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HEADER HYDROLASE 12-NOV-22 8HFW
TITLE THE CRYSTAL STRUCTURE OF ALPHA/BETA FOLD HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA FOLD HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PYRROCINIA;
SOURCE 3 ORGANISM_COMMON: PSEUDOMONAS PYRROCINIA;
SOURCE 4 ORGANISM_TAXID: 60550;
SOURCE 5 GENE: EVG18_06755;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ESTER SYNTHETASE, CARBOXYLESTERASE, SMALL MOLECULE FATTY ACID
KEYWDS 2 ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LU,Y.XU
REVDAT 1 24-MAY-23 8HFW 0
JRNL AUTH H.LU,Y.XU
JRNL TITL THE CRYSTAL STRUCTURE OF ALPHA/BETA FOLD HYDROLASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0352
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 98506
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.992
REMARK 3 FREE R VALUE TEST SET COUNT : 4917
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) : 1.66
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6724
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 350
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5977
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 329
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.22700
REMARK 3 B22 (A**2) : -0.98300
REMARK 3 B33 (A**2) : 0.67900
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.57800
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.136
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.078
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.215
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6144 ; 0.008 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 5350 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8380 ; 1.478 ; 1.643
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12361 ; 0.449 ; 1.564
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 846 ; 5.379 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 31 ; 3.461 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 701 ;14.840 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 920 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7280 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1226 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1407 ; 0.229 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 39 ; 0.129 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3084 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 227 ; 0.109 ; 0.200
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): 3375 ; 2.732 ; 1.467
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3375 ; 2.732 ; 1.467
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4206 ; 3.322 ; 2.203
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4207 ; 3.322 ; 2.203
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2769 ; 3.268 ; 1.624
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2770 ; 3.268 ; 1.624
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4169 ; 3.753 ; 2.363
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4170 ; 3.753 ; 2.363
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 11494 ; 5.374 ; 3.000
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 : 3
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 13 A 297
REMARK 3 ORIGIN FOR THE GROUP (A): 32.2730 -0.3538 33.0472
REMARK 3 T TENSOR
REMARK 3 T11: 0.0037 T22: 0.0445
REMARK 3 T33: 0.0052 T12: 0.0007
REMARK 3 T13: -0.0004 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 1.1097 L22: 1.4567
REMARK 3 L33: 1.0953 L12: -0.1455
REMARK 3 L13: 0.4669 L23: 0.1449
REMARK 3 S TENSOR
REMARK 3 S11: 0.0167 S12: -0.0145 S13: -0.0685
REMARK 3 S21: 0.0489 S22: 0.0304 S23: 0.0246
REMARK 3 S31: -0.0106 S32: -0.0108 S33: -0.0471
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9184 2.1220 3.0456
REMARK 3 T TENSOR
REMARK 3 T11: 0.2118 T22: 0.1507
REMARK 3 T33: 0.0208 T12: 0.0380
REMARK 3 T13: -0.0493 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 1.5548 L22: 1.3685
REMARK 3 L33: 2.7571 L12: -0.3278
REMARK 3 L13: -0.9805 L23: 0.2873
REMARK 3 S TENSOR
REMARK 3 S11: 0.1508 S12: 0.2540 S13: -0.0790
REMARK 3 S21: -0.3838 S22: -0.1009 S23: 0.0717
REMARK 3 S31: -0.1958 S32: -0.0201 S33: -0.0499
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2193 25.7536 23.1714
REMARK 3 T TENSOR
REMARK 3 T11: 0.1858 T22: 0.1817
REMARK 3 T33: 0.1855 T12: 0.0605
REMARK 3 T13: -0.0185 T23: 0.0629
REMARK 3 L TENSOR
REMARK 3 L11: 1.6398 L22: 1.1887
REMARK 3 L33: 1.8353 L12: 0.1201
REMARK 3 L13: -0.3320 L23: -0.0070
REMARK 3 S TENSOR
REMARK 3 S11: 0.0325 S12: 0.3239 S13: 0.3227
REMARK 3 S21: -0.2133 S22: -0.0315 S23: 0.0505
REMARK 3 S31: -0.4520 S32: -0.1330 S33: -0.0010
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 8HFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 15-NOV-22.
REMARK 100 THE DEPOSITION ID IS D_1300033400.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-21
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.0-7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL02U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 98523
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 57.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 6.370
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.46600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 5Y57
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, PH7.2, 0.2 M MAGNESIUM
REMARK 280 ACETATE, 17% PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 83.48000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.20500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 83.48000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.20500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -4.69783
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 75.19339
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 GLU A 2
REMARK 465 THR A 3
REMARK 465 ASN A 4
REMARK 465 VAL A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 PRO A 10
REMARK 465 SER A 11
REMARK 465 ASP A 12
REMARK 465 GLU A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 THR B 3
REMARK 465 ASN B 4
REMARK 465 VAL B 5
REMARK 465 THR B 6
REMARK 465 ALA B 7
REMARK 465 ALA B 8
REMARK 465 ALA B 9
REMARK 465 PRO B 10
REMARK 465 SER B 11
REMARK 465 ASP B 12
REMARK 465 ARG B 150
REMARK 465 PRO B 167
REMARK 465 ILE B 295
REMARK 465 ALA B 296
REMARK 465 LEU B 297
REMARK 465 GLU B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 HIS B 304
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 THR C 3
REMARK 465 ASN C 4
REMARK 465 VAL C 5
REMARK 465 THR C 6
REMARK 465 ALA C 7
REMARK 465 ALA C 8
REMARK 465 ALA C 9
REMARK 465 PRO C 10
REMARK 465 SER C 11
REMARK 465 ASP C 12
REMARK 465 ALA C 226
REMARK 465 ILE C 295
REMARK 465 ALA C 296
REMARK 465 LEU C 297
REMARK 465 GLU C 298
REMARK 465 HIS C 299
REMARK 465 HIS C 300
REMARK 465 HIS C 301
REMARK 465 HIS C 302
REMARK 465 HIS C 303
REMARK 465 HIS C 304
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 GLU A 38 CG CD OE1 OE2
REMARK 470 LEU A 42 CD1
REMARK 470 ILE A 53 CD1
REMARK 470 LEU A 62 CD2
REMARK 470 GLU A 63 CG CD OE1 OE2
REMARK 470 PRO A 65 CB CG
REMARK 470 LEU A 66 CD1 CD2
REMARK 470 LYS A 68 CG CD CE NZ
REMARK 470 ASP A 69 OD2
REMARK 470 THR A 88 CG2
REMARK 470 LEU A 100 O CD1 CD2
REMARK 470 HIS A 102 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 131 CD1
REMARK 470 LYS A 155 CE NZ
REMARK 470 LEU A 159 CD1 CD2
REMARK 470 ALA A 160 CB
REMARK 470 ARG A 168 CG CD NE CZ NH1 NH2
REMARK 470 MET A 204 CE
REMARK 470 VAL A 260 CG1 CG2
REMARK 470 ASP A 271 OD1 OD2
REMARK 470 LYS A 293 CE NZ
REMARK 470 ILE A 295 CG1 CD1
REMARK 470 ALA A 296 CB
REMARK 470 LEU A 297 CA C O CB CG CD1 CD2
REMARK 470 HIS B 13 CD2 CE1 NE2
REMARK 470 VAL B 15 CG1
REMARK 470 GLU B 38 CG CD OE1 OE2
REMARK 470 ARG B 39 NH1
REMARK 470 LEU B 42 CD1 CD2
REMARK 470 ILE B 53 CD1
REMARK 470 PRO B 65 CG CD
REMARK 470 LYS B 68 CG CD CE NZ
REMARK 470 ASP B 69 CG OD1 OD2
REMARK 470 ASN B 80 ND2
REMARK 470 THR B 88 CG2
REMARK 470 MET B 91 CE
REMARK 470 LEU B 100 CD1 CD2
REMARK 470 GLY B 101 CA O
REMARK 470 HIS B 102 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 104 CE NZ
REMARK 470 GLU B 122 CB CG CD OE1 OE2
REMARK 470 ARG B 123 NH1 NH2
REMARK 470 ILE B 131 CD1
REMARK 470 LEU B 146 CD1 CD2
REMARK 470 VAL B 149 CG1 CG2
REMARK 470 ALA B 151 CB
REMARK 470 LYS B 155 CG CD CE NZ
REMARK 470 GLU B 157 CB CG CD OE1 OE2
REMARK 470 LEU B 159 CB CG CD1 CD2
REMARK 470 ALA B 160 CB
REMARK 470 LEU B 162 CD1 CD2
REMARK 470 MET B 163 CE
REMARK 470 ARG B 168 O CB CG CD NE CZ NH1
REMARK 470 ARG B 168 NH2
REMARK 470 VAL B 169 CG1 CG2
REMARK 470 LEU B 173 CD1 CD2
REMARK 470 ILE B 175 CG2
REMARK 470 ARG B 178 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 181 OD2
REMARK 470 ALA B 182 CB
REMARK 470 ARG B 185 NH1 NH2
REMARK 470 LEU B 187 CD2
REMARK 470 ARG B 190 CD NE CZ NH1 NH2
REMARK 470 LEU B 192 CD1
REMARK 470 GLU B 202 OE1 OE2
REMARK 470 MET B 204 CE
REMARK 470 VAL B 212 CG1
REMARK 470 ALA B 225 CB
REMARK 470 ALA B 226 CB
REMARK 470 ARG B 227 CB CG CD NE CZ NH1 NH2
REMARK 470 ASP B 232 OD1
REMARK 470 VAL B 243 CG1
REMARK 470 VAL B 260 CB CG1 CG2
REMARK 470 PRO B 261 CB CG
REMARK 470 ASP B 271 OD1 OD2
REMARK 470 VAL B 289 CG1 CG2
REMARK 470 LYS B 293 CE NZ
REMARK 470 HIS C 13 N
REMARK 470 VAL C 15 CG1 CG2
REMARK 470 PHE C 16 CD1
REMARK 470 GLU C 38 CG CD OE1 OE2
REMARK 470 LEU C 42 CD1 CD2
REMARK 470 ILE C 44 CD1
REMARK 470 GLU C 63 OE1 OE2
REMARK 470 LYS C 68 NZ
REMARK 470 ASP C 69 OD2
REMARK 470 ASP C 84 OD2
REMARK 470 THR C 88 CG2
REMARK 470 MET C 91 CG SD CE
REMARK 470 GLU C 92 CG CD OE1 OE2
REMARK 470 TYR C 98 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU C 100 CG CD1 CD2
REMARK 470 HIS C 102 CG ND1 CD2 CE1 NE2
REMARK 470 GLY C 103 O
REMARK 470 LYS C 104 NZ
REMARK 470 VAL C 105 CG1
REMARK 470 VAL C 106 CG2
REMARK 470 LEU C 107 CD1 CD2
REMARK 470 ALA C 121 CB
REMARK 470 GLU C 122 OE2
REMARK 470 ARG C 123 CB CG CD NE CZ NH1 NH2
REMARK 470 PRO C 125 CB
REMARK 470 GLU C 126 CB CG CD OE1 OE2
REMARK 470 LYS C 127 CG CD CE NZ
REMARK 470 ALA C 129 CB
REMARK 470 LYS C 130 CB CG CD CE NZ
REMARK 470 ILE C 131 CD1
REMARK 470 VAL C 132 CG1 CG2
REMARK 470 LEU C 134 CD1 CD2
REMARK 470 VAL C 149 CG1
REMARK 470 LYS C 155 CG CD CE NZ
REMARK 470 GLU C 157 CG CD OE1 OE2
REMARK 470 LEU C 159 CD1 CD2
REMARK 470 ALA C 160 CB
REMARK 470 ARG C 168 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 173 CD1 CD2
REMARK 470 ARG C 178 CZ NH1 NH2
REMARK 470 LEU C 187 CD1
REMARK 470 GLU C 202 OE1 OE2
REMARK 470 MET C 204 CE
REMARK 470 ILE C 221 CD1
REMARK 470 PRO C 222 CD
REMARK 470 THR C 223 CG2
REMARK 470 THR C 224 CB OG1 CG2
REMARK 470 ALA C 225 CB
REMARK 470 ARG C 227 CD NE CZ NH1 NH2
REMARK 470 TRP C 228 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 228 CZ3 CH2
REMARK 470 ALA C 230 O CB
REMARK 470 ILE C 231 CB CG1 CG2 CD1
REMARK 470 ASP C 232 CB CG OD1 OD2
REMARK 470 ARG C 233 NE CZ NH1 NH2
REMARK 470 ARG C 242 CZ NH1 NH2
REMARK 470 ILE C 244 CD1
REMARK 470 LEU C 245 CD1
REMARK 470 ALA C 256 CB
REMARK 470 ASP C 257 CB CG OD1 OD2
REMARK 470 PHE C 259 CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL C 260 CG1 CG2
REMARK 470 PRO C 261 CG CD
REMARK 470 ASN C 263 CG OD1 ND2
REMARK 470 PRO C 264 CG
REMARK 470 THR C 265 CG2
REMARK 470 VAL C 267 CG1 CG2
REMARK 470 GLN C 269 NE2
REMARK 470 LEU C 270 CD1
REMARK 470 VAL C 283 CG1
REMARK 470 VAL C 289 CG1 CG2
REMARK 470 LYS C 293 NZ
REMARK 470 SER C 294 OG
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 233 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 233 NE - CZ - NH2 ANGL. DEV. = -3.6 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 SER A 111 -127.53 54.77
REMARK 500 TYR A 193 41.56 -143.44
REMARK 500 ARG A 227 -84.39 -108.04
REMARK 500 SER A 273 -172.98 -69.20
REMARK 500 SER A 275 63.90 -118.88
REMARK 500 GLN A 280 57.03 -146.94
REMARK 500 TRP B 23 -0.39 71.20
REMARK 500 SER B 111 -125.12 58.02
REMARK 500 ALA B 124 77.55 -157.44
REMARK 500 TYR B 193 38.51 -144.41
REMARK 500 ARG B 227 -83.38 -100.94
REMARK 500 SER B 275 64.31 -117.38
REMARK 500 SER C 111 -126.04 52.47
REMARK 500 ALA C 124 85.61 -164.70
REMARK 500 TYR C 193 39.36 -145.36
REMARK 500 SER C 273 -176.54 -68.64
REMARK 500 SER C 275 69.80 -118.41
REMARK 500 GLN C 280 47.86 -143.74
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 A 567 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH C 482 DISTANCE = 6.51 ANGSTROMS
DBREF1 8HFW A 1 294 UNP A0A4V2WUI0_BURPY
DBREF2 8HFW A A0A4V2WUI0 1 294
DBREF1 8HFW B 1 294 UNP A0A4V2WUI0_BURPY
DBREF2 8HFW B A0A4V2WUI0 1 294
DBREF1 8HFW C 1 294 UNP A0A4V2WUI0_BURPY
DBREF2 8HFW C A0A4V2WUI0 1 294
SEQADV 8HFW VAL A 5 UNP A0A4V2WUI ILE 5 CONFLICT
SEQADV 8HFW ALA A 8 UNP A0A4V2WUI PRO 8 CONFLICT
SEQADV 8HFW ALA A 9 UNP A0A4V2WUI GLN 9 CONFLICT
SEQADV 8HFW PRO A 10 UNP A0A4V2WUI GLN 10 CONFLICT
SEQADV 8HFW SER A 11 UNP A0A4V2WUI ALA 11 CONFLICT
SEQADV 8HFW GLU A 38 UNP A0A4V2WUI ALA 38 CONFLICT
SEQADV 8HFW GLU A 92 UNP A0A4V2WUI GLN 92 CONFLICT
SEQADV 8HFW HIS A 102 UNP A0A4V2WUI ARG 102 CONFLICT
SEQADV 8HFW ALA A 160 UNP A0A4V2WUI GLY 160 CONFLICT
SEQADV 8HFW PRO A 161 UNP A0A4V2WUI ALA 161 CONFLICT
SEQADV 8HFW ALA A 186 UNP A0A4V2WUI ASP 186 CONFLICT
SEQADV 8HFW LEU A 187 UNP A0A4V2WUI THR 187 CONFLICT
SEQADV 8HFW ALA A 188 UNP A0A4V2WUI MET 188 CONFLICT
SEQADV 8HFW ALA A 197 UNP A0A4V2WUI PRO 197 CONFLICT
SEQADV 8HFW MET A 204 UNP A0A4V2WUI VAL 204 CONFLICT
SEQADV 8HFW MET A 208 UNP A0A4V2WUI LEU 208 CONFLICT
SEQADV 8HFW THR A 219 UNP A0A4V2WUI SER 219 CONFLICT
SEQADV 8HFW ALA A 226 UNP A0A4V2WUI VAL 226 CONFLICT
SEQADV 8HFW ALA A 240 UNP A0A4V2WUI GLN 240 CONFLICT
SEQADV 8HFW VAL A 260 UNP A0A4V2WUI ALA 260 CONFLICT
SEQADV 8HFW GLN A 280 UNP A0A4V2WUI GLU 280 CONFLICT
SEQADV 8HFW PRO A 281 UNP A0A4V2WUI ALA 281 CONFLICT
SEQADV 8HFW GLY A 282 UNP A0A4V2WUI ALA 282 CONFLICT
SEQADV 8HFW VAL A 289 UNP A0A4V2WUI ALA 289 CONFLICT
SEQADV 8HFW ILE A 295 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW ALA A 296 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW LEU A 297 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW GLU A 298 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS A 299 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS A 300 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS A 301 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS A 302 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS A 303 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS A 304 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW VAL B 5 UNP A0A4V2WUI ILE 5 CONFLICT
SEQADV 8HFW ALA B 8 UNP A0A4V2WUI PRO 8 CONFLICT
SEQADV 8HFW ALA B 9 UNP A0A4V2WUI GLN 9 CONFLICT
SEQADV 8HFW PRO B 10 UNP A0A4V2WUI GLN 10 CONFLICT
SEQADV 8HFW SER B 11 UNP A0A4V2WUI ALA 11 CONFLICT
SEQADV 8HFW GLU B 38 UNP A0A4V2WUI ALA 38 CONFLICT
SEQADV 8HFW GLU B 92 UNP A0A4V2WUI GLN 92 CONFLICT
SEQADV 8HFW HIS B 102 UNP A0A4V2WUI ARG 102 CONFLICT
SEQADV 8HFW ALA B 160 UNP A0A4V2WUI GLY 160 CONFLICT
SEQADV 8HFW PRO B 161 UNP A0A4V2WUI ALA 161 CONFLICT
SEQADV 8HFW ALA B 186 UNP A0A4V2WUI ASP 186 CONFLICT
SEQADV 8HFW LEU B 187 UNP A0A4V2WUI THR 187 CONFLICT
SEQADV 8HFW ALA B 188 UNP A0A4V2WUI MET 188 CONFLICT
SEQADV 8HFW ALA B 197 UNP A0A4V2WUI PRO 197 CONFLICT
SEQADV 8HFW MET B 204 UNP A0A4V2WUI VAL 204 CONFLICT
SEQADV 8HFW MET B 208 UNP A0A4V2WUI LEU 208 CONFLICT
SEQADV 8HFW THR B 219 UNP A0A4V2WUI SER 219 CONFLICT
SEQADV 8HFW ALA B 226 UNP A0A4V2WUI VAL 226 CONFLICT
SEQADV 8HFW ALA B 240 UNP A0A4V2WUI GLN 240 CONFLICT
SEQADV 8HFW VAL B 260 UNP A0A4V2WUI ALA 260 CONFLICT
SEQADV 8HFW GLN B 280 UNP A0A4V2WUI GLU 280 CONFLICT
SEQADV 8HFW PRO B 281 UNP A0A4V2WUI ALA 281 CONFLICT
SEQADV 8HFW GLY B 282 UNP A0A4V2WUI ALA 282 CONFLICT
SEQADV 8HFW VAL B 289 UNP A0A4V2WUI ALA 289 CONFLICT
SEQADV 8HFW ILE B 295 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW ALA B 296 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW LEU B 297 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW GLU B 298 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS B 299 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS B 300 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS B 301 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS B 302 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS B 303 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS B 304 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW VAL C 5 UNP A0A4V2WUI ILE 5 CONFLICT
SEQADV 8HFW ALA C 8 UNP A0A4V2WUI PRO 8 CONFLICT
SEQADV 8HFW ALA C 9 UNP A0A4V2WUI GLN 9 CONFLICT
SEQADV 8HFW PRO C 10 UNP A0A4V2WUI GLN 10 CONFLICT
SEQADV 8HFW SER C 11 UNP A0A4V2WUI ALA 11 CONFLICT
SEQADV 8HFW GLU C 38 UNP A0A4V2WUI ALA 38 CONFLICT
SEQADV 8HFW GLU C 92 UNP A0A4V2WUI GLN 92 CONFLICT
SEQADV 8HFW HIS C 102 UNP A0A4V2WUI ARG 102 CONFLICT
SEQADV 8HFW ALA C 160 UNP A0A4V2WUI GLY 160 CONFLICT
SEQADV 8HFW PRO C 161 UNP A0A4V2WUI ALA 161 CONFLICT
SEQADV 8HFW ALA C 186 UNP A0A4V2WUI ASP 186 CONFLICT
SEQADV 8HFW LEU C 187 UNP A0A4V2WUI THR 187 CONFLICT
SEQADV 8HFW ALA C 188 UNP A0A4V2WUI MET 188 CONFLICT
SEQADV 8HFW ALA C 197 UNP A0A4V2WUI PRO 197 CONFLICT
SEQADV 8HFW MET C 204 UNP A0A4V2WUI VAL 204 CONFLICT
SEQADV 8HFW MET C 208 UNP A0A4V2WUI LEU 208 CONFLICT
SEQADV 8HFW THR C 219 UNP A0A4V2WUI SER 219 CONFLICT
SEQADV 8HFW ALA C 226 UNP A0A4V2WUI VAL 226 CONFLICT
SEQADV 8HFW ALA C 240 UNP A0A4V2WUI GLN 240 CONFLICT
SEQADV 8HFW VAL C 260 UNP A0A4V2WUI ALA 260 CONFLICT
SEQADV 8HFW GLN C 280 UNP A0A4V2WUI GLU 280 CONFLICT
SEQADV 8HFW PRO C 281 UNP A0A4V2WUI ALA 281 CONFLICT
SEQADV 8HFW GLY C 282 UNP A0A4V2WUI ALA 282 CONFLICT
SEQADV 8HFW VAL C 289 UNP A0A4V2WUI ALA 289 CONFLICT
SEQADV 8HFW ILE C 295 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW ALA C 296 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW LEU C 297 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW GLU C 298 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS C 299 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS C 300 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS C 301 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS C 302 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS C 303 UNP A0A4V2WUI EXPRESSION TAG
SEQADV 8HFW HIS C 304 UNP A0A4V2WUI EXPRESSION TAG
SEQRES 1 A 304 MET GLU THR ASN VAL THR ALA ALA ALA PRO SER ASP HIS
SEQRES 2 A 304 PRO VAL PHE VAL LEU VAL HIS GLY ALA TRP HIS GLY ALA
SEQRES 3 A 304 TRP CYS TYR ALA HIS VAL ALA ALA ALA LEU ALA GLU ARG
SEQRES 4 A 304 GLY TYR LEU SER ILE ALA ARG ASP LEU PRO ALA HIS GLY
SEQRES 5 A 304 ILE ASN ALA ARG PHE PRO ALA SER TYR LEU GLU ARG PRO
SEQRES 6 A 304 LEU ASP LYS ASP ALA PHE GLY ALA GLU PRO SER PRO VAL
SEQRES 7 A 304 ALA ASN THR THR LEU ASP ASP TYR ALA THR GLN VAL MET
SEQRES 8 A 304 GLU ALA VAL ASP ASP ALA TYR ALA LEU GLY HIS GLY LYS
SEQRES 9 A 304 VAL VAL LEU VAL GLY HIS SER MET GLY GLY LEU ALA ILE
SEQRES 10 A 304 THR ALA ALA ALA GLU ARG ALA PRO GLU LYS ILE ALA LYS
SEQRES 11 A 304 ILE VAL TYR LEU ALA ALA PHE MET PRO ALA SER GLY VAL
SEQRES 12 A 304 PRO GLY LEU ASP TYR VAL ARG ALA PRO GLU ASN LYS GLY
SEQRES 13 A 304 GLU MET LEU ALA PRO LEU MET LEU ALA SER PRO ARG VAL
SEQRES 14 A 304 ALA GLY ALA LEU ARG ILE ASP PRO ARG SER GLY ASP ALA
SEQRES 15 A 304 ALA TYR ARG ALA LEU ALA LYS ARG ALA LEU TYR ASP ASP
SEQRES 16 A 304 ALA ALA GLN ALA ASP PHE GLU ALA MET ALA ASN LEU MET
SEQRES 17 A 304 THR CYS ASP VAL PRO ALA ALA PRO PHE ALA THR ALA ILE
SEQRES 18 A 304 PRO THR THR ALA ALA ARG TRP GLY ALA ILE ASP ARG HIS
SEQRES 19 A 304 TYR ILE LYS CYS LEU ALA ASP ARG VAL ILE LEU PRO ALA
SEQRES 20 A 304 LEU GLN GLN ARG PHE ILE ASP GLU ALA ASP ALA PHE VAL
SEQRES 21 A 304 PRO GLY ASN PRO THR HIS VAL HIS GLN LEU ASP SER SER
SEQRES 22 A 304 HIS SER PRO PHE VAL SER GLN PRO GLY VAL LEU ALA GLY
SEQRES 23 A 304 VAL LEU VAL ASP ILE ALA LYS SER ILE ALA LEU GLU HIS
SEQRES 24 A 304 HIS HIS HIS HIS HIS
SEQRES 1 B 304 MET GLU THR ASN VAL THR ALA ALA ALA PRO SER ASP HIS
SEQRES 2 B 304 PRO VAL PHE VAL LEU VAL HIS GLY ALA TRP HIS GLY ALA
SEQRES 3 B 304 TRP CYS TYR ALA HIS VAL ALA ALA ALA LEU ALA GLU ARG
SEQRES 4 B 304 GLY TYR LEU SER ILE ALA ARG ASP LEU PRO ALA HIS GLY
SEQRES 5 B 304 ILE ASN ALA ARG PHE PRO ALA SER TYR LEU GLU ARG PRO
SEQRES 6 B 304 LEU ASP LYS ASP ALA PHE GLY ALA GLU PRO SER PRO VAL
SEQRES 7 B 304 ALA ASN THR THR LEU ASP ASP TYR ALA THR GLN VAL MET
SEQRES 8 B 304 GLU ALA VAL ASP ASP ALA TYR ALA LEU GLY HIS GLY LYS
SEQRES 9 B 304 VAL VAL LEU VAL GLY HIS SER MET GLY GLY LEU ALA ILE
SEQRES 10 B 304 THR ALA ALA ALA GLU ARG ALA PRO GLU LYS ILE ALA LYS
SEQRES 11 B 304 ILE VAL TYR LEU ALA ALA PHE MET PRO ALA SER GLY VAL
SEQRES 12 B 304 PRO GLY LEU ASP TYR VAL ARG ALA PRO GLU ASN LYS GLY
SEQRES 13 B 304 GLU MET LEU ALA PRO LEU MET LEU ALA SER PRO ARG VAL
SEQRES 14 B 304 ALA GLY ALA LEU ARG ILE ASP PRO ARG SER GLY ASP ALA
SEQRES 15 B 304 ALA TYR ARG ALA LEU ALA LYS ARG ALA LEU TYR ASP ASP
SEQRES 16 B 304 ALA ALA GLN ALA ASP PHE GLU ALA MET ALA ASN LEU MET
SEQRES 17 B 304 THR CYS ASP VAL PRO ALA ALA PRO PHE ALA THR ALA ILE
SEQRES 18 B 304 PRO THR THR ALA ALA ARG TRP GLY ALA ILE ASP ARG HIS
SEQRES 19 B 304 TYR ILE LYS CYS LEU ALA ASP ARG VAL ILE LEU PRO ALA
SEQRES 20 B 304 LEU GLN GLN ARG PHE ILE ASP GLU ALA ASP ALA PHE VAL
SEQRES 21 B 304 PRO GLY ASN PRO THR HIS VAL HIS GLN LEU ASP SER SER
SEQRES 22 B 304 HIS SER PRO PHE VAL SER GLN PRO GLY VAL LEU ALA GLY
SEQRES 23 B 304 VAL LEU VAL ASP ILE ALA LYS SER ILE ALA LEU GLU HIS
SEQRES 24 B 304 HIS HIS HIS HIS HIS
SEQRES 1 C 304 MET GLU THR ASN VAL THR ALA ALA ALA PRO SER ASP HIS
SEQRES 2 C 304 PRO VAL PHE VAL LEU VAL HIS GLY ALA TRP HIS GLY ALA
SEQRES 3 C 304 TRP CYS TYR ALA HIS VAL ALA ALA ALA LEU ALA GLU ARG
SEQRES 4 C 304 GLY TYR LEU SER ILE ALA ARG ASP LEU PRO ALA HIS GLY
SEQRES 5 C 304 ILE ASN ALA ARG PHE PRO ALA SER TYR LEU GLU ARG PRO
SEQRES 6 C 304 LEU ASP LYS ASP ALA PHE GLY ALA GLU PRO SER PRO VAL
SEQRES 7 C 304 ALA ASN THR THR LEU ASP ASP TYR ALA THR GLN VAL MET
SEQRES 8 C 304 GLU ALA VAL ASP ASP ALA TYR ALA LEU GLY HIS GLY LYS
SEQRES 9 C 304 VAL VAL LEU VAL GLY HIS SER MET GLY GLY LEU ALA ILE
SEQRES 10 C 304 THR ALA ALA ALA GLU ARG ALA PRO GLU LYS ILE ALA LYS
SEQRES 11 C 304 ILE VAL TYR LEU ALA ALA PHE MET PRO ALA SER GLY VAL
SEQRES 12 C 304 PRO GLY LEU ASP TYR VAL ARG ALA PRO GLU ASN LYS GLY
SEQRES 13 C 304 GLU MET LEU ALA PRO LEU MET LEU ALA SER PRO ARG VAL
SEQRES 14 C 304 ALA GLY ALA LEU ARG ILE ASP PRO ARG SER GLY ASP ALA
SEQRES 15 C 304 ALA TYR ARG ALA LEU ALA LYS ARG ALA LEU TYR ASP ASP
SEQRES 16 C 304 ALA ALA GLN ALA ASP PHE GLU ALA MET ALA ASN LEU MET
SEQRES 17 C 304 THR CYS ASP VAL PRO ALA ALA PRO PHE ALA THR ALA ILE
SEQRES 18 C 304 PRO THR THR ALA ALA ARG TRP GLY ALA ILE ASP ARG HIS
SEQRES 19 C 304 TYR ILE LYS CYS LEU ALA ASP ARG VAL ILE LEU PRO ALA
SEQRES 20 C 304 LEU GLN GLN ARG PHE ILE ASP GLU ALA ASP ALA PHE VAL
SEQRES 21 C 304 PRO GLY ASN PRO THR HIS VAL HIS GLN LEU ASP SER SER
SEQRES 22 C 304 HIS SER PRO PHE VAL SER GLN PRO GLY VAL LEU ALA GLY
SEQRES 23 C 304 VAL LEU VAL ASP ILE ALA LYS SER ILE ALA LEU GLU HIS
SEQRES 24 C 304 HIS HIS HIS HIS HIS
FORMUL 4 HOH *329(H2 O)
HELIX 1 AA1 GLY A 25 CYS A 28 5 4
HELIX 2 AA2 TYR A 29 ARG A 39 1 11
HELIX 3 AA3 HIS A 51 ALA A 55 5 5
HELIX 4 AA4 PRO A 58 LEU A 62 5 5
HELIX 5 AA5 ASP A 67 GLU A 74 1 8
HELIX 6 AA6 THR A 82 LEU A 100 1 19
HELIX 7 AA7 MET A 112 ALA A 124 1 13
HELIX 8 AA8 PRO A 144 ARG A 150 1 7
HELIX 9 AA9 ALA A 151 LYS A 155 5 5
HELIX 10 AB1 LEU A 159 MET A 163 5 5
HELIX 11 AB2 SER A 166 GLY A 171 1 6
HELIX 12 AB3 ASP A 181 TYR A 193 1 13
HELIX 13 AB4 ALA A 197 MET A 208 1 12
HELIX 14 AB5 ALA A 215 THR A 219 5 5
HELIX 15 AB6 ARG A 227 ILE A 231 5 5
HELIX 16 AB7 LEU A 245 VAL A 260 1 16
HELIX 17 AB8 SER A 275 GLN A 280 1 6
HELIX 18 AB9 GLN A 280 SER A 294 1 15
HELIX 19 AC1 GLY B 25 CYS B 28 5 4
HELIX 20 AC2 TYR B 29 ARG B 39 1 11
HELIX 21 AC3 HIS B 51 ALA B 55 5 5
HELIX 22 AC4 PRO B 58 GLU B 63 5 6
HELIX 23 AC5 ASP B 67 GLU B 74 1 8
HELIX 24 AC6 THR B 82 LEU B 100 1 19
HELIX 25 AC7 MET B 112 ALA B 124 1 13
HELIX 26 AC8 PRO B 144 VAL B 149 1 6
HELIX 27 AC9 ALA B 151 LYS B 155 5 5
HELIX 28 AD1 LEU B 159 MET B 163 5 5
HELIX 29 AD2 ASP B 181 TYR B 193 1 13
HELIX 30 AD3 ALA B 197 MET B 208 1 12
HELIX 31 AD4 ALA B 214 THR B 219 1 6
HELIX 32 AD5 ARG B 227 ILE B 231 5 5
HELIX 33 AD6 LEU B 245 VAL B 260 1 16
HELIX 34 AD7 SER B 275 GLN B 280 1 6
HELIX 35 AD8 GLN B 280 SER B 294 1 15
HELIX 36 AD9 GLY C 25 CYS C 28 5 4
HELIX 37 AE1 TYR C 29 ARG C 39 1 11
HELIX 38 AE2 HIS C 51 ALA C 55 5 5
HELIX 39 AE3 PRO C 58 GLU C 63 5 6
HELIX 40 AE4 ASP C 67 GLU C 74 1 8
HELIX 41 AE5 THR C 82 HIS C 102 1 21
HELIX 42 AE6 MET C 112 ALA C 124 1 13
HELIX 43 AE7 PRO C 144 ARG C 150 1 7
HELIX 44 AE8 ALA C 151 LYS C 155 5 5
HELIX 45 AE9 LEU C 159 MET C 163 5 5
HELIX 46 AF1 SER C 166 GLY C 171 1 6
HELIX 47 AF2 ASP C 181 TYR C 193 1 13
HELIX 48 AF3 ALA C 197 MET C 208 1 12
HELIX 49 AF4 ALA C 215 THR C 219 5 5
HELIX 50 AF5 LEU C 245 VAL C 260 1 16
HELIX 51 AF6 SER C 275 GLN C 280 1 6
HELIX 52 AF7 GLN C 280 SER C 294 1 15
SHEET 1 AA1 6 SER A 43 ALA A 45 0
SHEET 2 AA1 6 PHE A 16 VAL A 19 1 N LEU A 18 O ILE A 44
SHEET 3 AA1 6 VAL A 105 SER A 111 1 O VAL A 108 N VAL A 17
SHEET 4 AA1 6 ILE A 128 ALA A 136 1 O VAL A 132 N LEU A 107
SHEET 5 AA1 6 ASP A 232 CYS A 238 1 O ILE A 236 N TYR A 133
SHEET 6 AA1 6 HIS A 266 LEU A 270 1 O HIS A 266 N ARG A 233
SHEET 1 AA2 2 ALA A 172 ARG A 174 0
SHEET 2 AA2 2 ASP A 211 PRO A 213 -1 O VAL A 212 N LEU A 173
SHEET 1 AA3 6 SER B 43 ALA B 45 0
SHEET 2 AA3 6 PHE B 16 VAL B 19 1 N PHE B 16 O ILE B 44
SHEET 3 AA3 6 VAL B 105 SER B 111 1 O VAL B 108 N VAL B 17
SHEET 4 AA3 6 ILE B 128 ALA B 136 1 O VAL B 132 N LEU B 107
SHEET 5 AA3 6 ASP B 232 CYS B 238 1 O ILE B 236 N TYR B 133
SHEET 6 AA3 6 HIS B 266 LEU B 270 1 O HIS B 268 N LYS B 237
SHEET 1 AA4 2 ALA B 172 ARG B 174 0
SHEET 2 AA4 2 ASP B 211 PRO B 213 -1 O VAL B 212 N LEU B 173
SHEET 1 AA5 6 SER C 43 ALA C 45 0
SHEET 2 AA5 6 PHE C 16 VAL C 19 1 N PHE C 16 O ILE C 44
SHEET 3 AA5 6 VAL C 105 SER C 111 1 O HIS C 110 N VAL C 19
SHEET 4 AA5 6 ILE C 128 ALA C 136 1 O LEU C 134 N GLY C 109
SHEET 5 AA5 6 ASP C 232 CYS C 238 1 O ILE C 236 N TYR C 133
SHEET 6 AA5 6 HIS C 266 LEU C 270 1 O HIS C 266 N ARG C 233
SHEET 1 AA6 2 ALA C 172 ARG C 174 0
SHEET 2 AA6 2 ASP C 211 PRO C 213 -1 O VAL C 212 N LEU C 173
CISPEP 1 ARG A 64 PRO A 65 0 10.08
CISPEP 2 ARG B 64 PRO B 65 0 7.18
CISPEP 3 ARG C 64 PRO C 65 0 -7.75
CRYST1 166.960 68.410 75.340 90.00 93.58 90.00 C 1 2 1 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 0.005989 0.000000 0.000374 0.00000
SCALE2 0.000000 0.014618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013299 0.00000
TER 2078 LEU A 297
TER 4054 SER B 294
TER 5992 SER C 294
MASTER 605 0 0 52 24 0 0 6 6306 3 0 72
END |