HEADER DEHALOGENASE 08-SEP-93 2DHC
TITLE CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE
TITLE 2 DEHALOGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOBACTER AUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 280
KEYWDS DEHALOGENASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.H.G.VERSCHUEREN,B.W.DIJKSTRA
REVDAT 5 14-FEB-24 2DHC 1 REMARK
REVDAT 4 29-NOV-17 2DHC 1 HELIX
REVDAT 3 24-FEB-09 2DHC 1 VERSN
REVDAT 2 01-APR-03 2DHC 1 JRNL
REVDAT 1 31-JUL-94 2DHC 0
JRNL AUTH K.H.VERSCHUEREN,F.SELJEE,H.J.ROZEBOOM,K.H.KALK,B.W.DIJKSTRA
JRNL TITL CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF
JRNL TITL 2 HALOALKANE DEHALOGENASE.
JRNL REF NATURE V. 363 693 1993
JRNL REFN ISSN 0028-0836
JRNL PMID 8515812
JRNL DOI 10.1038/363693A0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.M.FRANKEN,H.J.ROZEBOOM,K.H.KALK,B.W.DIJKSTRA
REMARK 1 TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE: AN ENZYME TO
REMARK 1 TITL 2 DETOXIFY HALOGENATED ALKANES
REMARK 1 REF EMBO J. V. 10 1297 1991
REMARK 1 REFN ISSN 0261-4189
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.J.ROZEBOOM,J.KINGMA,D.B.JANSSEN,B.W.DIJKSTRA
REMARK 1 TITL CRYSTALLIZATION OF HALOALKANE DEHALOGENASE FROM XANTHOBACTER
REMARK 1 TITL 2 AUTOTROPHICUS GJ10
REMARK 1 REF J.MOL.BIOL. V. 200 611 1988
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 11326
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2479
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 122
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.014 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 3.900 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DHC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177995.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 -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 47.45000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.45000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.40000
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 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: MONOMERIC
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 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 DISTANCE
REMARK 500 O GLY A 288 O HOH A 522 2.12
REMARK 500 O HOH A 407 O HOH A 435 2.19
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 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 6 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP A 9 CB - CG - OD1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 PRO A 22 CB - CA - C ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG A 35 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASP A 48 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 LEU A 53 CB - CG - CD2 ANGL. DEV. = -11.6 DEGREES
REMARK 500 ARG A 76 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 LYS A 87 N - CA - CB ANGL. DEV. = 11.6 DEGREES
REMARK 500 ASP A 89 CB - CG - OD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP A 89 CB - CG - OD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP A 93 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 103 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG A 112 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASP A 124 CB - CG - OD1 ANGL. DEV. = -10.1 DEGREES
REMARK 500 ASP A 124 CB - CG - OD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP A 137 CB - CG - OD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG A 140 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 143 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG A 143 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ASP A 170 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 VAL A 180 CG1 - CB - CG2 ANGL. DEV. = -10.8 DEGREES
REMARK 500 ASP A 184 CB - CG - OD2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 ALA A 201 CB - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 ALA A 201 N - CA - CB ANGL. DEV. = 9.3 DEGREES
REMARK 500 PRO A 211 C - N - CD ANGL. DEV. = -12.9 DEGREES
REMARK 500 ARG A 220 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 MET A 225 CG - SD - CE ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG A 229 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP A 230 CB - CG - OD1 ANGL. DEV. = 10.1 DEGREES
REMARK 500 ASP A 230 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ASP A 235 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 235 CB - CG - OD2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 MET A 258 CG - SD - CE ANGL. DEV. = 9.7 DEGREES
REMARK 500 ASP A 266 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 PRO A 270 C - N - CD ANGL. DEV. = -12.8 DEGREES
REMARK 500 LEU A 274 CB - CG - CD2 ANGL. DEV. = -13.4 DEGREES
REMARK 500 ARG A 300 NE - CZ - NH2 ANGL. DEV. = 3.5 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 TYR A 31 51.88 -108.24
REMARK 500 ASN A 43 104.43 -59.81
REMARK 500 SER A 44 18.79 -67.32
REMARK 500 THR A 58 -162.92 -106.87
REMARK 500 ALA A 79 80.13 -172.16
REMARK 500 ASP A 114 70.04 51.59
REMARK 500 ASP A 124 -144.57 56.67
REMARK 500 ASP A 137 86.56 -161.89
REMARK 500 LYS A 142 -32.34 -130.52
REMARK 500 ASN A 148 91.61 -8.50
REMARK 500 CYS A 150 -161.87 -162.11
REMARK 500 PRO A 196 -10.07 -49.63
REMARK 500 LEU A 263 52.94 -118.98
REMARK 500 GLU A 280 109.97 -50.45
REMARK 500 GLN A 292 3.03 -64.24
REMARK 500 GLU A 308 -7.12 -59.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE HELIX AND SHEET STRUCTURES ARE SIMILAR TO THOSE IN
REMARK 700 PROTEIN DATA BANK ENTRY 2HAD.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCE A 600
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE ADVISORY NOTICE:
REMARK 999 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.
REMARK 999
REMARK 999 SWISS-PROT ENTRY NAME: HALO_XANAU
REMARK 999
REMARK 999 SWISS-PROT RESIDUE PDB SEQRES
REMARK 999
REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE
REMARK 999 ILE 120 LEU 120
REMARK 999
REMARK 999 THE SWISS-PROT ENTRY IS IN ERROR AND THE DEPOSITORS HAVE
REMARK 999 REQUESTED THAT THE SEQUENCE DATA BANKS MAKE THE PROPER
REMARK 999 CORRECTIONS.
DBREF 2DHC A 1 310 UNP P22643 DHLA_XANAU 1 310
SEQRES 1 A 310 MET ILE ASN ALA ILE ARG THR PRO ASP GLN ARG PHE SER
SEQRES 2 A 310 ASN LEU ASP GLN TYR PRO PHE SER PRO ASN TYR LEU ASP
SEQRES 3 A 310 ASP LEU PRO GLY TYR PRO GLY LEU ARG ALA HIS TYR LEU
SEQRES 4 A 310 ASP GLU GLY ASN SER ASP ALA GLU ASP VAL PHE LEU CYS
SEQRES 5 A 310 LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG LYS
SEQRES 6 A 310 MET ILE PRO VAL PHE ALA GLU SER GLY ALA ARG VAL ILE
SEQRES 7 A 310 ALA PRO ASP PHE PHE GLY PHE GLY LYS SER ASP LYS PRO
SEQRES 8 A 310 VAL ASP GLU GLU ASP TYR THR PHE GLU PHE HIS ARG ASN
SEQRES 9 A 310 PHE LEU LEU ALA LEU ILE GLU ARG LEU ASP LEU ARG ASN
SEQRES 10 A 310 ILE THR LEU VAL VAL GLN ASP TRP GLY GLY PHE LEU GLY
SEQRES 11 A 310 LEU THR LEU PRO MET ALA ASP PRO SER ARG PHE LYS ARG
SEQRES 12 A 310 LEU ILE ILE MET ASN ALA CYS LEU MET THR ASP PRO VAL
SEQRES 13 A 310 THR GLN PRO ALA PHE SER ALA PHE VAL THR GLN PRO ALA
SEQRES 14 A 310 ASP GLY PHE THR ALA TRP LYS TYR ASP LEU VAL THR PRO
SEQRES 15 A 310 SER ASP LEU ARG LEU ASP GLN PHE MET LYS ARG TRP ALA
SEQRES 16 A 310 PRO THR LEU THR GLU ALA GLU ALA SER ALA TYR ALA ALA
SEQRES 17 A 310 PRO PHE PRO ASP THR SER TYR GLN ALA GLY VAL ARG LYS
SEQRES 18 A 310 PHE PRO LYS MET VAL ALA GLN ARG ASP GLN ALA CYS ILE
SEQRES 19 A 310 ASP ILE SER THR GLU ALA ILE SER PHE TRP GLN ASN ASP
SEQRES 20 A 310 TRP ASN GLY GLN THR PHE MET ALA ILE GLY MET LYS ASP
SEQRES 21 A 310 LYS LEU LEU GLY PRO ASP VAL MET TYR PRO MET LYS ALA
SEQRES 22 A 310 LEU ILE ASN GLY CYS PRO GLU PRO LEU GLU ILE ALA ASP
SEQRES 23 A 310 ALA GLY HIS PHE VAL GLN GLU PHE GLY GLU GLN VAL ALA
SEQRES 24 A 310 ARG GLU ALA LEU LYS HIS PHE ALA GLU THR GLU
HET DCE A 600 4
HETNAM DCE 1,2-DICHLOROETHANE
HETSYN DCE ETHYLENE DICHLORIDE
FORMUL 2 DCE C2 H4 CL2
FORMUL 3 HOH *122(H2 O)
HELIX 1 A1 SER A 60 GLU A 72 1 13
HELIX 2 A2 PHE A 99 ARG A 112 1 14
HELIX 3 A3 ASP A 124 GLY A 130 1 7
HELIX 4 A4 PRO A 159 PHE A 164 1 6
HELIX 5 A5 PHE A 172 VAL A 180 1 9
HELIX 6 A6 LEU A 187 TRP A 194 1 8
HELIX 7 A7 GLU A 200 ALA A 207 1 8
HELIX 8 A8 THR A 213 ALA A 227 1 15
HELIX 9 A9 GLN A 231 ASN A 246 1 16
HELIX 10 A10 PRO A 265 LEU A 274 1 10
HELIX 11 A11 VAL A 291 HIS A 305 1 15
SHEET 1 S1 8 SER A 21 LEU A 25 0
SHEET 2 S1 8 ALA A 36 GLU A 41 -1
SHEET 3 S1 8 ARG A 76 PRO A 80 -1
SHEET 4 S1 8 VAL A 49 HIS A 54 1
SHEET 5 S1 8 ILE A 118 VAL A 122 1
SHEET 6 S1 8 PHE A 141 MET A 147 1
SHEET 7 S1 8 GLN A 251 GLY A 257 1
SHEET 8 S1 8 GLU A 280 ILE A 284 1
CISPEP 1 GLU A 56 PRO A 57 0 -5.64
CISPEP 2 GLN A 167 PRO A 168 0 2.04
SITE 1 AC1 8 GLU A 56 ASP A 124 TRP A 125 PHE A 128
SITE 2 AC1 8 TRP A 175 PRO A 223 VAL A 226 LEU A 262
CRYST1 94.900 72.800 41.500 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 0.010537 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013736 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024096 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
