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HEADER HYDROLASE/HYDROLASE INHIBITOR 01-SEP-17 6AUM
TITLE CRYSTAL STRUCTURE OF HUMAN SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH
TITLE 2 TRANS-4-[4-(3-TRIFLUOROMETHOXYPHENYL-L-UREIDO)-CYCLOHEXYLOXY]-BENZOIC
TITLE 3 ACID.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.3.2.10,3.1.3.76;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EPHX2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: ACHSEH1
KEYWDS SOLUBLE EPOXIDE HYDROLASE, UREA INHIBITORS, NEUROPATHIC PAIN,
KEYWDS 2 HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.D.KODANI,S.BAHKTA,S.H.HWANG,S.PAKHOMOVA,M.E.NEWCOMER,C.MORISSEAU,
AUTHOR 2 B.HAMMOCK
REVDAT 1 07-FEB-18 6AUM 0
JRNL AUTH S.D.KODANI,S.BHAKTA,S.H.HWANG,S.PAKHOMOVA,M.E.NEWCOMER,
JRNL AUTH 2 C.MORISSEAU,B.D.HAMMOCK
JRNL TITL IDENTIFICATION AND OPTIMIZATION OF SOLUBLE EPOXIDE HYDROLASE
JRNL TITL 2 INHIBITORS WITH DUAL POTENCY TOWARDS FATTY ACID AMIDE
JRNL TITL 3 HYDROLASE.
JRNL REF BIOORG. MED. CHEM. LETT. 2018
JRNL REFN ESSN 1464-3405
JRNL PMID 29366648
JRNL DOI 10.1016/J.BMCL.2018.01.003
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 12929
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 674
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) : 2.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : 908
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.3420
REMARK 3 BIN FREE R VALUE SET COUNT : 48
REMARK 3 BIN FREE R VALUE : 0.4540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4331
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 25
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 78.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.45000
REMARK 3 B22 (A**2) : -0.45000
REMARK 3 B33 (A**2) : 1.47000
REMARK 3 B12 (A**2) : -0.23000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.448
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.363
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 43.443
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4493 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4199 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6082 ; 1.407 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9763 ; 0.945 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 550 ; 6.520 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 194 ;36.069 ;24.227
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 787 ;16.698 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;18.097 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 665 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4916 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 901 ; 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): 2194 ; 0.525 ; 2.888
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2193 ; 0.525 ; 2.887
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2743 ; 0.925 ; 4.331
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2744 ; 0.925 ; 4.331
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2298 ; 0.585 ; 2.974
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2299 ; 0.585 ; 2.976
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3339 ; 0.866 ; 4.438
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4911 ; 2.132 ;33.690
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4912 ; 2.132 ;33.694
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 : 8
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 2 A 24
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2232 -50.4183 -10.8297
REMARK 3 T TENSOR
REMARK 3 T11: 0.2321 T22: 0.3035
REMARK 3 T33: 0.1773 T12: -0.1340
REMARK 3 T13: 0.0728 T23: -0.0957
REMARK 3 L TENSOR
REMARK 3 L11: 9.6110 L22: 5.3484
REMARK 3 L33: 4.6524 L12: -2.9257
REMARK 3 L13: 1.3199 L23: -0.9279
REMARK 3 S TENSOR
REMARK 3 S11: 0.2876 S12: -0.3047 S13: -0.7338
REMARK 3 S21: -0.4131 S22: 0.1724 S23: 0.2095
REMARK 3 S31: 0.3130 S32: 0.3727 S33: -0.4600
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 25 A 75
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9626 -70.3328 -5.4481
REMARK 3 T TENSOR
REMARK 3 T11: 0.3192 T22: 0.4455
REMARK 3 T33: 0.2459 T12: -0.0073
REMARK 3 T13: 0.0191 T23: -0.0535
REMARK 3 L TENSOR
REMARK 3 L11: 9.9595 L22: 0.6406
REMARK 3 L33: 2.0703 L12: -1.6098
REMARK 3 L13: -3.8877 L23: 0.9788
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: 0.5902 S13: -0.5328
REMARK 3 S21: 0.0016 S22: -0.0433 S23: -0.1297
REMARK 3 S31: 0.1093 S32: 0.0924 S33: 0.0338
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 76 A 152
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8961 -53.4429 -2.5311
REMARK 3 T TENSOR
REMARK 3 T11: 0.2719 T22: 0.4075
REMARK 3 T33: 0.1857 T12: -0.0555
REMARK 3 T13: 0.0346 T23: -0.1123
REMARK 3 L TENSOR
REMARK 3 L11: 1.3563 L22: 0.8038
REMARK 3 L33: 2.0650 L12: 1.0402
REMARK 3 L13: -0.1974 L23: -0.1233
REMARK 3 S TENSOR
REMARK 3 S11: 0.0608 S12: 0.0949 S13: -0.1984
REMARK 3 S21: 0.0524 S22: 0.0934 S23: -0.1807
REMARK 3 S31: -0.0982 S32: 0.3444 S33: -0.1542
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 : A 153 A 222
REMARK 3 ORIGIN FOR THE GROUP (A): -27.2533 -49.5768 -16.4239
REMARK 3 T TENSOR
REMARK 3 T11: 0.2845 T22: 0.4302
REMARK 3 T33: 0.1706 T12: -0.1571
REMARK 3 T13: 0.0289 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 1.0120 L22: 6.0137
REMARK 3 L33: 1.5441 L12: 1.3190
REMARK 3 L13: -0.4791 L23: -1.8263
REMARK 3 S TENSOR
REMARK 3 S11: -0.2870 S12: 0.4108 S13: 0.2448
REMARK 3 S21: -0.6526 S22: 0.5196 S23: 0.2432
REMARK 3 S31: 0.1571 S32: -0.3329 S33: -0.2327
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 : A 223 A 283
REMARK 3 ORIGIN FOR THE GROUP (A): -23.5953 -29.2211 13.4166
REMARK 3 T TENSOR
REMARK 3 T11: 0.1275 T22: 0.1291
REMARK 3 T33: 0.0318 T12: -0.0218
REMARK 3 T13: -0.0073 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 0.9047 L22: 1.8238
REMARK 3 L33: 3.7428 L12: 0.2606
REMARK 3 L13: 0.1127 L23: -0.5850
REMARK 3 S TENSOR
REMARK 3 S11: -0.0503 S12: -0.0441 S13: 0.0009
REMARK 3 S21: -0.1688 S22: 0.1538 S23: 0.2300
REMARK 3 S31: 0.0281 S32: 0.0164 S33: -0.1035
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 : A 284 A 382
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1076 -20.6204 24.7345
REMARK 3 T TENSOR
REMARK 3 T11: 0.1412 T22: 0.1667
REMARK 3 T33: 0.0571 T12: -0.0012
REMARK 3 T13: -0.0083 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 1.3464 L22: 1.7304
REMARK 3 L33: 1.3402 L12: 0.0780
REMARK 3 L13: -0.0253 L23: -0.6509
REMARK 3 S TENSOR
REMARK 3 S11: 0.0348 S12: -0.1270 S13: 0.1193
REMARK 3 S21: 0.2205 S22: -0.0565 S23: -0.2513
REMARK 3 S31: -0.3166 S32: 0.1381 S33: 0.0217
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 383 A 468
REMARK 3 ORIGIN FOR THE GROUP (A): -26.0339 -8.8858 10.2907
REMARK 3 T TENSOR
REMARK 3 T11: 0.2064 T22: 0.1926
REMARK 3 T33: 0.1358 T12: -0.0185
REMARK 3 T13: -0.0417 T23: 0.0893
REMARK 3 L TENSOR
REMARK 3 L11: 1.5945 L22: 4.1474
REMARK 3 L33: 3.8351 L12: -0.8069
REMARK 3 L13: 0.6860 L23: 0.4207
REMARK 3 S TENSOR
REMARK 3 S11: -0.1204 S12: 0.3107 S13: 0.3906
REMARK 3 S21: -0.4117 S22: 0.0632 S23: 0.1215
REMARK 3 S31: -0.4345 S32: 0.0391 S33: 0.0572
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 469 A 548
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6174 -20.6354 17.0871
REMARK 3 T TENSOR
REMARK 3 T11: 0.0752 T22: 0.1515
REMARK 3 T33: 0.1363 T12: -0.0226
REMARK 3 T13: 0.0229 T23: 0.0413
REMARK 3 L TENSOR
REMARK 3 L11: 2.1267 L22: 2.4357
REMARK 3 L33: 4.6713 L12: 0.6559
REMARK 3 L13: 0.8184 L23: 0.6860
REMARK 3 S TENSOR
REMARK 3 S11: -0.0893 S12: 0.1587 S13: 0.0451
REMARK 3 S21: -0.0342 S22: 0.0157 S23: -0.4946
REMARK 3 S31: -0.0381 S32: 0.2635 S33: 0.0735
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 6AUM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1000229820.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CAMD
REMARK 200 BEAMLINE : GCPCC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.38079
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13636
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11000
REMARK 200 FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.66000
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1S8O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, 0-10% SUCROSE, PH 7.5,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 162.49067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.24533
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 121.86800
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 40.62267
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 203.11333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 162.49067
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 81.24533
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 40.62267
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 121.86800
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 203.11333
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: 5890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.500000 -0.866025 0.000000 -46.35650
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 -80.29181
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 40.62267
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 PRO A 549
REMARK 465 PRO A 550
REMARK 465 VAL A 551
REMARK 465 VAL A 552
REMARK 465 SER A 553
REMARK 465 LYS A 554
REMARK 465 MET A 555
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 OH TYR A 383 O21 BXV A 603 2.19
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 ARG A 467 NE - CZ - NH1 ANGL. DEV. = 3.4 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 LEU A 10 -76.15 -85.28
REMARK 500 VAL A 13 -68.55 -132.99
REMARK 500 CYS A 154 3.81 -69.74
REMARK 500 PRO A 161 41.97 -104.53
REMARK 500 GLN A 204 -97.30 -110.09
REMARK 500 LYS A 245 145.25 171.67
REMARK 500 GLU A 269 -153.56 -129.30
REMARK 500 ASP A 335 -115.79 60.18
REMARK 500 ASN A 359 -56.75 81.61
REMARK 500 GLU A 414 27.19 -148.44
REMARK 500 LYS A 456 -73.70 -70.22
REMARK 500 VAL A 498 -60.63 -105.32
REMARK 500 HIS A 513 37.27 -97.99
REMARK 500 ASP A 521 71.17 44.64
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 MET A 291 ASP A 292 145.39
REMARK 500
REMARK 500 REMARK: NULL
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 MG A 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 9 OD2
REMARK 620 2 ASP A 11 O 92.7
REMARK 620 3 ASP A 185 OD1 84.4 85.9
REMARK 620 4 PO4 A 601 O1 108.5 99.3 165.7
REMARK 620 5 HOH A 702 O 106.8 160.3 93.4 77.2
REMARK 620 6 HOH A 701 O 157.8 68.6 82.6 86.9 91.8
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 PO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BXV A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 605
DBREF 6AUM A 1 555 UNP P34913 HYES_HUMAN 1 555
SEQRES 1 A 555 MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY VAL
SEQRES 2 A 555 LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG THR
SEQRES 3 A 555 GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN ASP
SEQRES 4 A 555 ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR ARG
SEQRES 5 A 555 LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE PRO
SEQRES 6 A 555 LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR ALA
SEQRES 7 A 555 LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU ILE
SEQRES 8 A 555 PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG PRO
SEQRES 9 A 555 MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY PHE
SEQRES 10 A 555 THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP ARG
SEQRES 11 A 555 ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU LEU
SEQRES 12 A 555 LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN VAL
SEQRES 13 A 555 GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE LEU
SEQRES 14 A 555 LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL PHE
SEQRES 15 A 555 LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG ASP
SEQRES 16 A 555 LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP THR
SEQRES 17 A 555 ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN LEU
SEQRES 18 A 555 LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO
SEQRES 19 A 555 SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG
SEQRES 20 A 555 VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA
SEQRES 21 A 555 VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER
SEQRES 22 A 555 TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR
SEQRES 23 A 555 ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER
SEQRES 24 A 555 SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL
SEQRES 25 A 555 LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY
SEQRES 26 A 555 LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY
SEQRES 27 A 555 MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG
SEQRES 28 A 555 VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO
SEQRES 29 A 555 ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA
SEQRES 30 A 555 ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO
SEQRES 31 A 555 GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG
SEQRES 32 A 555 THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL
SEQRES 33 A 555 LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE
SEQRES 34 A 555 VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET VAL
SEQRES 35 A 555 THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS
SEQRES 36 A 555 LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN
SEQRES 37 A 555 MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY
SEQRES 38 A 555 ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU
SEQRES 39 A 555 LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET
SEQRES 40 A 555 GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU
SEQRES 41 A 555 ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU
SEQRES 42 A 555 VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA
SEQRES 43 A 555 ARG ASN PRO PRO VAL VAL SER LYS MET
HET PO4 A 601 5
HET MG A 602 1
HET BXV A 603 31
HET CL A 604 1
HET CL A 605 1
HET CL A 606 1
HETNAM PO4 PHOSPHATE ION
HETNAM MG MAGNESIUM ION
HETNAM BXV 4-{[TRANS-4-({[4-(TRIFLUOROMETHOXY)
HETNAM 2 BXV PHENYL]CARBAMOYL}AMINO)CYCLOHEXYL]OXY}BENZOIC ACID
HETNAM CL CHLORIDE ION
FORMUL 2 PO4 O4 P 3-
FORMUL 3 MG MG 2+
FORMUL 4 BXV C21 H21 F3 N2 O5
FORMUL 5 CL 3(CL 1-)
FORMUL 8 HOH *25(H2 O)
HELIX 1 AA1 VAL A 19 ALA A 31 1 13
HELIX 2 AA2 GLY A 35 LYS A 43 1 9
HELIX 3 AA3 GLY A 44 GLU A 47 5 4
HELIX 4 AA4 GLY A 48 GLY A 56 1 9
HELIX 5 AA5 THR A 59 ALA A 78 1 20
HELIX 6 AA6 SER A 87 ARG A 99 1 13
HELIX 7 AA7 ASN A 102 LYS A 115 1 14
HELIX 8 AA8 ARG A 133 MET A 145 1 13
HELIX 9 AA9 SER A 153 GLY A 157 1 5
HELIX 10 AB1 GLU A 162 LYS A 174 1 13
HELIX 11 AB2 SER A 176 SER A 178 5 3
HELIX 12 AB3 ILE A 186 ASN A 189 5 4
HELIX 13 AB4 LEU A 190 LEU A 196 1 7
HELIX 14 AB5 ASP A 205 GLY A 218 1 14
HELIX 15 AB6 ASN A 233 MET A 237 5 5
HELIX 16 AB7 SER A 270 ARG A 275 5 6
HELIX 17 AB8 GLN A 277 TYR A 286 1 10
HELIX 18 AB9 GLU A 304 TYR A 308 5 5
HELIX 19 AC1 CYS A 309 LEU A 324 1 16
HELIX 20 AC2 ASP A 335 TYR A 348 1 14
HELIX 21 AC3 SER A 370 ALA A 377 1 8
HELIX 22 AC4 ASN A 378 VAL A 380 5 3
HELIX 23 AC5 PHE A 381 PHE A 387 1 7
HELIX 24 AC6 GLY A 391 ASN A 400 1 10
HELIX 25 AC7 ASN A 400 PHE A 409 1 10
HELIX 26 AC8 ALA A 411 SER A 415 5 5
HELIX 27 AC9 LYS A 421 GLY A 426 1 6
HELIX 28 AD1 THR A 443 GLY A 458 1 16
HELIX 29 AD2 PHE A 459 TRP A 465 1 7
HELIX 30 AD3 ASN A 468 CYS A 477 1 10
HELIX 31 AD4 LYS A 478 LEU A 480 5 3
HELIX 32 AD5 VAL A 500 GLN A 505 5 6
HELIX 33 AD6 HIS A 506 ILE A 511 1 6
HELIX 34 AD7 TRP A 525 LYS A 530 1 6
HELIX 35 AD8 LYS A 530 ALA A 546 1 17
SHEET 1 AA1 5 PHE A 149 GLU A 152 0
SHEET 2 AA1 5 THR A 118 THR A 123 1 N ILE A 121 O ILE A 151
SHEET 3 AA1 5 ALA A 5 PHE A 8 1 N PHE A 8 O ALA A 120
SHEET 4 AA1 5 VAL A 180 ASP A 184 1 O VAL A 181 N VAL A 7
SHEET 5 AA1 5 VAL A 199 LEU A 202 1 O VAL A 199 N VAL A 180
SHEET 1 AA2 2 ALA A 15 LEU A 16 0
SHEET 2 AA2 2 LYS A 100 ILE A 101 -1 O LYS A 100 N LEU A 16
SHEET 1 AA3 8 SER A 238 LYS A 245 0
SHEET 2 AA3 8 VAL A 248 LEU A 255 -1 O LEU A 250 N VAL A 242
SHEET 3 AA3 8 ARG A 287 MET A 291 -1 O ALA A 290 N VAL A 253
SHEET 4 AA3 8 ALA A 260 CYS A 264 1 N VAL A 261 O LEU A 289
SHEET 5 AA3 8 ALA A 329 HIS A 334 1 O VAL A 330 N CYS A 262
SHEET 6 AA3 8 VAL A 352 LEU A 358 1 O ALA A 356 N GLY A 333
SHEET 7 AA3 8 ALA A 488 ALA A 493 1 O VAL A 491 N SER A 357
SHEET 8 AA3 8 LYS A 515 ILE A 519 1 O LYS A 515 N ALA A 488
LINK OD2 ASP A 9 MG MG A 602 1555 1555 1.91
LINK O ASP A 11 MG MG A 602 1555 1555 2.18
LINK OD1 ASP A 185 MG MG A 602 1555 1555 1.93
LINK O1 PO4 A 601 MG MG A 602 1555 1555 1.94
LINK MG MG A 602 O HOH A 702 1555 1555 1.92
LINK MG MG A 602 O HOH A 701 1555 1555 1.91
CISPEP 1 LEU A 16 PRO A 17 0 -8.91
CISPEP 2 LYS A 160 PRO A 161 0 7.79
CISPEP 3 PHE A 267 PRO A 268 0 -16.59
SITE 1 AC1 9 ASP A 9 LEU A 10 ASP A 11 THR A 123
SITE 2 AC1 9 ASN A 124 LYS A 160 MG A 602 HOH A 701
SITE 3 AC1 9 HOH A 702
SITE 1 AC2 6 ASP A 9 ASP A 11 ASP A 185 PO4 A 601
SITE 2 AC2 6 HOH A 701 HOH A 702
SITE 1 AC3 12 PHE A 267 ASP A 335 TRP A 336 MET A 339
SITE 2 AC3 12 SER A 374 ILE A 375 TYR A 383 GLN A 384
SITE 3 AC3 12 LEU A 408 MET A 419 LEU A 428 TYR A 466
SITE 1 AC4 1 MET A 419
SITE 1 AC5 2 LYS A 144 PHE A 147
CRYST1 92.713 92.713 243.736 90.00 90.00 120.00 P 65 2 2 12
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 0.010786 0.006227 0.000000 0.00000
SCALE2 0.000000 0.012455 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004103 0.00000
TER 4344 ASN A 548
MASTER 540 0 6 35 15 0 10 6 4396 1 43 43
END |