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HEADER HYDROLASE 01-NOV-00 1G5F
TITLE STRUCTURE OF LINB COMPLEXED WITH 1,2-DICHLOROETHANE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1,3,4,6-TETRACHLORO-1,4-CYCLOHEXADIENE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,4-TCDN CHLOROHYDROLASE;
COMPND 5 EC: 3.8.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOMONAS PAUCIMOBILIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: LINB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMLBH6
KEYWDS LINB HALOALKANE DEHALOGENASE HALOALKANES
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.OAKLEY,M.BOHAC,J.DAMBORSKY,M.C.J.WILCE
REVDAT 2 21-NOV-01 1G5F 1 JRNL AUTHOR
REVDAT 1 01-NOV-01 1G5F 0
JRNL AUTH A.J.OAKLEY,M.BOHAC,J.DAMBORSKY,M.C.J.WILCE
JRNL TITL EXPLORING THE STRUCTURE AND ACTIVITY OF LINB FROM
JRNL TITL 2 SPHINGOMONAS PAUCIMOBILIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.MAREK,J.VEVODOVA,I.K.SMATANOVA,Y.NAGATA,
REMARK 1 AUTH 2 L.A.SVENSSON,J.NEWMAN,M.TAKAGI,J.DAMBORSKY
REMARK 1 TITL CRYSTAL STRUCTURE OF THE HALOALKANE DEHALOGENASE
REMARK 1 TITL 2 FROM SPHINGOMONAS PAUCIMOBILIS UT26
REMARK 1 REF BIOCHEMISTRY V. 39 14082 2000
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 23831
REMARK 3
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) : 0.173
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1209
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3608
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 194
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2359
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 275
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.13000
REMARK 3 B22 (A**2) : -0.16000
REMARK 3 B33 (A**2) : 2.28000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.18
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.86
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.46
REMARK 3 BSOL : 81.93
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 : DCE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DCE.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G5F COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-2000.
REMARK 100 THE RCSB ID CODE IS RCSB012255.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-2000
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.90
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NI MIRRORS
REMARK 200 OPTICS : NI MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54733
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.8500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.35900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.090
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1CV2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 26.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 18-20%
REMARK 280 PEG 6000, 0.1 M TRIS BUFFER PH 8.9
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 25.43000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.94500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.43000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.94500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CA CA A 502 LIES ON A SPECIAL POSITION.
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 SER A 2
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
REMARK 500 CL2 DCE 601 O HOH 312 2.08
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LEU A 3 CA LEU A 3 N 0.033
REMARK 500 PRO A 39 CG PRO A 39 CB 0.040
REMARK 500 PRO A 39 CD PRO A 39 CG 0.040
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 31 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 ILE A 32 N - CA - C ANGL. DEV. =-15.4 DEGREES
REMARK 500 PRO A 39 C - N - CA ANGL. DEV. = 8.3 DEGREES
REMARK 500 VAL A 105 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 ILE A 134 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 ILE A 178 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G42 RELATED DB: PDB
REMARK 900 STRUCTURE OF 1,3,4,6-TETRACHLORO-1,4-CYCLOHEXADIENE
REMARK 900 HYDROLASE (LINB) FROM SPHINGOMONAS PAUCIMOBILIS COMPLEXED
REMARK 900 WITH 1,2-DICHLOROPROPANE
REMARK 900 RELATED ID: 1G4H RELATED DB: PDB
REMARK 900 LINB COMPLEXED WITH BUTAN-1-OL
DBREF 1G5F A 1 296 SWS P51698 LINB_PSEPA 1 296
SEQADV 1G5F 2MR A 291 SWS P51698 ARG 291 MODIFIED RESIDUE
SEQRES 1 A 296 MET SER LEU GLY ALA LYS PRO PHE GLY GLU LYS LYS PHE
SEQRES 2 A 296 ILE GLU ILE LYS GLY ARG ARG MET ALA TYR ILE ASP GLU
SEQRES 3 A 296 GLY THR GLY ASP PRO ILE LEU PHE GLN HIS GLY ASN PRO
SEQRES 4 A 296 THR SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS CYS
SEQRES 5 A 296 ALA GLY LEU GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY
SEQRES 6 A 296 MET GLY ASP SER ASP LYS LEU ASP PRO SER GLY PRO GLU
SEQRES 7 A 296 ARG TYR ALA TYR ALA GLU HIS ARG ASP TYR LEU ASP ALA
SEQRES 8 A 296 LEU TRP GLU ALA LEU ASP LEU GLY ASP ARG VAL VAL LEU
SEQRES 9 A 296 VAL VAL HIS ASP TRP GLY SER ALA LEU GLY PHE ASP TRP
SEQRES 10 A 296 ALA ARG ARG HIS ARG GLU ARG VAL GLN GLY ILE ALA TYR
SEQRES 11 A 296 MET GLU ALA ILE ALA MET PRO ILE GLU TRP ALA ASP PHE
SEQRES 12 A 296 PRO GLU GLN ASP ARG ASP LEU PHE GLN ALA PHE ARG SER
SEQRES 13 A 296 GLN ALA GLY GLU GLU LEU VAL LEU GLN ASP ASN VAL PHE
SEQRES 14 A 296 VAL GLU GLN VAL LEU PRO GLY LEU ILE LEU ARG PRO LEU
SEQRES 15 A 296 SER GLU ALA GLU MET ALA ALA TYR ARG GLU PRO PHE LEU
SEQRES 16 A 296 ALA ALA GLY GLU ALA ARG ARG PRO THR LEU SER TRP PRO
SEQRES 17 A 296 ARG GLN ILE PRO ILE ALA GLY THR PRO ALA ASP VAL VAL
SEQRES 18 A 296 ALA ILE ALA ARG ASP TYR ALA GLY TRP LEU SER GLU SER
SEQRES 19 A 296 PRO ILE PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA
SEQRES 20 A 296 LEU THR THR GLY ARG MET ARG ASP PHE CYS ARG THR TRP
SEQRES 21 A 296 PRO ASN GLN THR GLU ILE THR VAL ALA GLY ALA HIS PHE
SEQRES 22 A 296 ILE GLN GLU ASP SER PRO ASP GLU ILE GLY ALA ALA ILE
SEQRES 23 A 296 ALA ALA PHE VAL 2MR ARG LEU ARG PRO ALA
MODRES 1G5F 2MR A 291 N3, N4-DIMETHYLARGININE
HET 2MR A 291 13
HET CA A 501 1
HET CA A 502 1
HET CA A 503 1
HET CL 504 1
HET DCE 601 8
HETNAM 2MR N3, N4-DIMETHYLARGININE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM DCE 1,2-DICHLOROETHANE
HETSYN DCE ETHYLENE DICHLORIDE
FORMUL 1 2MR C8 H18 N4 O2
FORMUL 2 CA 3(CA1 2+)
FORMUL 5 CL CL1 1-
FORMUL 6 DCE C2 H4 CL2
FORMUL 7 HOH *275(H2 O1)
HELIX 1 1 SER A 41 ARG A 46 5 6
HELIX 2 2 ILE A 48 ALA A 53 5 6
HELIX 3 3 ALA A 81 LEU A 96 1 16
HELIX 4 4 ASP A 108 HIS A 121 1 14
HELIX 5 5 GLU A 139 PHE A 143 5 5
HELIX 6 6 PRO A 144 ARG A 155 1 12
HELIX 7 7 ALA A 158 LEU A 164 1 7
HELIX 8 8 ASN A 167 GLN A 172 1 6
HELIX 9 9 GLN A 172 LEU A 177 1 6
HELIX 10 10 SER A 183 GLU A 192 1 10
HELIX 11 11 PRO A 193 LEU A 195 5 3
HELIX 12 12 GLY A 198 ARG A 201 5 4
HELIX 13 13 ARG A 202 TRP A 207 1 6
HELIX 14 14 PRO A 208 ILE A 211 5 4
HELIX 15 15 PRO A 217 SER A 232 1 16
HELIX 16 16 THR A 250 ARG A 258 1 9
HELIX 17 17 PHE A 273 ASP A 277 5 5
HELIX 18 18 SER A 278 VAL A 290 1 13
SHEET 1 A 8 LYS A 12 ILE A 16 0
SHEET 2 A 8 ARG A 19 GLU A 26 -1 O ARG A 19 N ILE A 16
SHEET 3 A 8 ARG A 57 CYS A 61 -1 N LEU A 58 O GLU A 26
SHEET 4 A 8 PRO A 31 GLN A 35 1 N ILE A 32 O ARG A 57
SHEET 5 A 8 VAL A 102 HIS A 107 1 O VAL A 103 N LEU A 33
SHEET 6 A 8 VAL A 125 MET A 131 1 N GLN A 126 O VAL A 102
SHEET 7 A 8 LYS A 238 PRO A 245 1 O LEU A 239 N TYR A 130
SHEET 8 A 8 GLN A 263 GLY A 270 1 O THR A 264 N PHE A 240
CISPEP 1 ASN A 38 PRO A 39 0 0.01
CISPEP 2 ASP A 73 PRO A 74 0 -0.16
CISPEP 3 THR A 216 PRO A 217 0 -0.24
CISPEP 4 GLU A 244 PRO A 245 0 0.47
CRYST1 50.860 71.890 73.290 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 0.019662 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013910 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013644 0.00000
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