HEADER CHAPERONE 01-FEB-07 2OR3
TITLE PRE-OXIDATION COMPLEX OF HUMAN DJ-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN DJ-1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ONCOGENE DJ1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PARK7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS CYSTEINE OXIDATION, NUCLEOPHILE ELBOW, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.WITT,M.LAKSHMINARASIMHAN,M.A.WILSON
REVDAT 4 22-JUL-08 2OR3 1 JRNL
REVDAT 3 08-JUL-08 2OR3 1 JRNL
REVDAT 2 01-JUL-08 2OR3 1 JRNL VERSN
REVDAT 1 13-FEB-07 2OR3 0
JRNL AUTH A.C.WITT,M.LAKSHMINARASIMHAN,B.C.REMINGTON,S.HASIM,
JRNL AUTH 2 E.POZHARSKI,M.A.WILSON
JRNL TITL CYSTEINE PKA DEPRESSION BY A PROTONATED GLUTAMIC
JRNL TITL 2 ACID IN HUMAN DJ-1.
JRNL REF BIOCHEMISTRY V. 47 7430 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18570440
JRNL DOI 10.1021/BI800282D
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.20 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) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 CROSS-VALIDATION METHOD : FREE R
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) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.136
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 5761
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 114654
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)) : 0.109
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.154
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 4273
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 86103
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2955
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 583
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 3302.50
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2794.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 24
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 31968
REMARK 3 NUMBER OF RESTRAINTS : 40468
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 ANGLE DISTANCES (A) : 0.031
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.030
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.069
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.077
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.019
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.051
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.115
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: AUTHORS STATE THAT THERE WERE SLIGHT
REMARK 3 MODEL CHANGES AFTER COMBINING THE TEST AND WORKING SET, SO THE
REMARK 3 FINAL R FACTOR IS LOWER THAN THE WORKING R FACTOR.
REMARK 4
REMARK 4 2OR3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-07.
REMARK 100 THE RCSB ID CODE IS RCSB041482.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : BENT GE(111)
REMARK 200 OPTICS : BENT CONICAL SI MIRROR
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 : 114729
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 22.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.70200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.040
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1P5F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG 4000, 200 MM AMMONIUM
REMARK 280 SULFATE, 50 MM SODIUM ACETATE, 2.5 MM EPIGALLOCATECHIN 3-
REMARK 280 GALLATE, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 21.95700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.41450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.88300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.41450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.95700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.88300
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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 189
REMARK 465 MET B 1
REMARK 465 ASP B 189
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 5 NH1 - CZ - NH2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG A 5 NE - CZ - NH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 48 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LYS A 89 CD - CE - NZ ANGL. DEV. = 16.6 DEGREES
REMARK 500 ASP A 131 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 GLU A 143 OE1 - CD - OE2 ANGL. DEV. = 15.5 DEGREES
REMARK 500 ARG A 145 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LYS A 188 CA - CB - CG ANGL. DEV. = 18.4 DEGREES
REMARK 500 GLU B 94 OE1 - CD - OE2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 GLU B 96 OE1 - CD - OE2 ANGL. DEV. = 8.0 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 CYS A 106 -107.43 72.50
REMARK 500 CYS B 106 -106.42 72.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 645 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH A 797 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 830 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH B 837 DISTANCE = 6.72 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 600
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P5F RELATED DB: PDB
REMARK 900 RELATED ID: 1SOA RELATED DB: PDB
DBREF 2OR3 A 1 189 UNP Q99497 PARK7_HUMAN 1 189
DBREF 2OR3 B 1 189 UNP Q99497 PARK7_HUMAN 1 189
SEQRES 1 A 189 MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES 2 A 189 ALA GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET
SEQRES 3 A 189 ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES 4 A 189 GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES 5 A 189 CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES 6 A 189 PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES 7 A 189 ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES 8 A 189 LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES 9 A 189 ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES 10 A 189 GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES 11 A 189 ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES 12 A 189 ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES 13 A 189 GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES 14 A 189 GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES 15 A 189 ALA PRO LEU VAL LEU LYS ASP
SEQRES 1 B 189 MET ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES 2 B 189 ALA GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET
SEQRES 3 B 189 ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES 4 B 189 GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES 5 B 189 CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES 6 B 189 PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES 7 B 189 ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES 8 B 189 LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES 9 B 189 ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES 10 B 189 GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES 11 B 189 ASP LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES 12 B 189 ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES 13 B 189 GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES 14 B 189 GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES 15 B 189 ALA PRO LEU VAL LEU LYS ASP
HET SO4 A 600 5
HET SO4 B 601 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *583(H2 O)
HELIX 1 1 GLU A 15 ALA A 29 1 15
HELIX 2 2 LEU A 58 GLU A 64 1 7
HELIX 3 3 GLY A 75 SER A 85 1 11
HELIX 4 4 SER A 85 ARG A 98 1 14
HELIX 5 5 GLY A 108 HIS A 115 1 8
HELIX 6 6 HIS A 126 LEU A 128 5 3
HELIX 7 7 ALA A 129 ASN A 135 1 7
HELIX 8 8 GLY A 157 GLY A 159 5 3
HELIX 9 9 THR A 160 GLY A 174 1 15
HELIX 10 10 GLY A 174 ALA A 183 1 10
HELIX 11 11 PRO A 184 VAL A 186 5 3
HELIX 12 12 GLU B 15 ALA B 29 1 15
HELIX 13 13 LEU B 58 GLU B 64 1 7
HELIX 14 14 GLY B 75 GLU B 84 1 10
HELIX 15 15 SER B 85 ARG B 98 1 14
HELIX 16 16 PRO B 109 HIS B 115 1 7
HELIX 17 17 HIS B 126 LEU B 128 5 3
HELIX 18 18 ALA B 129 ASN B 135 1 7
HELIX 19 19 GLY B 157 GLY B 159 5 3
HELIX 20 20 THR B 160 GLY B 174 1 15
HELIX 21 21 GLY B 174 ALA B 183 1 10
HELIX 22 22 PRO B 184 VAL B 186 5 3
SHEET 1 A 7 ALA A 56 SER A 57 0
SHEET 2 A 7 LYS A 32 GLY A 37 1 N GLY A 37 O ALA A 56
SHEET 3 A 7 ARG A 5 LEU A 10 1 N ALA A 6 O THR A 34
SHEET 4 A 7 VAL A 69 LEU A 72 1 O VAL A 71 N LEU A 7
SHEET 5 A 7 LEU A 101 ILE A 105 1 O ALA A 103 N VAL A 70
SHEET 6 A 7 ILE A 152 SER A 155 1 O LEU A 153 N ILE A 102
SHEET 7 A 7 VAL A 146 ASP A 149 -1 N GLU A 147 O THR A 154
SHEET 1 B 4 VAL A 44 GLN A 45 0
SHEET 2 B 4 VAL A 51 CYS A 53 -1 O ILE A 52 N VAL A 44
SHEET 3 B 4 VAL B 51 ILE B 52 -1 O VAL B 51 N CYS A 53
SHEET 4 B 4 VAL B 44 GLN B 45 -1 N VAL B 44 O ILE B 52
SHEET 1 C 2 LYS A 122 VAL A 123 0
SHEET 2 C 2 THR A 140 TYR A 141 1 O THR A 140 N VAL A 123
SHEET 1 D 7 ALA B 56 SER B 57 0
SHEET 2 D 7 LYS B 32 GLY B 37 1 N GLY B 37 O ALA B 56
SHEET 3 D 7 ARG B 5 LEU B 10 1 N LEU B 10 O ALA B 36
SHEET 4 D 7 VAL B 69 LEU B 72 1 O VAL B 71 N LEU B 7
SHEET 5 D 7 LEU B 101 ILE B 105 1 O ALA B 103 N VAL B 70
SHEET 6 D 7 ILE B 152 SER B 155 1 O LEU B 153 N ILE B 102
SHEET 7 D 7 VAL B 146 ASP B 149 -1 N GLU B 147 O THR B 154
SHEET 1 E 2 LYS B 122 VAL B 123 0
SHEET 2 E 2 THR B 140 TYR B 141 1 O THR B 140 N VAL B 123
CISPEP 1 GLY A 65 PRO A 66 0 0.52
CISPEP 2 GLY B 65 PRO B 66 0 1.98
SITE 1 AC1 6 GLU A 15 ARG A 48 GLY A 75 ASN A 76
SITE 2 AC1 6 HOH A 639 HOH A 719
SITE 1 AC2 5 ARG B 48 GLY B 75 ASN B 76 HOH B 634
SITE 2 AC2 5 HOH B 806
CRYST1 43.914 85.766 98.829 90.00 90.00 90.00 P 21 21 21 8
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 0.022772 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011660 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010118 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
