HEADER DNA-BINDING REGULATORY PROTEIN 13-FEB-96 1DBQ
TITLE DNA-BINDING REGULATORY PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PURINE REPRESSOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: COREPRESSOR-FREE COREPRESSOR-BINDING DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS TRANSCRIPTION REGULATION, DNA-BINDING REGULATORY PROTEIN, PURINE
KEYWDS 2 REPRESSOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.SCHUMACHER,K.Y.CHOI,F.LU,H.ZALKIN,R.G.BRENNAN
REVDAT 3 07-FEB-24 1DBQ 1 REMARK LINK
REVDAT 2 24-FEB-09 1DBQ 1 VERSN
REVDAT 1 07-DEC-96 1DBQ 0
JRNL AUTH M.A.SCHUMACHER,K.Y.CHOI,F.LU,H.ZALKIN,R.G.BRENNAN
JRNL TITL MECHANISM OF COREPRESSOR-MEDIATED SPECIFIC DNA BINDING BY
JRNL TITL 2 THE PURINE REPRESSOR.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 83 147 1995
JRNL REFN ISSN 0092-8674
JRNL PMID 7553867
JRNL DOI 10.1016/0092-8674(95)90243-0
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 25876
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.156
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 : 4344
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 244
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) : 0.018 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.790 ; 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 1DBQ 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_1000172724.
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 (%): 44.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 62.63000
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 300 REMARK: AS FOR FULL LENGTH PURINE REPRESSOR, THE COREPRESSOR
REMARK 300 BINDING DOMAIN IS DIMERIC AND THE ENTRY CONTAINS TWO
REMARK 300 MONOMERS IN THE ASU. THE CHAIN IDENTIFIERS ARE A AND B.
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: 3260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 SER A 53
REMARK 465 LEU A 54
REMARK 465 LYS A 55
REMARK 465 VAL A 56
REMARK 465 ASN A 57
REMARK 465 HIS A 58
REMARK 465 THR A 59
REMARK 465 LEU A 188
REMARK 465 GLU A 189
REMARK 465 ARG A 190
REMARK 465 ASN A 191
REMARK 465 THR A 192
REMARK 465 GLY A 193
REMARK 465 SER B 53
REMARK 465 LEU B 54
REMARK 465 LYS B 55
REMARK 465 VAL B 56
REMARK 465 ASN B 57
REMARK 465 HIS B 58
REMARK 465 THR B 59
REMARK 465 LEU B 188
REMARK 465 GLU B 189
REMARK 465 ARG B 190
REMARK 465 ASN B 191
REMARK 465 THR B 192
REMARK 465 GLY B 193
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 76 CG GLU A 76 CD 0.090
REMARK 500 SER A 330 CB SER A 330 OG 0.080
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 105 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 GLY A 148 C - N - CA ANGL. DEV. = -15.2 DEGREES
REMARK 500 MET A 204 CG - SD - CE ANGL. DEV. = 11.9 DEGREES
REMARK 500 ASP A 338 N - CA - CB ANGL. DEV. = 11.3 DEGREES
REMARK 500 TYR A 339 N - CA - CB ANGL. DEV. = 14.0 DEGREES
REMARK 500 TYR A 339 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 PRO B 187 C - N - CD ANGL. DEV. = -28.1 DEGREES
REMARK 500 GLY B 195 N - CA - C ANGL. DEV. = -15.9 DEGREES
REMARK 500 MET B 204 CG - SD - CE ANGL. DEV. = -13.8 DEGREES
REMARK 500 PRO B 323 C - N - CD ANGL. DEV. = -14.6 DEGREES
REMARK 500 ASP B 338 N - CA - CB ANGL. DEV. = 16.2 DEGREES
REMARK 500 ASP B 338 CA - C - N ANGL. DEV. = -14.0 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 ASN A 99 16.04 108.55
REMARK 500 SER A 124 -33.57 62.37
REMARK 500 ASN A 161 68.92 -103.83
REMARK 500 PHE A 221 -28.34 84.69
REMARK 500 ASP A 275 -55.96 124.85
REMARK 500 ASN A 276 57.14 74.24
REMARK 500 LYS A 312 84.03 -44.82
REMARK 500 GLU A 314 44.36 -97.90
REMARK 500 ARG A 328 -113.11 -113.18
REMARK 500 PHE A 336 21.23 -76.81
REMARK 500 ASP A 338 65.31 -163.91
REMARK 500 ARG A 340 -164.70 159.28
REMARK 500 SER B 68 103.55 164.42
REMARK 500 ALA B 72 -31.24 -32.96
REMARK 500 TYR B 73 -74.57 -62.64
REMARK 500 PHE B 74 -70.95 -54.63
REMARK 500 ALA B 75 -69.32 10.03
REMARK 500 GLU B 82 -71.45 -58.33
REMARK 500 ALA B 97 -125.18 -68.67
REMARK 500 TRP B 98 31.08 143.54
REMARK 500 ASN B 99 75.10 70.37
REMARK 500 ARG B 115 64.54 37.55
REMARK 500 ASP B 117 37.06 -88.95
REMARK 500 LEU B 120 116.37 -169.43
REMARK 500 TYR B 126 56.33 -155.19
REMARK 500 GLU B 149 97.38 -19.75
REMARK 500 ALA B 152 83.15 -59.47
REMARK 500 ASP B 153 -102.70 -127.83
REMARK 500 PHE B 154 14.09 -165.00
REMARK 500 ASN B 161 64.64 -111.93
REMARK 500 MET B 208 31.80 72.47
REMARK 500 PHE B 221 -11.56 101.64
REMARK 500 ASP B 275 -57.14 133.31
REMARK 500 ASN B 276 63.45 71.66
REMARK 500 PRO B 293 92.22 -53.63
REMARK 500 SER B 296 -34.61 -148.73
REMARK 500 LEU B 306 -71.22 -53.42
REMARK 500 VAL B 310 -81.36 -78.95
REMARK 500 ASN B 311 -5.66 -52.70
REMARK 500 PRO B 316 174.96 -55.03
REMARK 500 ARG B 328 -124.76 -139.08
REMARK 500 PHE B 336 53.23 -93.37
REMARK 500 TYR B 339 103.45 136.35
REMARK 500 ARG B 340 170.77 78.99
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 MG A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 3
DBREF 1DBQ A 53 341 UNP P0ACP7 PURR_ECOLI 52 340
DBREF 1DBQ B 53 341 UNP P0ACP7 PURR_ECOLI 52 340
SEQRES 1 A 289 SER LEU LYS VAL ASN HIS THR LYS SER ILE GLY LEU LEU
SEQRES 2 A 289 ALA THR SER SER GLU ALA ALA TYR PHE ALA GLU ILE ILE
SEQRES 3 A 289 GLU ALA VAL GLU LYS ASN CYS PHE GLN LYS GLY TYR THR
SEQRES 4 A 289 LEU ILE LEU GLY ASN ALA TRP ASN ASN LEU GLU LYS GLN
SEQRES 5 A 289 ARG ALA TYR LEU SER MET MET ALA GLN LYS ARG VAL ASP
SEQRES 6 A 289 GLY LEU LEU VAL MET CYS SER GLU TYR PRO GLU PRO LEU
SEQRES 7 A 289 LEU ALA MET LEU GLU GLU TYR ARG HIS ILE PRO MET VAL
SEQRES 8 A 289 VAL MET ASP TRP GLY GLU ALA LYS ALA ASP PHE THR ASP
SEQRES 9 A 289 ALA VAL ILE ASP ASN ALA PHE GLU GLY GLY TYR MET ALA
SEQRES 10 A 289 GLY ARG TYR LEU ILE GLU ARG GLY HIS ARG GLU ILE GLY
SEQRES 11 A 289 VAL ILE PRO GLY PRO LEU GLU ARG ASN THR GLY ALA GLY
SEQRES 12 A 289 ARG LEU ALA GLY PHE MET LYS ALA MET GLU GLU ALA MET
SEQRES 13 A 289 ILE LYS VAL PRO GLU SER TRP ILE VAL GLN GLY ASP PHE
SEQRES 14 A 289 GLU PRO GLU SER GLY TYR ARG ALA MET GLN GLN ILE LEU
SEQRES 15 A 289 SER GLN PRO HIS ARG PRO THR ALA VAL PHE CYS GLY GLY
SEQRES 16 A 289 ASP ILE MET ALA MET GLY ALA LEU CYS ALA ALA ASP GLU
SEQRES 17 A 289 MET GLY LEU ARG VAL PRO GLN ASP VAL SER LEU ILE GLY
SEQRES 18 A 289 TYR ASP ASN VAL ARG ASN ALA ARG TYR PHE THR PRO ALA
SEQRES 19 A 289 LEU THR THR ILE HIS GLN PRO LYS ASP SER LEU GLY GLU
SEQRES 20 A 289 THR ALA PHE ASN MET LEU LEU ASP ARG ILE VAL ASN LYS
SEQRES 21 A 289 ARG GLU GLU PRO GLN SER ILE GLU VAL HIS PRO ARG LEU
SEQRES 22 A 289 ILE GLU ARG ARG SER VAL ALA ASP GLY PRO PHE ARG ASP
SEQRES 23 A 289 TYR ARG ARG
SEQRES 1 B 289 SER LEU LYS VAL ASN HIS THR LYS SER ILE GLY LEU LEU
SEQRES 2 B 289 ALA THR SER SER GLU ALA ALA TYR PHE ALA GLU ILE ILE
SEQRES 3 B 289 GLU ALA VAL GLU LYS ASN CYS PHE GLN LYS GLY TYR THR
SEQRES 4 B 289 LEU ILE LEU GLY ASN ALA TRP ASN ASN LEU GLU LYS GLN
SEQRES 5 B 289 ARG ALA TYR LEU SER MET MET ALA GLN LYS ARG VAL ASP
SEQRES 6 B 289 GLY LEU LEU VAL MET CYS SER GLU TYR PRO GLU PRO LEU
SEQRES 7 B 289 LEU ALA MET LEU GLU GLU TYR ARG HIS ILE PRO MET VAL
SEQRES 8 B 289 VAL MET ASP TRP GLY GLU ALA LYS ALA ASP PHE THR ASP
SEQRES 9 B 289 ALA VAL ILE ASP ASN ALA PHE GLU GLY GLY TYR MET ALA
SEQRES 10 B 289 GLY ARG TYR LEU ILE GLU ARG GLY HIS ARG GLU ILE GLY
SEQRES 11 B 289 VAL ILE PRO GLY PRO LEU GLU ARG ASN THR GLY ALA GLY
SEQRES 12 B 289 ARG LEU ALA GLY PHE MET LYS ALA MET GLU GLU ALA MET
SEQRES 13 B 289 ILE LYS VAL PRO GLU SER TRP ILE VAL GLN GLY ASP PHE
SEQRES 14 B 289 GLU PRO GLU SER GLY TYR ARG ALA MET GLN GLN ILE LEU
SEQRES 15 B 289 SER GLN PRO HIS ARG PRO THR ALA VAL PHE CYS GLY GLY
SEQRES 16 B 289 ASP ILE MET ALA MET GLY ALA LEU CYS ALA ALA ASP GLU
SEQRES 17 B 289 MET GLY LEU ARG VAL PRO GLN ASP VAL SER LEU ILE GLY
SEQRES 18 B 289 TYR ASP ASN VAL ARG ASN ALA ARG TYR PHE THR PRO ALA
SEQRES 19 B 289 LEU THR THR ILE HIS GLN PRO LYS ASP SER LEU GLY GLU
SEQRES 20 B 289 THR ALA PHE ASN MET LEU LEU ASP ARG ILE VAL ASN LYS
SEQRES 21 B 289 ARG GLU GLU PRO GLN SER ILE GLU VAL HIS PRO ARG LEU
SEQRES 22 B 289 ILE GLU ARG ARG SER VAL ALA ASP GLY PRO PHE ARG ASP
SEQRES 23 B 289 TYR ARG ARG
HET MG A 1 1
HET MG A 2 1
HET MG B 3 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG 3(MG 2+)
FORMUL 6 HOH *244(H2 O)
HELIX 1 1 ALA A 72 LYS A 88 1 17
HELIX 2 2 LEU A 101 GLN A 113 1 13
HELIX 3 3 GLU A 128 TYR A 137 1 10
HELIX 4 4 ALA A 162 GLU A 175 1 14
HELIX 5 5 GLY A 195 ALA A 207 1 13
HELIX 6 6 GLU A 213 TRP A 215 5 3
HELIX 7 7 PRO A 223 LEU A 234 1 12
HELIX 8 8 ASP A 248 MET A 261 1 14
HELIX 9 9 ALA A 280 TYR A 282 5 3
HELIX 10 10 ASP A 295 VAL A 310 1 16
HELIX 11 11 GLU B 76 LYS B 88 1 13
HELIX 12 12 LYS B 103 GLN B 113 1 11
HELIX 13 13 GLU B 128 GLU B 136 1 9
HELIX 14 14 ALA B 162 GLU B 175 1 14
HELIX 15 15 GLY B 195 ALA B 207 1 13
HELIX 16 16 GLU B 213 TRP B 215 5 3
HELIX 17 17 PRO B 223 LEU B 234 1 12
HELIX 18 18 ASP B 248 MET B 261 1 14
HELIX 19 19 ALA B 280 TYR B 282 5 3
HELIX 20 20 LEU B 297 ILE B 309 1 13
SHEET 1 A 6 MET A 142 MET A 145 0
SHEET 2 A 6 GLY A 118 MET A 122 1 N LEU A 119 O VAL A 143
SHEET 3 A 6 SER A 61 ALA A 66 1 N GLY A 63 O GLY A 118
SHEET 4 A 6 THR A 91 ASN A 96 1 N THR A 91 O ILE A 62
SHEET 5 A 6 THR B 91 ASN B 96 -1 N LEU B 94 O LEU A 92
SHEET 6 A 6 SER B 61 ALA B 66 1 N ILE B 62 O THR B 91
SHEET 1 B 2 ALA A 157 ASP A 160 0
SHEET 2 B 2 SER A 318 VAL A 321 1 N ILE A 319 O ALA A 157
SHEET 1 C 5 ILE A 181 ILE A 184 0
SHEET 2 C 5 ALA A 242 CYS A 245 1 N ALA A 242 O GLY A 182
SHEET 3 C 5 SER A 270 ASP A 275 1 N SER A 270 O VAL A 243
SHEET 4 C 5 THR A 288 HIS A 291 1 N THR A 288 O GLY A 273
SHEET 5 C 5 ARG A 324 ILE A 326 -1 N ILE A 326 O THR A 289
SHEET 1 D 2 MET B 145 TRP B 147 0
SHEET 2 D 2 ASP B 156 VAL B 158 1 N ASP B 156 O ASP B 146
SHEET 1 E 5 ILE B 181 ILE B 184 0
SHEET 2 E 5 ALA B 242 CYS B 245 1 N ALA B 242 O GLY B 182
SHEET 3 E 5 SER B 270 ASP B 275 1 N SER B 270 O VAL B 243
SHEET 4 E 5 THR B 288 HIS B 291 1 N THR B 288 O GLY B 273
SHEET 5 E 5 ARG B 324 ILE B 326 -1 N ILE B 326 O THR B 289
LINK MG MG A 2 O HOH A 409 1555 1656 2.41
LINK MG MG B 3 O HOH B 393 1555 1555 3.06
CISPEP 1 VAL A 265 PRO A 266 0 0.13
CISPEP 2 THR A 284 PRO A 285 0 -1.39
CISPEP 3 VAL B 265 PRO B 266 0 1.59
CISPEP 4 THR B 284 PRO B 285 0 3.14
SITE 1 AC1 1 HOH A 409
SITE 1 AC2 1 HOH B 393
CRYST1 38.040 125.260 61.290 90.00 100.17 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 0.026288 0.000000 0.004716 0.00000
SCALE2 0.000000 0.007983 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016576 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
