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HEADER HYDROLASE 27-AUG-02 1MJ5
TITLE LINB (HALOALKANE DEHALOGENASE) FROM SPHINGOMONAS
TITLE 2 PAUCIMOBILIS UT26 AT ATOMIC RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1,3,4,6-TETRACHLORO-1,4-CYCLOHEXADIENE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HALOALKANE DEHALOGENASE, 1,4- TCDN
COMPND 5 CHLOROHYDROLASE;
COMPND 6 EC: 3.8.1.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOMONAS PAUCIMOBILIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: UT26;
SOURCE 5 GENE: LINB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAQN
KEYWDS LINB, HYDROLASE,HALOALKANE DEHALOGENASE, 1,3,4,6-
KEYWDS 2 TETRACHLORO-1,4-CYCLOHEXADIENE DEHALOGENASE, GAMMA-
KEYWDS 3 HEXACHLOROCYCLOHEXANE DEGRADATION,ALPHA/BETA-HYDROLASE,
KEYWDS 4 ULTRA HIGH RESOLUTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.OAKLEY,J.DAMBORSKY,M.C.J.WILCE
REVDAT 1 27-AUG-03 1MJ5 0
JRNL AUTH A.J.OAKLEY,J.DAMBORSKY,M.C.J.WILCE
JRNL TITL THE STRUCTURE OF LINB AT 0.95A RESOLUTION:
JRNL TITL 2 DYNAMICS OF ACTIVE SITE RESIDUES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.J.OAKLEY,Z.PROKOP,M.BOHAC,J.KMUNICEK,T.JEDLICKA,
REMARK 1 AUTH 2 M.MONINCOVA,I.KUTA-SMATANOVA,Y.NAGATA,J.DAMBORSKY,
REMARK 1 AUTH 3 M.C.J.WILCE
REMARK 1 TITL SPHINGOMONAS PAUCIMOBILIS UT26: EVIDENCE FOR
REMARK 1 TITL 2 PRODUCT- AND WATER-MEDIATED INHIBITION
REMARK 1 REF BIOCHEMISTRY V. 41 4847 2002
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1 REFERENCE 2
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. 0.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.112
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.112
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.141
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 6763
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 134890
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5139
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 658
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.021
REMARK 3 ANGLE DISTANCES (A) : 0.037
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.115
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.106
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MJ5 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-DEC-2002.
REMARK 100 THE RCSB ID CODE IS RCSB016949.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-FEB-2002
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14BMC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 134890
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.950
REMARK 200 RESOLUTION RANGE LOW (A) : 22.763
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
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: PDB ENTRY 1CV2
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: 200 MM MGCL2, 100 MM TRIS HCL PH
REMARK 280 8.5, 20% (W/V) PEG 4,000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298.0K
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 23.19500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.36000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.19000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.36000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.19500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.19000
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 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 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
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 HIS A 299 CA C O CB CG ND1 CD2
REMARK 470 HIS A 299 CE1 NE2
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 NE2 GLN A 146 O HOH 3551 1.47
REMARK 500 O HOH 3428 O HOH 3582 2.03
REMARK 500 O HOH 3220 O HOH 3557 2.04
REMARK 500 NH1 ARG A 191 O HOH 3260 2.06
REMARK 500 O HOH 3328 O HOH 3372 2.13
REMARK 500 O HOH 3386 O HOH 3577 2.16
REMARK 500 O HOH 3500 O HOH 3618 2.18
REMARK 500 O HOH 3220 O HOH 3548 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 3220 O HOH 3328 2564 2.15
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 ASP A 147 O - C - N ANGL. DEV. =-19.8 DEGREES
REMARK 500 GLU A 184 OE1 - CD - OE2 ANGL. DEV. =-18.4 DEGREES
REMARK 500 ARG A 291 CD - NE - CZ ANGL. DEV. = 16.3 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 3526 DISTANCE = 6.32 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CV2 RELATED DB: PDB
REMARK 900 FIRST DESCRIPTION OF LINB
REMARK 900 RELATED ID: 1G42 RELATED DB: PDB
REMARK 900 LINB COMPLEXED WITH 1,2-DICHLOROPROPANE
REMARK 900 RELATED ID: 1G5F RELATED DB: PDB
REMARK 900 LINB COMPLEXED WITH 1,2-DICHLOROETHANE
REMARK 900 RELATED ID: 1G4H RELATED DB: PDB
REMARK 900 LINB COMPLEXED WITH BUTAN-1-OL
DBREF 1MJ5 A 1 296 SWS P51698 LINB_PSEPA 1 296
SEQADV 1MJ5 HIS A 297 SWS P51698 HIS TAG
SEQADV 1MJ5 HIS A 298 SWS P51698 HIS TAG
SEQADV 1MJ5 HIS A 299 SWS P51698 HIS TAG
SEQADV 1MJ5 HIS A 300 SWS P51698 HIS TAG
SEQADV 1MJ5 HIS A 301 SWS P51698 HIS TAG
SEQADV 1MJ5 HIS A 302 SWS P51698 HIS TAG
SEQRES 1 A 302 MET SER LEU GLY ALA LYS PRO PHE GLY GLU LYS LYS PHE
SEQRES 2 A 302 ILE GLU ILE LYS GLY ARG ARG MET ALA TYR ILE ASP GLU
SEQRES 3 A 302 GLY THR GLY ASP PRO ILE LEU PHE GLN HIS GLY ASN PRO
SEQRES 4 A 302 THR SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS CYS
SEQRES 5 A 302 ALA GLY LEU GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY
SEQRES 6 A 302 MET GLY ASP SER ASP LYS LEU ASP PRO SER GLY PRO GLU
SEQRES 7 A 302 ARG TYR ALA TYR ALA GLU HIS ARG ASP TYR LEU ASP ALA
SEQRES 8 A 302 LEU TRP GLU ALA LEU ASP LEU GLY ASP ARG VAL VAL LEU
SEQRES 9 A 302 VAL VAL HIS ASP TRP GLY SER ALA LEU GLY PHE ASP TRP
SEQRES 10 A 302 ALA ARG ARG HIS ARG GLU ARG VAL GLN GLY ILE ALA TYR
SEQRES 11 A 302 MET GLU ALA ILE ALA MET PRO ILE GLU TRP ALA ASP PHE
SEQRES 12 A 302 PRO GLU GLN ASP ARG ASP LEU PHE GLN ALA PHE ARG SER
SEQRES 13 A 302 GLN ALA GLY GLU GLU LEU VAL LEU GLN ASP ASN VAL PHE
SEQRES 14 A 302 VAL GLU GLN VAL LEU PRO GLY LEU ILE LEU ARG PRO LEU
SEQRES 15 A 302 SER GLU ALA GLU MET ALA ALA TYR ARG GLU PRO PHE LEU
SEQRES 16 A 302 ALA ALA GLY GLU ALA ARG ARG PRO THR LEU SER TRP PRO
SEQRES 17 A 302 ARG GLN ILE PRO ILE ALA GLY THR PRO ALA ASP VAL VAL
SEQRES 18 A 302 ALA ILE ALA ARG ASP TYR ALA GLY TRP LEU SER GLU SER
SEQRES 19 A 302 PRO ILE PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA
SEQRES 20 A 302 LEU THR THR GLY ARG MET ARG ASP PHE CYS ARG THR TRP
SEQRES 21 A 302 PRO ASN GLN THR GLU ILE THR VAL ALA GLY ALA HIS PHE
SEQRES 22 A 302 ILE GLN GLU ASP SER PRO ASP GLU ILE GLY ALA ALA ILE
SEQRES 23 A 302 ALA ALA PHE VAL ARG ARG LEU ARG PRO ALA HIS HIS HIS
SEQRES 24 A 302 HIS HIS HIS
HET MG 2001 1
HET MG 2002 1
HET MG 2003 1
HET CL 2004 1
HET CL 2005 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 MG 3(MG1 2+)
FORMUL 5 CL 2(CL1 1-)
FORMUL 7 HOH *658(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 SER A 156 1 10
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 TYR A 23 N LYS A 12
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 -13.40
CISPEP 2 ASP A 73 PRO A 74 0 17.12
CISPEP 3 THR A 216 PRO A 217 0 -11.99
CISPEP 4 THR A 216 PRO A 217 0 -3.73
CISPEP 5 GLU A 244 PRO A 245 0 5.79
CISPEP 6 GLU A 244 PRO A 245 0 -0.99
CRYST1 46.390 68.380 80.720 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 0.021556 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014624 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012389 0.00000
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