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HEADER HYDROLASE 06-JUN-13 4BRZ
TITLE HALOALKANE DEHALOGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTERACEAE;
SOURCE 3 ORGANISM_TAXID: 31989;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA2;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-28A
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.R.NOVAK,C.SAYER,M.ISUPOV,D.GOTZ,A.M.SPRAGG,J.A.LITTLECHILD
REVDAT 1 14-MAY-14 4BRZ 0
JRNL AUTH H.R.NOVAK,C.SAYER,M.N.ISUPOV,D.GOTZ,A.M.SPRAGG,
JRNL AUTH 2 J.A.LITTLECHILD
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERISATION OF A HALOALKANE
JRNL TITL 2 DEHALOGENASE FROM A MARINE RHODOBACTERACEAE.
JRNL REF FEBS LETT. V. 588 1616 2014
JRNL REFN ISSN 0014-5793
JRNL PMID 24613925
JRNL DOI 10.1016/J.FEBSLET.2014.02.056
REMARK 2
REMARK 2 RESOLUTION. 1.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD4
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.54
REMARK 3 NUMBER OF REFLECTIONS : 58063
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 + TEST SET) : 0.20700
REMARK 3 R VALUE (WORKING SET) : 0.20486
REMARK 3 FREE R VALUE : 0.24600
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 3100
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.670
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.713
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4269
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.307
REMARK 3 BIN FREE R VALUE SET COUNT : 214
REMARK 3 BIN FREE R VALUE : 0.371
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4796
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 466
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.608
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.72
REMARK 3 B22 (A**2) : 0.44
REMARK 3 B33 (A**2) : -1.12
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.58
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.131
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.126
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.985
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4955 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6796 ; 1.235 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 654 ; 5.340 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 249 ;33.459 ;23.976
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 835 ;14.153 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;16.755 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 740 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3902 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2396 ; 3.082 ; 6.477
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3011 ; 3.883 ;10.905
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2559 ; 3.872 ; 7.070
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 4BRZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JUN-13.
REMARK 100 THE PDBE ID CODE IS EBI-57188.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 287
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9778
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61186
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.67
REMARK 200 RESOLUTION RANGE LOW (A) : 44.40
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.4
REMARK 200 R MERGE (I) : 0.04
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.50
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1CV2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 M MGCL2, 0.1 M TRIS-HCL AND
REMARK 280 30% PEG-4000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 37.76000
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 CD B GLU A 24 O HOH A 2023 1.54
REMARK 500 OE1B GLU A 24 O HOH A 2023 1.37
REMARK 500 OE2B GLU A 24 O HOH A 2023 1.52
REMARK 500 OE1B GLU A 160 O HOH A 2179 1.92
REMARK 500 OE2B GLU B 24 O HOH B 2009 1.37
REMARK 500 OG1B THR B 79 NE2B GLN B 209 2.14
REMARK 500 OG A SER B 291 O HOH B 2186 1.71
REMARK 500 O HOH B 2074 O HOH B 2075 1.85
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 PRO A 37 50.77 -102.34
REMARK 500 MET A 38 -159.14 -104.29
REMARK 500 ASP A 106 -134.72 59.85
REMARK 500 VAL A 246 -59.70 -137.77
REMARK 500 LEU A 270 -101.24 -102.33
REMARK 500 PRO B 37 49.19 -101.49
REMARK 500 MET B 38 -160.08 -103.40
REMARK 500 THR B 97 -16.57 -140.38
REMARK 500 ASP B 106 -124.23 54.07
REMARK 500 PRO B 211 97.88 -69.76
REMARK 500 VAL B 246 -60.39 -140.65
REMARK 500 LEU B 270 -97.25 -102.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1293
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1293
DBREF 4BRZ A 3 292 PDB 4BRZ 4BRZ 3 292
DBREF 4BRZ B 3 292 PDB 4BRZ 4BRZ 3 292
SEQRES 1 A 290 THR SER PHE ARG ASP LYS LYS LYS PHE ALA THR VAL HIS
SEQRES 2 A 290 GLY LYS GLN MET ALA TYR ILE GLU GLU GLY THR GLY ASP
SEQRES 3 A 290 PRO ILE VAL PHE LEU HIS GLY ASN PRO MET SER SER TYR
SEQRES 4 A 290 LEU TRP ARG ASN ILE MET PRO HIS LEU ALA GLY LYS GLY
SEQRES 5 A 290 ARG LEU ILE ALA PRO ASP LEU ILE GLY MET GLY ASP SER
SEQRES 6 A 290 ASP LYS LEU ASP ASN SER GLY PRO ASP SER TYR THR PHE
SEQRES 7 A 290 ALA GLU HIS CYS THR TYR LEU PHE ALA LEU LEU GLU GLN
SEQRES 8 A 290 LEU GLY VAL THR GLU ASN VAL THR LEU VAL ILE HIS ASP
SEQRES 9 A 290 TRP GLY SER GLY LEU GLY PHE HIS TRP ALA HIS THR HIS
SEQRES 10 A 290 SER ASP ALA VAL LYS GLY ILE ALA PHE MET GLU ALA ILE
SEQRES 11 A 290 VAL GLU THR ARG GLU SER TRP ASP ALA PHE PRO GLU ARG
SEQRES 12 A 290 ALA ARG GLU MET PHE GLN ALA LEU ARG SER PRO ALA GLY
SEQRES 13 A 290 GLU GLU MET VAL LEU GLU LYS ASN LEU PHE VAL GLU ALA
SEQRES 14 A 290 LEU VAL PRO GLY SER ILE LEU ARG ASP LEU THR GLU GLU
SEQRES 15 A 290 GLU MET ASN GLU TYR ARG ARG PRO PHE ALA ASN ALA GLY
SEQRES 16 A 290 GLU ASP ARG ARG PRO THR LEU THR PHE PRO ARG GLN VAL
SEQRES 17 A 290 PRO ILE GLU GLY GLN PRO LYS ASP VAL THR GLU LEU VAL
SEQRES 18 A 290 ASP ALA TYR VAL ASP TRP LEU GLY GLN THR SER ILE PRO
SEQRES 19 A 290 LYS LEU PHE ILE ASN ALA ASP PRO GLY VAL LEU ILE THR
SEQRES 20 A 290 GLY GLU VAL ARG ASP ARG VAL ARG SER TRP PRO ASN LEU
SEQRES 21 A 290 THR GLU VAL THR VAL ALA GLY LEU HIS PHE ILE GLN GLU
SEQRES 22 A 290 ASP SER PRO ASP GLU ILE GLY ALA ALA VAL ARG ASP TRP
SEQRES 23 A 290 HIS ALA SER LEU
SEQRES 1 B 290 THR SER PHE ARG ASP LYS LYS LYS PHE ALA THR VAL HIS
SEQRES 2 B 290 GLY LYS GLN MET ALA TYR ILE GLU GLU GLY THR GLY ASP
SEQRES 3 B 290 PRO ILE VAL PHE LEU HIS GLY ASN PRO MET SER SER TYR
SEQRES 4 B 290 LEU TRP ARG ASN ILE MET PRO HIS LEU ALA GLY LYS GLY
SEQRES 5 B 290 ARG LEU ILE ALA PRO ASP LEU ILE GLY MET GLY ASP SER
SEQRES 6 B 290 ASP LYS LEU ASP ASN SER GLY PRO ASP SER TYR THR PHE
SEQRES 7 B 290 ALA GLU HIS CYS THR TYR LEU PHE ALA LEU LEU GLU GLN
SEQRES 8 B 290 LEU GLY VAL THR GLU ASN VAL THR LEU VAL ILE HIS ASP
SEQRES 9 B 290 TRP GLY SER GLY LEU GLY PHE HIS TRP ALA HIS THR HIS
SEQRES 10 B 290 SER ASP ALA VAL LYS GLY ILE ALA PHE MET GLU ALA ILE
SEQRES 11 B 290 VAL GLU THR ARG GLU SER TRP ASP ALA PHE PRO GLU ARG
SEQRES 12 B 290 ALA ARG GLU MET PHE GLN ALA LEU ARG SER PRO ALA GLY
SEQRES 13 B 290 GLU GLU MET VAL LEU GLU LYS ASN LEU PHE VAL GLU ALA
SEQRES 14 B 290 LEU VAL PRO GLY SER ILE LEU ARG ASP LEU THR GLU GLU
SEQRES 15 B 290 GLU MET ASN GLU TYR ARG ARG PRO PHE ALA ASN ALA GLY
SEQRES 16 B 290 GLU ASP ARG ARG PRO THR LEU THR PHE PRO ARG GLN VAL
SEQRES 17 B 290 PRO ILE GLU GLY GLN PRO LYS ASP VAL THR GLU LEU VAL
SEQRES 18 B 290 ASP ALA TYR VAL ASP TRP LEU GLY GLN THR SER ILE PRO
SEQRES 19 B 290 LYS LEU PHE ILE ASN ALA ASP PRO GLY VAL LEU ILE THR
SEQRES 20 B 290 GLY GLU VAL ARG ASP ARG VAL ARG SER TRP PRO ASN LEU
SEQRES 21 B 290 THR GLU VAL THR VAL ALA GLY LEU HIS PHE ILE GLN GLU
SEQRES 22 B 290 ASP SER PRO ASP GLU ILE GLY ALA ALA VAL ARG ASP TRP
SEQRES 23 B 290 HIS ALA SER LEU
HET CL A1293 1
HET CL B1293 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL 2(CL 1-)
FORMUL 4 HOH *466(H2 O)
HELIX 1 1 PHE A 5 LYS A 9 5 5
HELIX 2 2 SER A 39 ARG A 44 5 6
HELIX 3 3 ILE A 46 ALA A 51 5 6
HELIX 4 4 THR A 79 LEU A 94 1 16
HELIX 5 5 ASP A 106 HIS A 119 1 14
HELIX 6 6 SER A 138 PHE A 142 5 5
HELIX 7 7 PRO A 143 ARG A 145 5 3
HELIX 8 8 ALA A 146 SER A 155 1 10
HELIX 9 9 ALA A 157 GLU A 164 1 8
HELIX 10 10 ASN A 166 ALA A 171 1 6
HELIX 11 11 VAL A 173 ILE A 177 5 5
HELIX 12 12 THR A 182 ARG A 191 1 10
HELIX 13 13 PRO A 192 ALA A 194 5 3
HELIX 14 14 GLY A 197 ARG A 200 5 4
HELIX 15 15 ARG A 201 VAL A 210 1 10
HELIX 16 16 PRO A 216 GLY A 231 1 16
HELIX 17 17 GLY A 250 ARG A 257 1 8
HELIX 18 18 PHE A 272 ASP A 276 5 5
HELIX 19 19 SER A 277 SER A 291 1 15
HELIX 20 20 PHE B 5 LYS B 9 5 5
HELIX 21 21 SER B 39 ARG B 44 5 6
HELIX 22 22 ILE B 46 ALA B 51 5 6
HELIX 23 23 THR B 79 LEU B 94 1 16
HELIX 24 24 ASP B 106 HIS B 119 1 14
HELIX 25 25 SER B 138 PHE B 142 5 5
HELIX 26 26 ALA B 146 ARG B 154 1 9
HELIX 27 27 ALA B 157 GLU B 164 1 8
HELIX 28 28 ASN B 166 SER B 176 1 11
HELIX 29 29 THR B 182 ARG B 191 1 10
HELIX 30 30 PRO B 192 ALA B 194 5 3
HELIX 31 31 GLY B 197 ARG B 200 5 4
HELIX 32 32 ARG B 201 VAL B 210 1 10
HELIX 33 33 PRO B 216 GLY B 231 1 16
HELIX 34 34 THR B 249 SER B 258 1 10
HELIX 35 35 PHE B 272 ASP B 276 5 5
HELIX 36 36 SER B 277 SER B 291 1 15
SHEET 1 AA 8 LYS A 10 VAL A 14 0
SHEET 2 AA 8 LYS A 17 GLU A 24 -1 O LYS A 17 N VAL A 14
SHEET 3 AA 8 ARG A 55 PRO A 59 -1 O LEU A 56 N GLU A 24
SHEET 4 AA 8 PRO A 29 LEU A 33 1 O ILE A 30 N ILE A 57
SHEET 5 AA 8 VAL A 100 HIS A 105 1 O THR A 101 N VAL A 31
SHEET 6 AA 8 VAL A 123 MET A 129 1 N LYS A 124 O VAL A 100
SHEET 7 AA 8 LYS A 237 PRO A 244 1 O LEU A 238 N PHE A 128
SHEET 8 AA 8 LEU A 262 GLY A 269 1 O THR A 263 N PHE A 239
SHEET 1 BA 8 LYS B 10 VAL B 14 0
SHEET 2 BA 8 LYS B 17 GLU B 24 -1 O LYS B 17 N VAL B 14
SHEET 3 BA 8 ARG B 55 PRO B 59 -1 O LEU B 56 N GLU B 24
SHEET 4 BA 8 PRO B 29 LEU B 33 1 O ILE B 30 N ILE B 57
SHEET 5 BA 8 VAL B 100 HIS B 105 1 O THR B 101 N VAL B 31
SHEET 6 BA 8 VAL B 123 MET B 129 1 N LYS B 124 O VAL B 100
SHEET 7 BA 8 LYS B 237 PRO B 244 1 O LEU B 238 N PHE B 128
SHEET 8 BA 8 LEU B 262 GLY B 269 1 O THR B 263 N PHE B 239
CISPEP 1 ASN A 36 PRO A 37 0 -6.31
CISPEP 2 GLN A 215 PRO A 216 0 -3.92
CISPEP 3 ASP A 243 PRO A 244 0 9.55
CISPEP 4 ASN B 36 PRO B 37 0 -10.36
CISPEP 5 GLN B 215 PRO B 216 0 -4.02
CISPEP 6 ASP B 243 PRO B 244 0 5.72
SITE 1 AC1 5 ASN A 36 TRP A 107 PHE A 150 PHE A 168
SITE 2 AC1 5 PRO A 207
SITE 1 AC2 3 ASN B 36 TRP B 107 PRO B 207
CRYST1 54.970 75.520 64.870 90.00 92.94 90.00 P 1 21 1 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 0.018192 0.000000 0.000934 0.00000
SCALE2 0.000000 0.013242 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015436 0.00000
TER 2400 LEU A 292
TER 4798 LEU B 292
MASTER 281 0 2 36 16 0 3 6 5264 2 0 46
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