HEADER APOPTOSIS 02-JAN-15 4S0O
TITLE CRYSTAL STRUCTURE OF THE AUTOINHIBITED DIMER OF PRO-APOPTOTIC BAX (I)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BAX;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BCL-2-LIKE PROTEIN 4, BCL2-L-4;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BAX, BCL2L4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BCL-2 FAMILY PROTEIN, APOPTOSIS REGULATOR, AUTOINHIBITED DIMER,
KEYWDS 2 APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PRIYADARSHI,E.GAVATHIOTIS
REVDAT 4 20-SEP-23 4S0O 1 SEQADV
REVDAT 3 22-NOV-17 4S0O 1 REMARK
REVDAT 2 17-AUG-16 4S0O 1 JRNL
REVDAT 1 20-JUL-16 4S0O 0
JRNL AUTH T.P.GARNER,D.E.REYNA,A.PRIYADARSHI,H.C.CHEN,S.LI,Y.WU,
JRNL AUTH 2 Y.T.GANESAN,V.N.MALASHKEVICH,S.S.ALMO,E.H.CHENG,
JRNL AUTH 3 E.GAVATHIOTIS
JRNL TITL AN AUTOINHIBITED DIMERIC FORM OF BAX REGULATES THE BAX
JRNL TITL 2 ACTIVATION PATHWAY.
JRNL REF MOL.CELL V. 63 485 2016
JRNL REFN ISSN 1097-2765
JRNL PMID 27425408
JRNL DOI 10.1016/J.MOLCEL.2016.06.010
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 24766
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1315
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1818
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 83
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2754
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.189
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.176
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.125
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.350
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2814 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3807 ; 1.856 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 348 ; 5.740 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 118 ;36.075 ;23.898
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 492 ;16.943 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;17.035 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 432 ; 0.132 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2074 ; 0.011 ; 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): 1738 ; 1.342 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2787 ; 2.219 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1076 ; 3.197 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1020 ; 4.877 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 13 A 192
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8697 -0.4708 13.2349
REMARK 3 T TENSOR
REMARK 3 T11: 0.0735 T22: 0.0249
REMARK 3 T33: 0.0385 T12: 0.0323
REMARK 3 T13: -0.0190 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 2.2922 L22: 0.7431
REMARK 3 L33: 0.9852 L12: -0.0017
REMARK 3 L13: 0.7146 L23: 0.3754
REMARK 3 S TENSOR
REMARK 3 S11: -0.1057 S12: -0.1624 S13: -0.0680
REMARK 3 S21: 0.1071 S22: 0.0899 S23: -0.1196
REMARK 3 S31: 0.0313 S32: -0.0093 S33: 0.0158
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 13 B 192
REMARK 3 ORIGIN FOR THE GROUP (A): 36.6218 0.1200 19.4609
REMARK 3 T TENSOR
REMARK 3 T11: 0.0672 T22: 0.0226
REMARK 3 T33: 0.0348 T12: -0.0305
REMARK 3 T13: -0.0084 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 2.2692 L22: 0.8401
REMARK 3 L33: 0.9898 L12: 0.0235
REMARK 3 L13: -0.9087 L23: 0.1983
REMARK 3 S TENSOR
REMARK 3 S11: -0.0889 S12: 0.1384 S13: 0.0593
REMARK 3 S21: -0.1018 S22: 0.0890 S23: -0.1309
REMARK 3 S31: -0.0191 S32: -0.0019 S33: -0.0001
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4S0O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000088031.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24766
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.60000
REMARK 200 R SYM FOR SHELL (I) : 0.23000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLECULAR REPLACEMENT
REMARK 200 STARTING MODEL: 1F16
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE, 0.1 M BIS-TRIS
REMARK 280 , PH 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 20.13800
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: 1870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 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 ASP A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 GLY A 5
REMARK 465 GLU A 6
REMARK 465 GLN A 7
REMARK 465 PRO A 8
REMARK 465 ARG A 9
REMARK 465 GLY A 10
REMARK 465 GLY A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 36
REMARK 465 ARG A 37
REMARK 465 MET A 38
REMARK 465 GLY A 39
REMARK 465 GLY A 40
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 GLY B 3
REMARK 465 SER B 4
REMARK 465 GLY B 5
REMARK 465 GLU B 6
REMARK 465 GLN B 7
REMARK 465 PRO B 8
REMARK 465 ARG B 9
REMARK 465 GLY B 10
REMARK 465 GLY B 11
REMARK 465 GLY B 12
REMARK 465 ARG B 37
REMARK 465 MET B 38
REMARK 465 GLY B 39
REMARK 465 GLY B 40
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 ASP A 84 107.01 -51.47
REMARK 500 ALA B 35 48.71 -71.22
REMARK 500 ASP B 84 102.99 -54.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4S0P RELATED DB: PDB
REMARK 900 RELATED ID: 1F16 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX
DBREF 4S0O A 1 192 UNP Q07812 BAX_HUMAN 1 192
DBREF 4S0O B 1 192 UNP Q07812 BAX_HUMAN 1 192
SEQADV 4S0O GLY A 168 UNP Q07812 PRO 168 ENGINEERED MUTATION
SEQADV 4S0O GLY B 168 UNP Q07812 PRO 168 ENGINEERED MUTATION
SEQRES 1 A 192 MET ASP GLY SER GLY GLU GLN PRO ARG GLY GLY GLY PRO
SEQRES 2 A 192 THR SER SER GLU GLN ILE MET LYS THR GLY ALA LEU LEU
SEQRES 3 A 192 LEU GLN GLY PHE ILE GLN ASP ARG ALA GLY ARG MET GLY
SEQRES 4 A 192 GLY GLU ALA PRO GLU LEU ALA LEU ASP PRO VAL PRO GLN
SEQRES 5 A 192 ASP ALA SER THR LYS LYS LEU SER GLU CYS LEU LYS ARG
SEQRES 6 A 192 ILE GLY ASP GLU LEU ASP SER ASN MET GLU LEU GLN ARG
SEQRES 7 A 192 MET ILE ALA ALA VAL ASP THR ASP SER PRO ARG GLU VAL
SEQRES 8 A 192 PHE PHE ARG VAL ALA ALA ASP MET PHE SER ASP GLY ASN
SEQRES 9 A 192 PHE ASN TRP GLY ARG VAL VAL ALA LEU PHE TYR PHE ALA
SEQRES 10 A 192 SER LYS LEU VAL LEU LYS ALA LEU CYS THR LYS VAL PRO
SEQRES 11 A 192 GLU LEU ILE ARG THR ILE MET GLY TRP THR LEU ASP PHE
SEQRES 12 A 192 LEU ARG GLU ARG LEU LEU GLY TRP ILE GLN ASP GLN GLY
SEQRES 13 A 192 GLY TRP ASP GLY LEU LEU SER TYR PHE GLY THR GLY THR
SEQRES 14 A 192 TRP GLN THR VAL THR ILE PHE VAL ALA GLY VAL LEU THR
SEQRES 15 A 192 ALA SER LEU THR ILE TRP LYS LYS MET GLY
SEQRES 1 B 192 MET ASP GLY SER GLY GLU GLN PRO ARG GLY GLY GLY PRO
SEQRES 2 B 192 THR SER SER GLU GLN ILE MET LYS THR GLY ALA LEU LEU
SEQRES 3 B 192 LEU GLN GLY PHE ILE GLN ASP ARG ALA GLY ARG MET GLY
SEQRES 4 B 192 GLY GLU ALA PRO GLU LEU ALA LEU ASP PRO VAL PRO GLN
SEQRES 5 B 192 ASP ALA SER THR LYS LYS LEU SER GLU CYS LEU LYS ARG
SEQRES 6 B 192 ILE GLY ASP GLU LEU ASP SER ASN MET GLU LEU GLN ARG
SEQRES 7 B 192 MET ILE ALA ALA VAL ASP THR ASP SER PRO ARG GLU VAL
SEQRES 8 B 192 PHE PHE ARG VAL ALA ALA ASP MET PHE SER ASP GLY ASN
SEQRES 9 B 192 PHE ASN TRP GLY ARG VAL VAL ALA LEU PHE TYR PHE ALA
SEQRES 10 B 192 SER LYS LEU VAL LEU LYS ALA LEU CYS THR LYS VAL PRO
SEQRES 11 B 192 GLU LEU ILE ARG THR ILE MET GLY TRP THR LEU ASP PHE
SEQRES 12 B 192 LEU ARG GLU ARG LEU LEU GLY TRP ILE GLN ASP GLN GLY
SEQRES 13 B 192 GLY TRP ASP GLY LEU LEU SER TYR PHE GLY THR GLY THR
SEQRES 14 B 192 TRP GLN THR VAL THR ILE PHE VAL ALA GLY VAL LEU THR
SEQRES 15 B 192 ALA SER LEU THR ILE TRP LYS LYS MET GLY
FORMUL 3 HOH *124(H2 O)
HELIX 1 1 SER A 15 ALA A 35 1 21
HELIX 2 2 ALA A 42 ALA A 46 5 5
HELIX 3 3 ASP A 53 SER A 72 1 20
HELIX 4 4 ASN A 73 ALA A 82 1 10
HELIX 5 5 PRO A 88 PHE A 100 1 13
HELIX 6 6 ASN A 106 THR A 127 1 22
HELIX 7 7 PRO A 130 LEU A 148 1 19
HELIX 8 8 LEU A 148 GLN A 155 1 8
HELIX 9 9 GLY A 157 PHE A 165 5 9
HELIX 10 10 THR A 169 GLY A 192 1 24
HELIX 11 11 SER B 15 ALA B 35 1 21
HELIX 12 12 ALA B 42 ALA B 46 5 5
HELIX 13 13 ASP B 53 SER B 72 1 20
HELIX 14 14 ASN B 73 ALA B 82 1 10
HELIX 15 15 PRO B 88 PHE B 100 1 13
HELIX 16 16 ASN B 106 THR B 127 1 22
HELIX 17 17 PRO B 130 LEU B 148 1 19
HELIX 18 18 LEU B 148 GLN B 155 1 8
HELIX 19 19 GLY B 157 ASP B 159 5 3
HELIX 20 20 GLY B 160 PHE B 165 1 6
HELIX 21 21 THR B 169 GLY B 192 1 24
CRYST1 63.657 40.276 65.303 90.00 90.02 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 0.015709 0.000000 0.000005 0.00000
SCALE2 0.000000 0.024829 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015313 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
