
REMARK 3 T TENSOR
REMARK 3 T11: .0729 T22: .0686
REMARK 3 T33: .0695 T12: .0196
REMARK 3 T13: -.0083 T23: .0012
REMARK 3 L TENSOR
REMARK 3 L11: .6246 L22: .7472
REMARK 3 L33: .4718 L12: -.3485
REMARK 3 L13: -.0798 L23: .3139
REMARK 3 S TENSOR
REMARK 3 S11: -.0673 S12: -.0913 S13: -.0387
REMARK 3 S21: .0721 S22: .0820 S23: .0048
REMARK 3 S31: .0384 S32: .0680 S33: -.0147
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 227 A 582
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3961 47.7015 66.4355
REMARK 3 T TENSOR
REMARK 3 T11: .0389 T22: .0351
REMARK 3 T33: .0532 T12: -.0048
REMARK 3 T13: -.0074 T23: -.0144
REMARK 3 L TENSOR
REMARK 3 L11: .6613 L22: .5279
REMARK 3 L33: .6480 L12: -.4560
REMARK 3 L13: .0936 L23: .0625
REMARK 3 S TENSOR
REMARK 3 S11: -.0271 S12: -.1330 S13: -.0008
REMARK 3 S21: .0556 S22: .0654 S23: .0226
REMARK 3 S31: -.0365 S32: -.0069 S33: -.0383
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 33 B 119
REMARK 3 ORIGIN FOR THE GROUP (A): 43.9869 57.8689 29.1286
REMARK 3 T TENSOR
REMARK 3 T11: .2051 T22: .0509
REMARK 3 T33: .1445 T12: -.0577
REMARK 3 T13: .0664 T23: .0408
REMARK 3 L TENSOR
REMARK 3 L11: 1.4679 L22: 1.3492
REMARK 3 L33: 1.1293 L12: -1.1801
REMARK 3 L13: -.2180 L23: .1344
REMARK 3 S TENSOR
REMARK 3 S11: .2193 S12: .0830 S13: .2764
REMARK 3 S21: -.2274 S22: -.1146 S23: -.3387
REMARK 3 S31: -.4355 S32: .1588 S33: -.1047
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 120 B 228
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0893 41.0382 26.7697
REMARK 3 T TENSOR
REMARK 3 T11: .0772 T22: .0918
REMARK 3 T33: .0462 T12: .0477
REMARK 3 T13: -.0160 T23: -.0192
REMARK 3 L TENSOR
REMARK 3 L11: .3281 L22: .6792
REMARK 3 L33: .7960 L12: -.2177
REMARK 3 L13: -.2070 L23: .3113
REMARK 3 S TENSOR
REMARK 3 S11: .0916 S12: .1063 S13: -.0175
REMARK 3 S21: -.1366 S22: -.0954 S23: .0146
REMARK 3 S31: -.1490 S32: -.0429 S33: .0038
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 229 B 582
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3094 29.9826 27.3896
REMARK 3 T TENSOR
REMARK 3 T11: .0287 T22: .0678
REMARK 3 T33: .0493 T12: .0130
REMARK 3 T13: .0044 T23: -.0345
REMARK 3 L TENSOR
REMARK 3 L11: .4960 L22: .7349
REMARK 3 L33: .8355 L12: -.3199
REMARK 3 L13: .0696 L23: .0156
REMARK 3 S TENSOR
REMARK 3 S11: .0733 S12: .1375 S13: -.0415
REMARK 3 S21: -.1304 S22: -.0245 S23: -.0341
REMARK 3 S31: -.0611 S32: .0110 S33: -.0488
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: NULL
REMARK 4
REMARK 4 4E1G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071048.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9767
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79080
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000
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) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.51600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB ENTRY 1CVU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-34% POLYACRYLIC ACID 5100, 100MM
REMARK 280 HEPES PH 7.5, 20MM MGCL2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 60.18900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.06550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 90.21900
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 60.18900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.06550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 90.21900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 60.18900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.06550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 90.21900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 60.18900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 66.06550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 90.21900
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 10
REMARK 465 LEU A 11
REMARK 465 PHE A 12
REMARK 465 ARG A 13
REMARK 465 ALA A 14
REMARK 465 VAL A 15
REMARK 465 LEU A 16
REMARK 465 LEU A 17
REMARK 465 CYS A 18
REMARK 465 ALA A 19
REMARK 465 ALA A 20
REMARK 465 LEU A 21
REMARK 465 GLY A 22
REMARK 465 LEU A 23
REMARK 465 SER A 24
REMARK 465 GLN A 25
REMARK 465 ALA A 26
REMARK 465 ALA A 27
REMARK 465 ASN A 28
REMARK 465 HIS A 29
REMARK 465 HIS A 30
REMARK 465 HIS A 31
REMARK 465 HIS A 32
REMARK 465 GLN A 583
REMARK 465 ASP A 584
REMARK 465 PRO A 585
REMARK 465 GLN A 586
REMARK 465 PRO A 587
REMARK 465 THR A 588
REMARK 465 LYS A 589
REMARK 465 THR A 590
REMARK 465 ALA A 591
REMARK 465 THR A 592
REMARK 465 ILE A 593
REMARK 465 ALA A 594
REMARK 465 ALA A 595
REMARK 465 SER A 596
REMARK 465 ALA A 597
REMARK 465 SER A 598
REMARK 465 HIS A 599
REMARK 465 SER A 600
REMARK 465 ARG A 601
REMARK 465 LEU A 602
REMARK 465 ASP A 603
REMARK 465 ASP A 604
REMARK 465 ILE A 605
REMARK 465 ASN A 606
REMARK 465 PRO A 607
REMARK 465 THR A 608
REMARK 465 VAL A 609
REMARK 465 LEU A 610
REMARK 465 ILE A 611
REMARK 465 LYS A 612
REMARK 465 ARG A 613
REMARK 465 ARG A 614
REMARK 465 SER A 615
REMARK 465 THR A 616
REMARK 465 GLU A 617
REMARK 465 LEU A 618
REMARK 465 MET B 10
REMARK 465 LEU B 11
REMARK 465 PHE B 12
REMARK 465 ARG B 13
REMARK 465 ALA B 14
REMARK 465 VAL B 15
REMARK 465 LEU B 16
REMARK 465 LEU B 17
REMARK 465 CYS B 18
REMARK 465 ALA B 19
REMARK 465 ALA B 20
REMARK 465 LEU B 21
REMARK 465 GLY B 22
REMARK 465 LEU B 23
REMARK 465 SER B 24
REMARK 465 GLN B 25
REMARK 465 ALA B 26
REMARK 465 ALA B 27
REMARK 465 ASN B 28
REMARK 465 HIS B 29
REMARK 465 HIS B 30
REMARK 465 HIS B 31
REMARK 465 HIS B 32
REMARK 465 GLN B 583
REMARK 465 ASP B 584
REMARK 465 PRO B 585
REMARK 465 GLN B 586
REMARK 465 PRO B 587
REMARK 465 THR B 588
REMARK 465 LYS B 589
REMARK 465 THR B 590
REMARK 465 ALA B 591
REMARK 465 THR B 592
REMARK 465 ILE B 593
REMARK 465 ALA B 594
REMARK 465 ALA B 595
REMARK 465 SER B 596
REMARK 465 ALA B 597
REMARK 465 SER B 598
REMARK 465 HIS B 599
REMARK 465 SER B 600
REMARK 465 ARG B 601
REMARK 465 LEU B 602
REMARK 465 ASP B 603
REMARK 465 ASP B 604
REMARK 465 ILE B 605
REMARK 465 ASN B 606
REMARK 465 PRO B 607
REMARK 465 THR B 608
REMARK 465 VAL B 609
REMARK 465 LEU B 610
REMARK 465 ILE B 611
REMARK 465 LYS B 612
REMARK 465 ARG B 613
REMARK 465 ARG B 614
REMARK 465 SER B 615
REMARK 465 THR B 616
REMARK 465 GLU B 617
REMARK 465 LEU B 618
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 53 CG OD1 OD2
REMARK 470 GLN A 54 CD OE1 NE2
REMARK 470 LYS A 56 CE NZ
REMARK 470 LEU A 75 CD1 CD2
REMARK 470 LYS A 79 CG CD CE NZ
REMARK 470 LEU A 81 CD1 CD2
REMARK 470 LYS A 83 CG CD CE NZ
REMARK 470 LYS A 97 CD CE NZ
REMARK 470 LYS A 169 CD CE NZ
REMARK 470 GLU A 170 CD OE1 OE2
REMARK 470 LYS A 175 NZ
REMARK 470 LYS A 215 CD CE NZ
REMARK 470 ASP A 239 OD1 OD2
REMARK 470 LYS A 248 CE NZ
REMARK 470 LYS A 267 CD CE NZ
REMARK 470 GLU A 272 CD OE1 OE2
REMARK 470 LYS A 358 CE NZ
REMARK 470 LYS A 405 CD CE NZ
REMARK 470 GLU A 416 OE1 OE2
REMARK 470 LYS A 473 CG CD CE NZ
REMARK 470 LYS A 485 CE NZ
REMARK 470 LYS A 511 CE NZ
REMARK 470 LYS A 557 CG CD CE NZ
REMARK 470 GLN B 54 CG CD OE1 NE2
REMARK 470 LYS B 56 CE NZ
REMARK 470 LEU B 75 CD1 CD2
REMARK 470 LYS B 79 CE NZ
REMARK 470 LYS B 83 CD CE NZ
REMARK 470 LYS B 97 CE NZ
REMARK 470 LYS B 169 CD CE NZ
REMARK 470 LYS B 215 CD CE NZ
REMARK 470 ASP B 239 OD1 OD2
REMARK 470 LYS B 267 NZ
REMARK 470 GLU B 281 CG CD OE1 OE2
REMARK 470 LYS B 358 CE NZ
REMARK 470 ASP B 399 OD1 OD2
REMARK 470 LYS B 405 CE NZ
REMARK 470 GLU B 416 CD OE1 OE2
REMARK 470 LYS B 473 CD CE NZ
REMARK 470 LYS B 492 CE NZ
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 ND2 ASN B 68 O5 NAG B 703 1.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 275 CE2 TYR A 275 CD2 0.093
REMARK 500 CYS A 575 CB CYS A 575 SG 0.114
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 230 CB - CG - CD1 ANGL. DEV. = 10.5 DEGREES
REMARK 500 LEU A 294 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 MET A 299 CG - SD - CE ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG B 44 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP B 173 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 LEU B 294 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 MET B 458 CG - SD - CE ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG B 467 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG B 467 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
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 THR A 60 119.36 -36.49
REMARK 500 SER A 126 111.10 -160.33
REMARK 500 THR A 129 -96.79 -125.37
REMARK 500 TRP A 387 45.98 -90.16
REMARK 500 GLU A 398 -123.60 60.84
REMARK 500 ASN A 410 74.02 -111.28
REMARK 500 SER A 496 -47.90 62.93
REMARK 500 THR B 129 -92.34 -124.86
REMARK 500 ARG B 185 -89.00 -88.14
REMARK 500 TRP B 387 46.25 -88.86
REMARK 500 GLU B 398 -117.63 59.49
REMARK 500 TYR B 409 -1.61 73.48
REMARK 500 ASN B 439 20.50 -140.83
REMARK 500 SER B 496 -54.77 66.69
REMARK 500 SER B 579 -169.57 -169.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 581 VAL A 582 145.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 HIS A 207 24.9 L L OUTSIDE RANGE
REMARK 500 VAL A 582 16.9 L L OUTSIDE RANGE
REMARK 500 PHE B 209 24.9 L L OUTSIDE RANGE
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 B1135 DISTANCE = 5.07 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 COH B 702 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388 NE2
REMARK 620 2 COH B 702 NA 88.8
REMARK 620 3 COH B 702 NB 92.3 89.6
REMARK 620 4 COH B 702 NC 86.9 175.1 92.9
REMARK 620 5 COH B 702 ND 80.0 88.7 172.1 88.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 COH A 702 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388 NE2
REMARK 620 2 COH A 702 NA 80.8
REMARK 620 3 COH A 702 NB 90.4 81.2
REMARK 620 4 COH A 702 NC 89.8 169.8 95.2
REMARK 620 5 COH A 702 ND 77.2 93.2 167.1 88.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LNL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 712
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKR A 713
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LNL B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 712
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TZI RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF
REMARK 900 G533V MURINE COX-2
REMARK 900 RELATED ID: 3HS5 RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF
REMARK 900 CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3HS6 RELATED DB: PDB
REMARK 900 EICOSAPENTAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL
REMARK 900 OF CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3HS7 RELATED DB: PDB
REMARK 900 DOCOSAHEXAENOIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF
REMARK 900 CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 3QH0 RELATED DB: PDB
REMARK 900 PALMITIC ACID BOUND TO THE CYCLOOXYGENASE CHANNEL OF
REMARK 900 CYCLOOXYGENASE-2
REMARK 900 RELATED ID: 1DIY RELATED DB: PDB
REMARK 900 ARACHIDONIC ACID BOUND TO COX-1
DBREF 4E1G A 10 618 UNP Q05769 PGH2_MOUSE 1 604
DBREF 4E1G B 10 618 UNP Q05769 PGH2_MOUSE 1 604
SEQADV 4E1G HIS A 29 UNP Q05769 EXPRESSION TAG
SEQADV 4E1G HIS A 30 UNP Q05769 EXPRESSION TAG
SEQADV 4E1G HIS A 31 UNP Q05769 EXPRESSION TAG
SEQADV 4E1G HIS A 32 UNP Q05769 EXPRESSION TAG
SEQADV 4E1G HIS A 33 UNP Q05769 EXPRESSION TAG
SEQADV 4E1G HIS A 34 UNP Q05769 EXPRESSION TAG
SEQADV 4E1G ALA A 594 UNP Q05769 ASN 580 ENGINEERED MUTATION
SEQADV 4E1G HIS B 29 UNP Q05769 EXPRESSION TAG
SEQADV 4E1G HIS B 30 UNP Q05769 EXPRESSION TAG
SEQADV 4E1G HIS B 31 UNP Q05769 EXPRESSION TAG
SEQADV 4E1G HIS B 32 UNP Q05769 EXPRESSION TAG
SEQADV 4E1G HIS B 33 UNP Q05769 EXPRESSION TAG
SEQADV 4E1G HIS B 34 UNP Q05769 EXPRESSION TAG
SEQADV 4E1G ALA B 594 UNP Q05769 ASN 580 ENGINEERED MUTATION
SEQRES 1 A 610 MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY
SEQRES 2 A 610 LEU SER GLN ALA ALA ASN HIS HIS HIS HIS HIS HIS PRO
SEQRES 3 A 610 CYS CYS SER ASN PRO CYS GLN ASN ARG GLY GLU CYS MET
SEQRES 4 A 610 SER THR GLY PHE ASP GLN TYR LYS CYS ASP CYS THR ARG
SEQRES 5 A 610 THR GLY PHE TYR GLY GLU ASN CYS THR THR PRO GLU PHE
SEQRES 6 A 610 LEU THR ARG ILE LYS LEU LEU LEU LYS PRO THR PRO ASN
SEQRES 7 A 610 THR VAL HIS TYR ILE LEU THR HIS PHE LYS GLY VAL TRP
SEQRES 8 A 610 ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG SER LEU ILE
SEQRES 9 A 610 MET LYS TYR VAL LEU THR SER ARG SER TYR LEU ILE ASP
SEQRES 10 A 610 SER PRO PRO THR TYR ASN VAL HIS TYR GLY TYR LYS SER
SEQRES 11 A 610 TRP GLU ALA PHE SER ASN LEU SER TYR TYR THR ARG ALA
SEQRES 12 A 610 LEU PRO PRO VAL ALA ASP ASP CYS PRO THR PRO MET GLY
SEQRES 13 A 610 VAL LYS GLY ASN LYS GLU LEU PRO ASP SER LYS GLU VAL
SEQRES 14 A 610 LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE ILE PRO ASP
SEQRES 15 A 610 PRO GLN GLY SER ASN MET MET PHE ALA PHE PHE ALA GLN
SEQRES 16 A 610 HIS PHE THR HIS GLN PHE PHE LYS THR ASP HIS LYS ARG
SEQRES 17 A 610 GLY PRO GLY PHE THR ARG GLY LEU GLY HIS GLY VAL ASP
SEQRES 18 A 610 LEU ASN HIS ILE TYR GLY GLU THR LEU ASP ARG GLN HIS
SEQRES 19 A 610 LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN
SEQRES 20 A 610 VAL ILE GLY GLY GLU VAL TYR PRO PRO THR VAL LYS ASP
SEQRES 21 A 610 THR GLN VAL GLU MET ILE TYR PRO PRO HIS ILE PRO GLU
SEQRES 22 A 610 ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL PHE GLY LEU
SEQRES 23 A 610 VAL PRO GLY LEU MET MET TYR ALA THR ILE TRP LEU ARG
SEQRES 24 A 610 GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS GLN GLU HIS
SEQRES 25 A 610 PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN THR SER ARG
SEQRES 26 A 610 LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL ILE GLU
SEQRES 27 A 610 ASP TYR VAL GLN HIS LEU SER GLY TYR HIS PHE LYS LEU
SEQRES 28 A 610 LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN GLN PHE GLN
SEQRES 29 A 610 TYR GLN ASN ARG ILE ALA SER GLU PHE ASN THR LEU TYR
SEQRES 30 A 610 HIS TRP HIS PRO LEU LEU PRO ASP THR PHE ASN ILE GLU
SEQRES 31 A 610 ASP GLN GLU TYR SER PHE LYS GLN PHE LEU TYR ASN ASN
SEQRES 32 A 610 SER ILE LEU LEU GLU HIS GLY LEU THR GLN PHE VAL GLU
SEQRES 33 A 610 SER PHE THR ARG GLN ILE ALA GLY ARG VAL ALA GLY GLY
SEQRES 34 A 610 ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL ALA LYS ALA
SEQRES 35 A 610 SER ILE ASP GLN SER ARG GLU MET LYS TYR GLN SER LEU
SEQRES 36 A 610 ASN GLU TYR ARG LYS ARG PHE SER LEU LYS PRO TYR THR
SEQRES 37 A 610 SER PHE GLU GLU LEU THR GLY GLU LYS GLU MET ALA ALA
SEQRES 38 A 610 GLU LEU LYS ALA LEU TYR SER ASP ILE ASP VAL MET GLU
SEQRES 39 A 610 LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO ARG PRO ASP
SEQRES 40 A 610 ALA ILE PHE GLY GLU THR MET VAL GLU LEU GLY ALA PRO
SEQRES 41 A 610 PHE SER LEU LYS GLY LEU MET GLY ASN PRO ILE CYS SER
SEQRES 42 A 610 PRO GLN TYR TRP LYS PRO SER THR PHE GLY GLY GLU VAL
SEQRES 43 A 610 GLY PHE LYS ILE ILE ASN THR ALA SER ILE GLN SER LEU
SEQRES 44 A 610 ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE THR SER PHE
SEQRES 45 A 610 ASN VAL GLN ASP PRO GLN PRO THR LYS THR ALA THR ILE
SEQRES 46 A 610 ALA ALA SER ALA SER HIS SER ARG LEU ASP ASP ILE ASN
SEQRES 47 A 610 PRO THR VAL LEU ILE LYS ARG ARG SER THR GLU LEU
SEQRES 1 B 610 MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY
SEQRES 2 B 610 LEU SER GLN ALA ALA ASN HIS HIS HIS HIS HIS HIS PRO
SEQRES 3 B 610 CYS CYS SER ASN PRO CYS GLN ASN ARG GLY GLU CYS MET
SEQRES 4 B 610 SER THR GLY PHE ASP GLN TYR LYS CYS ASP CYS THR ARG
SEQRES 5 B 610 THR GLY PHE TYR GLY GLU ASN CYS THR THR PRO GLU PHE
SEQRES 6 B 610 LEU THR ARG ILE LYS LEU LEU LEU LYS PRO THR PRO ASN
SEQRES 7 B 610 THR VAL HIS TYR ILE LEU THR HIS PHE LYS GLY VAL TRP
SEQRES 8 B 610 ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG SER LEU ILE
SEQRES 9 B 610 MET LYS TYR VAL LEU THR SER ARG SER TYR LEU ILE ASP
SEQRES 10 B 610 SER PRO PRO THR TYR ASN VAL HIS TYR GLY TYR LYS SER
SEQRES 11 B 610 TRP GLU ALA PHE SER ASN LEU SER TYR TYR THR ARG ALA
SEQRES 12 B 610 LEU PRO PRO VAL ALA ASP ASP CYS PRO THR PRO MET GLY
SEQRES 13 B 610 VAL LYS GLY ASN LYS GLU LEU PRO ASP SER LYS GLU VAL
SEQRES 14 B 610 LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE ILE PRO ASP
SEQRES 15 B 610 PRO GLN GLY SER ASN MET MET PHE ALA PHE PHE ALA GLN
SEQRES 16 B 610 HIS PHE THR HIS GLN PHE PHE LYS THR ASP HIS LYS ARG
SEQRES 17 B 610 GLY PRO GLY PHE THR ARG GLY LEU GLY HIS GLY VAL ASP
SEQRES 18 B 610 LEU ASN HIS ILE TYR GLY GLU THR LEU ASP ARG GLN HIS
SEQRES 19 B 610 LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN
SEQRES 20 B 610 VAL ILE GLY GLY GLU VAL TYR PRO PRO THR VAL LYS ASP
SEQRES 21 B 610 THR GLN VAL GLU MET ILE TYR PRO PRO HIS ILE PRO GLU
SEQRES 22 B 610 ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL PHE GLY LEU
SEQRES 23 B 610 VAL PRO GLY LEU MET MET TYR ALA THR ILE TRP LEU ARG
SEQRES 24 B 610 GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS GLN GLU HIS
SEQRES 25 B 610 PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN THR SER ARG
SEQRES 26 B 610 LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL ILE GLU
SEQRES 27 B 610 ASP TYR VAL GLN HIS LEU SER GLY TYR HIS PHE LYS LEU
SEQRES 28 B 610 LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN GLN PHE GLN
SEQRES 29 B 610 TYR GLN ASN ARG ILE ALA SER GLU PHE ASN THR LEU TYR
SEQRES 30 B 610 HIS TRP HIS PRO LEU LEU PRO ASP THR PHE ASN ILE GLU
SEQRES 31 B 610 ASP GLN GLU TYR SER PHE LYS GLN PHE LEU TYR ASN ASN
SEQRES 32 B 610 SER ILE LEU LEU GLU HIS GLY LEU THR GLN PHE VAL GLU
SEQRES 33 B 610 SER PHE THR ARG GLN ILE ALA GLY ARG VAL ALA GLY GLY
SEQRES 34 B 610 ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL ALA LYS ALA
SEQRES 35 B 610 SER ILE ASP GLN SER ARG GLU MET LYS TYR GLN SER LEU
SEQRES 36 B 610 ASN GLU TYR ARG LYS ARG PHE SER LEU LYS PRO TYR THR
SEQRES 37 B 610 SER PHE GLU GLU LEU THR GLY GLU LYS GLU MET ALA ALA
SEQRES 38 B 610 GLU LEU LYS ALA LEU TYR SER ASP ILE ASP VAL MET GLU
SEQRES 39 B 610 LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO ARG PRO ASP
SEQRES 40 B 610 ALA ILE PHE GLY GLU THR MET VAL GLU LEU GLY ALA PRO
SEQRES 41 B 610 PHE SER LEU LYS GLY LEU MET GLY ASN PRO ILE CYS SER
SEQRES 42 B 610 PRO GLN TYR TRP LYS PRO SER THR PHE GLY GLY GLU VAL
SEQRES 43 B 610 GLY PHE LYS ILE ILE ASN THR ALA SER ILE GLN SER LEU
SEQRES 44 B 610 ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE THR SER PHE
SEQRES 45 B 610 ASN VAL GLN ASP PRO GLN PRO THR LYS THR ALA THR ILE
SEQRES 46 B 610 ALA ALA SER ALA SER HIS SER ARG LEU ASP ASP ILE ASN
SEQRES 47 B 610 PRO THR VAL LEU ILE LYS ARG ARG SER THR GLU LEU
MODRES 4E1G ASN B 68 ASN GLYCOSYLATION SITE
MODRES 4E1G ASN B 144 ASN GLYCOSYLATION SITE
MODRES 4E1G ASN A 68 ASN GLYCOSYLATION SITE
MODRES 4E1G ASN A 144 ASN GLYCOSYLATION SITE
MODRES 4E1G ASN B 410 ASN GLYCOSYLATION SITE
MODRES 4E1G ASN A 410 ASN GLYCOSYLATION SITE
HET LNL A 701 20
HET COH A 702 43
HET NAG A 703 14
HET NAG A 704 14
HET NAG A 705 14
HET NAG A 706 14
HET MAN A 707 11
HET NAG A 708 14
HET BOG A 709 20
HET EDO A 710 4
HET EDO A 711 4
HET AKR A 712 5
HET AKR A 713 5
HET LNL B 701 20
HET COH B 702 43
HET NAG B 703 14
HET NAG B 704 14
HET NAG B 705 14
HET NAG B 706 14
HET NAG B 707 14
HET EDO B 708 4
HET EDO B 709 4
HET EDO B 710 4
HET EDO B 711 4
HET EDO B 712 4
HETNAM LNL ALPHA-LINOLENIC ACID
HETNAM COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM BOG B-OCTYLGLUCOSIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM AKR ACRYLIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 LNL 2(C18 H30 O2)
FORMUL 4 COH 2(C34 H32 CO N4 O4)
FORMUL 5 NAG 10(C8 H15 N O6)
FORMUL 6 MAN C6 H12 O6
FORMUL 8 BOG C14 H28 O6
FORMUL 9 EDO 7(C2 H6 O2)
FORMUL 11 AKR 2(C3 H4 O2)
FORMUL 23 HOH *746(H2 O)
HELIX 1 1 GLU A 73 LYS A 83 1 11
HELIX 2 2 THR A 85 THR A 94 1 10
HELIX 3 3 PHE A 96 ASN A 105 1 10
HELIX 4 4 ILE A 105A TYR A 122 1 18
HELIX 5 5 SER A 138 ASN A 144 1 7
HELIX 6 6 ASP A 173 LEU A 182 1 10
HELIX 7 7 ASN A 195 HIS A 207 1 13
HELIX 8 8 LEU A 230 GLY A 235 1 6
HELIX 9 9 THR A 237 ARG A 245 1 9
HELIX 10 10 THR A 265 GLN A 270 1 6
HELIX 11 11 PRO A 280 GLN A 284 5 5
HELIX 12 12 VAL A 291 LEU A 294 5 4
HELIX 13 13 VAL A 295 HIS A 320 1 26
HELIX 14 14 GLY A 324 ASP A 347 1 24
HELIX 15 15 ASP A 347 GLY A 354 1 8
HELIX 16 16 ASP A 362 PHE A 367 5 6
HELIX 17 17 ALA A 378 TYR A 385 1 8
HELIX 18 18 HIS A 386 LEU A 391 5 6
HELIX 19 19 SER A 403 LEU A 408 1 6
HELIX 20 20 ASN A 410 GLN A 429 1 20
HELIX 21 21 PRO A 441 ALA A 443 5 3
HELIX 22 22 VAL A 444 MET A 458 1 15
HELIX 23 23 SER A 462 PHE A 470 1 9
HELIX 24 24 SER A 477 GLY A 483 1 7
HELIX 25 25 LYS A 485 SER A 496 1 12
HELIX 26 26 ASP A 497 MET A 501 5 5
HELIX 27 27 GLU A 502 GLU A 510 1 9
HELIX 28 28 GLY A 519 GLY A 536 1 18
HELIX 29 29 ASN A 537 SER A 541 5 5
HELIX 30 30 LYS A 546 GLY A 551 5 6
HELIX 31 31 GLY A 552 THR A 561 1 10
HELIX 32 32 SER A 563 VAL A 572 1 10
HELIX 33 33 GLU B 73 LYS B 83 1 11
HELIX 34 34 THR B 85 THR B 94 1 10
HELIX 35 35 PHE B 96 ASN B 105 1 10
HELIX 36 36 ILE B 105A LEU B 123 1 19
HELIX 37 37 SER B 138 ASN B 144 1 7
HELIX 38 38 ASP B 173 LEU B 182 1 10
HELIX 39 39 ASN B 195 HIS B 207 1 13
HELIX 40 40 LEU B 230 GLY B 235 1 6
HELIX 41 41 THR B 237 ARG B 245 1 9
HELIX 42 42 THR B 265 GLN B 270 1 6
HELIX 43 43 PRO B 280 GLN B 284 5 5
HELIX 44 44 VAL B 291 LEU B 294 5 4
HELIX 45 45 VAL B 295 HIS B 320 1 26
HELIX 46 46 GLY B 324 ASP B 347 1 24
HELIX 47 47 ASP B 347 GLY B 354 1 8
HELIX 48 48 ASP B 362 PHE B 367 5 6
HELIX 49 49 ALA B 378 TYR B 385 1 8
HELIX 50 50 HIS B 386 LEU B 391 5 6
HELIX 51 51 SER B 403 LEU B 408 1 6
HELIX 52 52 ASN B 411 GLY B 418 1 8
HELIX 53 53 GLY B 418 GLN B 429 1 12
HELIX 54 54 PRO B 441 ALA B 443 5 3
HELIX 55 55 VAL B 444 MET B 458 1 15
HELIX 56 56 SER B 462 PHE B 470 1 9
HELIX 57 57 SER B 477 GLY B 483 1 7
HELIX 58 58 LYS B 485 SER B 496 1 12
HELIX 59 59 ASP B 497 MET B 501 5 5
HELIX 60 60 GLU B 502 GLU B 510 1 9
HELIX 61 61 GLY B 519 GLY B 536 1 18
HELIX 62 62 ASN B 537 SER B 541 5 5
HELIX 63 63 LYS B 546 GLY B 551 5 6
HELIX 64 64 GLY B 552 THR B 561 1 10
HELIX 65 65 SER B 563 VAL B 572 1 10
SHEET 1 A 2 GLU A 46 GLY A 51 0
SHEET 2 A 2 GLN A 54 ASP A 58 -1 O GLN A 54 N THR A 50
SHEET 1 B 2 PHE A 64 TYR A 65 0
SHEET 2 B 2 THR A 71 PRO A 72 -1 O THR A 71 N TYR A 65
SHEET 1 C 2 GLN A 255 ILE A 257 0
SHEET 2 C 2 GLU A 260 TYR A 262 -1 O GLU A 260 N ILE A 257
SHEET 1 D 2 PHE A 395 ILE A 397 0
SHEET 2 D 2 GLN A 400 TYR A 402 -1 O TYR A 402 N PHE A 395
SHEET 1 E 2 GLU B 46 SER B 49 0
SHEET 2 E 2 TYR B 55 ASP B 58 -1 O ASP B 58 N GLU B 46
SHEET 1 F 2 PHE B 64 TYR B 65 0
SHEET 2 F 2 THR B 71 PRO B 72 -1 O THR B 71 N TYR B 65
SHEET 1 G 2 THR B 212 ASP B 213 0
SHEET 2 G 2 GLY B 217 THR B 221 -1 O GLY B 217 N ASP B 213
SHEET 1 H 2 GLN B 255 ILE B 257 0
SHEET 2 H 2 GLU B 260 TYR B 262 -1 O TYR B 262 N GLN B 255
SHEET 1 I 2 PHE B 395 ILE B 397 0
SHEET 2 I 2 GLN B 400 TYR B 402 -1 O TYR B 402 N PHE B 395
SSBOND 1 CYS A 36 CYS A 47 1555 1555 2.08
SSBOND 2 CYS A 37 CYS A 159 1555 1555 2.03
SSBOND 3 CYS A 41 CYS A 57 1555 1555 2.01
SSBOND 4 CYS A 59 CYS A 69 1555 1555 2.10
SSBOND 5 CYS A 569 CYS A 575 1555 1555 2.09
SSBOND 6 CYS B 36 CYS B 47 1555 1555 2.14
SSBOND 7 CYS B 37 CYS B 159 1555 1555 2.07
SSBOND 8 CYS B 41 CYS B 57 1555 1555 2.02
SSBOND 9 CYS B 59 CYS B 69 1555 1555 2.06
SSBOND 10 CYS B 569 CYS B 575 1555 1555 2.07
LINK ND2 ASN B 68 C1 NAG B 703 1555 1555 1.34
LINK O4 NAG B 703 C1 NAG B 704 1555 1555 1.43
LINK O4 NAG A 703 C1 NAG A 704 1555 1555 1.43
LINK ND2 ASN B 144 C1 NAG B 705 1555 1555 1.43
LINK ND2 ASN A 68 C1 NAG A 703 1555 1555 1.44
LINK ND2 ASN A 144 C1 NAG A 705 1555 1555 1.44
LINK O4 NAG A 705 C1 NAG A 706 1555 1555 1.45
LINK ND2 ASN B 410 C1 NAG B 707 1555 1555 1.45
LINK O4 NAG B 705 C1 NAG B 706 1555 1555 1.45
LINK O4 NAG A 706 C1 MAN A 707 1555 1555 1.45
LINK ND2 ASN A 410 C1 NAG A 708 1555 1555 1.46
LINK NE2AHIS B 388 CO COH B 702 1555 1555 2.38
LINK NE2BHIS A 388 CO COH A 702 1555 1555 2.72
CISPEP 1 SER A 126 PRO A 127 0 -0.92
CISPEP 2 SER B 126 PRO B 127 0 1.15
SITE 1 AC1 13 ARG A 120 PHE A 205 PHE A 209 TYR A 348
SITE 2 AC1 13 VAL A 349 TYR A 355 ILE A 377 PHE A 381
SITE 3 AC1 13 TYR A 385 ALA A 527 SER A 530 GLY A 533
SITE 4 AC1 13 LEU A 534
SITE 1 AC2 15 ALA A 199 GLN A 203 HIS A 207 PHE A 210
SITE 2 AC2 15 THR A 212 HIS A 214 VAL A 295 ASN A 382
SITE 3 AC2 15 TYR A 385 HIS A 386 HIS A 388 LEU A 391
SITE 4 AC2 15 LEU A 408 VAL A 447 HOH A1080
SITE 1 AC3 7 TYR A 55 GLU A 67 ASN A 68 NAG A 704
SITE 2 AC3 7 HOH A 882 HOH A1078 HOH A1162
SITE 1 AC4 3 NAG A 703 HOH A1078 HOH A1153
SITE 1 AC5 9 GLU A 140 ASN A 144 TYR A 147 ARG A 216
SITE 2 AC5 9 NAG A 706 HOH A 847 HOH A 904 HOH A 914
SITE 3 AC5 9 HOH A1077
SITE 1 AC6 3 ARG A 216 NAG A 705 MAN A 707
SITE 1 AC7 2 NAG A 706 HOH A1180
SITE 1 AC8 3 ASN A 410 SER A 412 ILE A 413
SITE 1 AC9 11 GLU A 179 LYS A 180 ARG A 184 ARG A 185
SITE 2 AC9 11 ARG A 438 GLU A 486 GLU A 490 GLU B 179
SITE 3 AC9 11 ARG B 185 ILE B 442 GLN B 445
SITE 1 BC1 6 PRO A 162 SER A 455 ARG A 456 LYS A 459
SITE 2 BC1 6 TYR A 460 HOH A 942
SITE 1 BC2 8 GLU A 308 ARG A 311 GLU A 339 SER A 566
SITE 2 BC2 8 LEU A 567 ASN A 570 ASN A 571 HOH A 845
SITE 1 BC3 5 SER A 477 PHE A 478 GLU A 479 LYS A 492
SITE 2 BC3 5 HOH A1076
SITE 1 BC4 6 ASP A 239 ARG A 240 LYS A 243 VAL A 271
SITE 2 BC4 6 GLU A 272 HOH A1114
SITE 1 BC5 14 ARG B 120 PHE B 205 PHE B 209 TYR B 348
SITE 2 BC5 14 VAL B 349 LEU B 352 TYR B 355 ILE B 377
SITE 3 BC5 14 PHE B 381 TYR B 385 ALA B 527 SER B 530
SITE 4 BC5 14 GLY B 533 LEU B 534
SITE 1 BC6 17 ALA B 199 GLN B 203 HIS B 207 PHE B 210
SITE 2 BC6 17 LYS B 211 THR B 212 HIS B 214 VAL B 295
SITE 3 BC6 17 ASN B 382 TYR B 385 HIS B 386 TRP B 387
SITE 4 BC6 17 HIS B 388 LEU B 391 LEU B 408 VAL B 447
SITE 5 BC6 17 HOH B1119
SITE 1 BC7 5 TYR B 55 GLU B 67 ASN B 68 NAG B 704
SITE 2 BC7 5 HOH B1004
SITE 1 BC8 1 NAG B 703
SITE 1 BC9 9 LEU A 238 GLU B 140 ASN B 144 ARG B 216
SITE 2 BC9 9 NAG B 706 HOH B 802 HOH B 916 HOH B1019
SITE 3 BC9 9 HOH B1117
SITE 1 CC1 3 ARG B 216 NAG B 705 HOH B1091
SITE 1 CC2 6 GLN B 406 ASN B 410 ILE B 413 HOH B 937
SITE 2 CC2 6 HOH B 938 HOH B1125
SITE 1 CC3 5 PRO B 162 ARG B 456 LYS B 459 TYR B 460
SITE 2 CC3 5 HOH B 914
SITE 1 CC4 5 ARG B 240 LYS B 243 GLN B 270 VAL B 271
SITE 2 CC4 5 GLU B 272
SITE 1 CC5 6 LYS B 251 TYR B 254 VAL B 261 ASN B 310
SITE 2 CC5 6 HOH B 857 HOH B1007
SITE 1 CC6 6 LEU A 224 SER B 143 HOH B 867 HOH B 911
SITE 2 CC6 6 HOH B 954 HOH B1093
SITE 1 CC7 7 GLU B 308 ARG B 311 GLU B 339 SER B 566
SITE 2 CC7 7 LEU B 567 ASN B 570 HOH B 854
CRYST1 120.378 132.131 180.438 90.00 90.00 90.00 I 2 2 2 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 0.008307 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007568 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005542 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
