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HEADER HYDROLASE 16-OCT-01 1K6E
TITLE COMPLEX OF HYDROLYTIC HALOALKANE DEHALOGENASE LINB FROM
TITLE 2 SPHINGOMONAS PAUCIMOBILIS UT26 WITH 1,2-PROPANEDIOL
TITLE 3 (PRODUCT OF DEHALOGENATION OF 1,2-DIBROMOPROPANE) AT 1.85A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LINB, 1,3,4,6-TETRACHLORO-1,4-CYCLOHEXADIENE
COMPND 5 HYDROLASE;
COMPND 6 EC: 3.8.1.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOMONAS PAUCIMOBILIS;
SOURCE 3 STRAIN: UT26;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMYLB1
KEYWDS DEHALOGENASE, LINDANE, BIODEGRADATION, ALPHA/BETA-HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.A.STRELTSOV,Z.PROKOP,J.DAMBORSKY,Y.NAGATA,A.OAKLEY,
AUTHOR 2 M.C.J.WILCE
REVDAT 1 19-AUG-03 1K6E 0
JRNL AUTH V.A.STRELTSOV,Z.PROKOP,J.DAMBORSKY,Y.NAGATA,
JRNL AUTH 2 A.OAKLEY,M.C.J.WILCE
JRNL TITL HALOALKANE DEHALOGENASE LINB FROM SPHINGOMONAS
JRNL TITL 2 PAUCIMOBILIS UT26: X-RAY CRYSTALLOGRAPHIC STUDIES
JRNL TITL 3 OF DEHALOGENATION OF BROMINATED SUBSTRATES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0 AND XTALVIEW
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 21714
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) : 0.142
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2155
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 4
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 65.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3513
REMARK 3 BIN R VALUE (WORKING SET) : 0.1910
REMARK 3 BIN FREE R VALUE : 0.2270
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 389
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2327
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 468
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.66000
REMARK 3 B22 (A**2) : -3.02000
REMARK 3 B33 (A**2) : -0.64000
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) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.13
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) : 0.21
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.70
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.08
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 75.86
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : PGO_DRG.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : PGO_DRG.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS REFINED ALSO WITH
REMARK 3 XTALVIEW.
REMARK 4
REMARK 4 1K6E COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-2001.
REMARK 100 THE RCSB ID CODE IS RCSB014617.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-2001
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.20
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) : 1.54179
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MONOCHROMATOR AND MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21714
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 34.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.8590
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1K5P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000,MAGNESIUM CHLORIDE, TRIS,
REMARK 280 PH 8.20, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-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 23.20500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.49000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.16500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.49000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.20500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.16500
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 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 SER A 2 CB
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 O HOH 234 O HOH 251 1.98
REMARK 500 O HOH 229 O HOH 330 2.19
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 234 O HOH 467 3545 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 MET A 66 SD MET A 66 CE 0.100
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 LEU A 3 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 LYS A 12 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 ILE A 32 N - CA - C ANGL. DEV. =-16.1 DEGREES
REMARK 500 PRO A 39 C - N - CA ANGL. DEV. = 12.5 DEGREES
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 387 DISTANCE = 7.28 ANGSTROMS
REMARK 525 HOH 427 DISTANCE = 7.92 ANGSTROMS
REMARK 525 HOH 431 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH 433 DISTANCE = 7.17 ANGSTROMS
REMARK 525 HOH 446 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH 460 DISTANCE = 6.58 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 BR(1001) AND CL(1003) ARE IN ALTERNATE CONFORMATIONS
REMARK 600 OF EACH OTHER.
REMARK 600 CL(1004) AND BR(1002) ARE IN ALTERNATE CONFORMATIONS
REMARK 600 OF EACH OTHER.
REMARK 600 PGO(2001) AND 1BP(2002) AND 1BP(2003) ARE IN ALTERNATE
REMARK 600 CONFORMATIONS OF EACH OTHER.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K5P RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE LINB
REMARK 900 RELATED ID: 1K63 RELATED DB: PDB
REMARK 900 COMPLEX OF HALOALKANE DEHALOGENASE LINB WITH 2-BROMO-2-
REMARK 900 PROPENE-1-OL
DBREF 1K6E A 2 296 SWS P51698 LINB_PSEPA 2 296
SEQRES 1 A 295 SER LEU GLY ALA LYS PRO PHE GLY GLU LYS LYS PHE ILE
SEQRES 2 A 295 GLU ILE LYS GLY ARG ARG MET ALA TYR ILE ASP GLU GLY
SEQRES 3 A 295 THR GLY ASP PRO ILE LEU PHE GLN HIS GLY ASN PRO THR
SEQRES 4 A 295 SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS CYS ALA
SEQRES 5 A 295 GLY LEU GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY MET
SEQRES 6 A 295 GLY ASP SER ASP LYS LEU ASP PRO SER GLY PRO GLU ARG
SEQRES 7 A 295 TYR ALA TYR ALA GLU HIS ARG ASP TYR LEU ASP ALA LEU
SEQRES 8 A 295 TRP GLU ALA LEU ASP LEU GLY ASP ARG VAL VAL LEU VAL
SEQRES 9 A 295 VAL HIS ASP TRP GLY SER ALA LEU GLY PHE ASP TRP ALA
SEQRES 10 A 295 ARG ARG HIS ARG GLU ARG VAL GLN GLY ILE ALA TYR MET
SEQRES 11 A 295 GLU ALA ILE ALA MET PRO ILE GLU TRP ALA ASP PHE PRO
SEQRES 12 A 295 GLU GLN ASP ARG ASP LEU PHE GLN ALA PHE ARG SER GLN
SEQRES 13 A 295 ALA GLY GLU GLU LEU VAL LEU GLN ASP ASN VAL PHE VAL
SEQRES 14 A 295 GLU GLN VAL LEU PRO GLY LEU ILE LEU ARG PRO LEU SER
SEQRES 15 A 295 GLU ALA GLU MET ALA ALA TYR ARG GLU PRO PHE LEU ALA
SEQRES 16 A 295 ALA GLY GLU ALA ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 17 A 295 GLN ILE PRO ILE ALA GLY THR PRO ALA ASP VAL VAL ALA
SEQRES 18 A 295 ILE ALA ARG ASP TYR ALA GLY TRP LEU SER GLU SER PRO
SEQRES 19 A 295 ILE PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA LEU
SEQRES 20 A 295 THR THR GLY ARG MET ARG ASP PHE CYS ARG THR TRP PRO
SEQRES 21 A 295 ASN GLN THR GLU ILE THR VAL ALA GLY ALA HIS PHE ILE
SEQRES 22 A 295 GLN GLU ASP SER PRO ASP GLU ILE GLY ALA ALA ILE ALA
SEQRES 23 A 295 ALA PHE VAL ARG ARG LEU ARG PRO ALA
HET BR 1001 1
HET BR 1002 1
HET CL 1003 1
HET CL 1004 1
HET MG 1005 1
HET MG 1006 1
HET MG 1007 1
HET PGO 2001 5
HET 1BP 2002 5
HET 1BP 2003 5
HETNAM BR BROMIDE ION
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETNAM PGO 1,2-PROPANEDIOL
HETNAM 1BP 1-BROMOPROPANE-2-OL
FORMUL 2 BR 2(BR1 1-)
FORMUL 4 CL 2(CL1 1-)
FORMUL 6 MG 3(MG1 2+)
FORMUL 9 PGO C3 H8 O2
FORMUL 10 1BP 2(C3 H7 O1 BR1)
FORMUL 12 HOH *468(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 GLN A 146 5 3
HELIX 7 7 ASP A 147 ARG A 155 1 9
HELIX 8 8 ALA A 158 LEU A 164 1 7
HELIX 9 9 ASN A 167 GLN A 172 1 6
HELIX 10 10 GLN A 172 LEU A 177 1 6
HELIX 11 11 SER A 183 GLU A 192 1 10
HELIX 12 12 PRO A 193 LEU A 195 5 3
HELIX 13 13 GLY A 198 ALA A 200 5 3
HELIX 14 14 ARG A 201 TRP A 207 1 7
HELIX 15 15 PRO A 208 ILE A 211 5 4
HELIX 16 16 PRO A 217 SER A 232 1 16
HELIX 17 17 THR A 250 ARG A 258 1 9
HELIX 18 18 PHE A 273 ASP A 277 5 5
HELIX 19 19 SER A 278 ARG A 294 1 17
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 O LEU A 58 N GLU A 26
SHEET 4 A 8 PRO A 31 GLN A 35 1 N PHE A 34 O ILE A 59
SHEET 5 A 8 VAL A 102 HIS A 107 1 O VAL A 105 N LEU A 33
SHEET 6 A 8 VAL A 125 MET A 131 1 O ALA A 129 N LEU A 104
SHEET 7 A 8 LYS A 238 PRO A 245 1 O ILE A 241 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 -1.15
CISPEP 2 ASP A 73 PRO A 74 0 1.25
CISPEP 3 THR A 216 PRO A 217 0 -0.42
CISPEP 4 GLU A 244 PRO A 245 0 0.21
CRYST1 46.410 68.330 80.980 90.00 90.00 90.00 P 21 21 21 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 0.021547 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014635 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012349 0.00000
TER 2328 ALA A 296
MASTER 316 0 10 19 8 0 0 6 2817 1 15 23
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