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HEADER HYDROLASE 31-JUL-98 1BN6
TITLE HALOALKANE DEHALOGENASE FROM A RHODOCOCCUS SPECIES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 BIOLOGICAL_UNIT: MONOMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 COLLECTION: ATCC 55388;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS DEHALOGENASE, ALPHA/BETA-HYDROLASE, DHLA, CRYSTAL STRUCTURE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.NEWMAN,T.S.PEAT,R.RICHARD,L.KAN,P.E.SWANSON,J.A.AFFHOLTER,
AUTHOR 2 I.H.HOLMES,J.F.SCHINDLER,C.J.UNKEFER,T.C.TERWILLIGER
REVDAT 1 18-FEB-00 1BN6 0
JRNL AUTH J.NEWMAN,T.S.PEAT,R.RICHARD,L.KAN,P.E.SWANSON,
JRNL AUTH 2 J.A.AFFHOLTER,I.H.HOLMES,J.F.SCHINDLER,C.J.UNKEFER,
JRNL AUTH 3 T.C.TERWILLIGER
JRNL TITL HALOALKANE DEHALOGENASES: STRUCTURE OF A
JRNL TITL 2 RHODOCOCCUS ENZYME
JRNL REF BIOCHEMISTRY V. 38 16105 1999
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.3
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,
REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,
REMARK 3 PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MLF
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.5
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 51084
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 SET) : 0.167
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5
REMARK 3 FREE R VALUE TEST SET COUNT : 2577
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7873
REMARK 3 BIN R VALUE (WORKING SET) : 0.179
REMARK 3 BIN FREE R VALUE : 0.202
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.3
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 437
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2336
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 329
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.4
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.413
REMARK 3 B22 (A**2) : -0.224
REMARK 3 B33 (A**2) : -0.189
REMARK 3 B12 (A**2) : 0.0
REMARK 3 B13 (A**2) : 0.0
REMARK 3 B23 (A**2) : 0.0
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.14
REMARK 3 ESD FROM SIGMAA (A) : 0.05
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.14
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.09
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.033
REMARK 3 BOND ANGLES (DEGREES) : 2.6
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.6
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.17
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.41 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 0.69 ; 2.0
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.50 ; 2.0
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 0.79 ; 2.5
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.385
REMARK 3 BSOL : 28.53
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 3 CUTOFF HIGH (ABS(F)) : 1447832.12
REMARK 4
REMARK 4 1BN6 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 6
REMARK 6 DID NOT SEE ANY OF THE C-TERMINAL EXFLAG TAG
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : APR-1998
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8157
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53599
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.48
REMARK 200 RESOLUTION RANGE LOW (A) : 50.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 4.8
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.065
REMARK 200 FOR THE DATA SET : 9.0
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.0
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.264
REMARK 200 FOR SHELL : 2.8
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: MODEL AT PH 5.5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.8
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS:
REMARK 280 1 UL PROTEIN (5MG/ML PROTEIN IN 150MM AMMONIUM SULFATE,
REMARK 280 10MM TRISSO4 PH 7.5, 1MM EDTA) +1 UL RESERVOIR OVER
REMARK 280 20-25% PEG 1.5K, 0.2M NAACETATE, 0.1M MES PH 5.5 AT 8C
REMARK 280 SOAKED INTO SAME CONDITIONS BUT HEPES PH 7.0 BEFORE DATA
REMARK 280 COLLECTION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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 1/2-X,1/2+Y,-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 46.75956
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.98401
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.75956
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.98401
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 12
REMARK 465 SER A 13
REMARK 465 GLU A 14
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH 559 O HOH 523 3547 1.75
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 ASP 167 VAL 168 0 117.23
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 15 DEGREES (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION
REMARK 500 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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 0 GLU 109 CB - CG - CD ANGL. DEV. = 24.9 DEGREES
REMARK 500 0 ALA 166 N - CA - CB ANGL. DEV. = 39.7 DEGREES
REMARK 500 0 ALA 166 C - CA - CB ANGL. DEV. = 17.7 DEGREES
REMARK 500 0 ALA 166 N - CA - C ANGL. DEV. = 15.5 DEGREES
REMARK 500 0 ALA 166 C-1 - N - CA ANGL. DEV. = 19.8 DEGREES
REMARK 500 0 ASP 167 C - CA - CB ANGL. DEV. = 35.8 DEGREES
REMARK 500 0 ASP 167 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 0 ASP 167 CA-1 - C-1 - N ANGL. DEV. = 27.8 DEGREES
REMARK 500 0 ASP 167 O-1 - C-1 - N ANGL. DEV. = 27.7 DEGREES
REMARK 500 0 VAL 168 CA-1 - C-1 - N ANGL. DEV. = 29.8 DEGREES
REMARK 500 0 VAL 168 O-1 - C-1 - N ANGL. DEV. = 33.9 DEGREES
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 4*RMSD AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,A4,A1,2X,
REMARK 500 A3,1X,A1,I4,A1,1X,A4,A1,4X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 0 LYS A 128 CB B LYS A 128 CA 0.207
REMARK 500 0 GLU A 158 CB GLU A 158 CG 0.153
REMARK 500 0 ALA A 166 N A ALA A 166 CA A 0.913
REMARK 500 0 ALA A 166 CA A ALA A 166 C A 0.203
REMARK 500 0 ALA A 166 CB A ALA A 166 CA A 0.450
REMARK 500 0 ASP A 167 N A ASP A 167 CA A 0.267
REMARK 500 0 ASP A 167 N B ASP A 167 CA B 0.185
REMARK 500 0 ASP A 167 CA B ASP A 167 C B 0.160
REMARK 500 0 VAL A 168 N VAL A 168 CA 0.210
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD RESIDUES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FIRST 11 RESIDUES ARE A HIS-TAG, THE LAST 12 ARE AN EXFLAG.
DBREF 1BN6 A 12 304 GB 3114657 AF060871 1 293
SEQADV 1BN6 VAL A 183 GB 3114657 ALA A 172 CONFLICT
SEQADV 1BN6 ILE A 220 GB 3114657 LEU A 209 CONFLICT
SEQADV 1BN6 GLY A 303 GB 3114657 ALA A 292 CONFLICT
SEQADV 1BN6 ALA A 305 GB 3114657 CONFLICT
SEQRES 1 A 294 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 294 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 A 294 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 294 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 A 294 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 294 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 A 294 TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 A 294 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 294 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 294 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU
SEQRES 11 A 294 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 A 294 PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP
SEQRES 13 A 294 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 A 294 GLU GLY VAL LEU PRO LYS CYS VAL VAL ARG PRO LEU THR
SEQRES 15 A 294 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 A 294 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 294 ILE PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 A 294 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 294 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 A 294 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 A 294 ASN CYS LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 A 294 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 A 294 ALA ARG TRP LEU PRO GLY LEU ALA
FORMUL 2 HOH *329(H2 O1)
HELIX 1 1 SER A 56 VAL A 66 5 11
HELIX 2 2 PHE A 92 ALA A 105 1 14
HELIX 3 3 ASP A 117 ARG A 129 1 13
HELIX 4 4 PRO A 131 ARG A 133 5 3
HELIX 5 5 TRP A 149 GLU A 151 5 3
HELIX 6 6 GLU A 154 PHE A 163 1 10
HELIX 7 7 VAL A 168 ILE A 173 1 6
HELIX 8 8 ALA A 178 GLU A 181 1 4
HELIX 9 9 VAL A 183 CYS A 187 1 5
HELIX 10 10 GLU A 194 PHE A 204 1 11
HELIX 11 11 PRO A 207 GLU A 219 5 13
HELIX 12 12 ALA A 227 GLN A 242 1 16
HELIX 13 13 PRO A 260 SER A 269 1 10
HELIX 14 14 LEU A 285 GLU A 287 5 3
HELIX 15 15 PRO A 290 GLY A 303 1 14
SHEET 1 A 3 HIS A 24 VAL A 28 0
SHEET 2 A 3 GLU A 31 VAL A 38 -1 N TYR A 35 O HIS A 24
SHEET 3 A 3 CYS A 72 PRO A 75 -1 N ALA A 74 O VAL A 36
SHEET 1 B 5 PRO A 45 LEU A 49 0
SHEET 2 B 5 VAL A 111 HIS A 116 1 N VAL A 112 O PRO A 45
SHEET 3 B 5 VAL A 134 MET A 140 1 N LYS A 135 O VAL A 111
SHEET 4 B 5 PRO A 246 TRP A 251 1 N PRO A 246 O ILE A 137
SHEET 5 B 5 CYS A 273 ASP A 277 1 N LYS A 274 O LYS A 247
CISPEP 1 ASN A 52 PRO A 53 0 0.15
CISPEP 2 GLU A 225 PRO A 226 0 -1.27
CISPEP 3 THR A 253 PRO A 254 0 1.10
SITE 1 CAT 3 ASP A 117 GLU A 141 HIS A 283
CRYST1 93.520 79.970 43.160 90.00 90.00 90.00 P 21 21 2 4
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 0.010693 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012505 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023170 0.00000
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