HEADER TRANSCRIPTION/DNA 04-OCT-97 2PUB
TITLE CRYSTAL STRUCTURE OF THE LACI FAMILY MEMBER, PURR, BOUND TO DNA: MINOR
TITLE 2 GROOVE BINDING BY ALPHA HELICES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-
COMPND 3 D(*TP*AP*CP*GP*CP*AP*AP*AP*CP*GP*TP*TP*TP*GP*CP*GP*T )-3');
COMPND 4 CHAIN: B;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PURINE REPRESSOR;
COMPND 8 CHAIN: A;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 4 ORGANISM_TAXID: 32630;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 7 ORGANISM_TAXID: 562;
SOURCE 8 GENE: PURR;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR: PET24A;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PDNA100
KEYWDS COMPLEX (DNA-BINDING PROTEIN-DNA), DNA-BINDING REGULATORY PROTEIN,
KEYWDS 2 TRANSCRIPTION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.G.SCHUMACHER,K.Y.CHOI,H.ZALKIN,M.A.BRENNAN
REVDAT 6 21-FEB-24 2PUB 1 REMARK
REVDAT 5 03-NOV-21 2PUB 1 REMARK SEQADV
REVDAT 4 04-APR-18 2PUB 1 REMARK
REVDAT 3 08-MAR-17 2PUB 1 AUTHOR SOURCE VERSN
REVDAT 2 24-FEB-09 2PUB 1 VERSN
REVDAT 1 06-MAY-98 2PUB 0
JRNL AUTH M.A.SCHUMACHER,K.Y.CHOI,H.ZALKIN,R.G.BRENNAN
JRNL TITL CRYSTAL STRUCTURE OF LACI MEMBER, PURR, BOUND TO DNA: MINOR
JRNL TITL 2 GROOVE BINDING BY ALPHA HELICES.
JRNL REF SCIENCE V. 266 763 1994
JRNL REFN ISSN 0036-8075
JRNL PMID 7973627
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.LU,M.A.SCHUMACHER,D.N.ARVIDSON,A.HALDIMANN,B.L.WANNER,
REMARK 1 AUTH 2 H.ZALKIN,R.G.BRENNAN
REMARK 1 TITL STRUCTURE-BASED REDESIGN OF COREPRESSOR SPECIFICITY OF THE
REMARK 1 TITL 2 ESCHERICHIA COLI PURINE REPRESSOR BY SUBSTITUTION OF RESIDUE
REMARK 1 TITL 3 190
REMARK 1 REF BIOCHEMISTRY V. 37 971 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 18609
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) : 0.171
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 : 2646
REMARK 3 NUCLEIC ACID ATOMS : 345
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 53
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 42.000
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.015 ; 1.700 ; 3092
REMARK 3 BOND ANGLES (DEGREES) : 1.704 ; 1.900 ; 4236
REMARK 3 TORSION ANGLES (DEGREES) : 20.810; 0.000 ; 1751
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : 64.340; 1.000 ; 15
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.014 ; 2.400 ; 67
REMARK 3 GENERAL PLANES (A) : 0.012 ; 3.000 ; 408
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 4.430 ; 4.900 ; 2700
REMARK 3 NON-BONDED CONTACTS (A) : 0.095 ; 19.000; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : TNT
REMARK 3 KSOL : 0.80
REMARK 3 BSOL : 150.0
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : ISOTROPIC
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2PUB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY NDB.
REMARK 100 THE DEPOSITION ID IS D_1000178519.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293.00
REMARK 200 PH : 7.40
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SDMS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18609
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.150
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
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: DIFFERENCE FOURIER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.40, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293.00K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 40.87500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.87500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 87.90500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.43500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 87.90500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.43500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 40.87500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 87.90500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.43500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 40.87500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 87.90500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 47.43500
REMARK 290 SMTRY3 8 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: THE COMPLEX LIES ON A CRYSTALLOGRAPHIC TWO-FOLD AXIS, AND
REMARK 300 ONLY ONE MONOMER-DNA HALF-SITE CONSTITUTES THE ASYMMETRIC
REMARK 300 UNIT. THE COORDINATES COMPRISE ONE REPRESSOR MONOMER AND
REMARK 300 ONE DNA STRAND FOR THE ENTIRE SITE. THE FULL COMPLEX CAN
REMARK 300 BE CONSTRUCTED BY GENERATING THE SECOND HALF USING THE
REMARK 300 CRYSTALLOGRAPHIC SYMMETRY OPERATION (X, -Y, -Z).
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THE HYDROGEN BONDS FROM ARG 190 TO THE O6 EXOCYCLIC ATOM
REMARK 400 IS WHAT DETERMINES PURR'S SPECIFICITY FOR COREPRESSORS
REMARK 400 HYPOXANTHINE AND GUANINE AND ALLOWS IT TO DISCRIMINATE
REMARK 400 AGAINST ADENINE. MUTATING ARG 190 TO ALA RESULTS IN A
REMARK 400 PURR PROTEIN WHICH CAN BIND ADENINE IN ADDITION TO
REMARK 400 HYPOXANTHINE AND GUANINE.
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 ALA A 2
REMARK 465 ARG A 341
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 DG B 702 N7 DG B 702 C8 0.052
REMARK 500 DG B 708 N7 DG B 708 C8 0.057
REMARK 500 DG B 712 N7 DG B 712 C8 0.060
REMARK 500 DG B 714 N7 DG B 714 C8 0.067
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 DC B 701 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DC B 703 O4' - C4' - C3' ANGL. DEV. = -3.9 DEGREES
REMARK 500 DC B 703 C4' - C3' - C2' ANGL. DEV. = -4.3 DEGREES
REMARK 500 DA B 704 C3' - C2' - C1' ANGL. DEV. = -5.6 DEGREES
REMARK 500 DC B 713 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 PRO A 212 C - N - CD ANGL. DEV. = -18.2 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 57 41.18 71.16
REMARK 500 TYR A 73 -73.28 -46.45
REMARK 500 SER A 124 -66.19 64.40
REMARK 500 GLU A 149 -161.82 -113.76
REMARK 500 ALA A 150 79.94 -106.24
REMARK 500 ASP A 220 30.48 -145.32
REMARK 500 PHE A 221 -5.40 66.99
REMARK 500 SER A 235 42.60 -78.82
REMARK 500 TYR A 274 129.59 -171.59
REMARK 500 ASP A 275 -41.54 132.25
REMARK 500 ARG A 278 -38.41 -30.60
REMARK 500 PRO A 293 96.93 -68.38
REMARK 500 ILE A 309 -70.87 -63.60
REMARK 500 VAL A 310 -76.01 -61.92
REMARK 500 ASN A 311 29.86 -63.86
REMARK 500 LYS A 312 57.06 25.27
REMARK 500 ARG A 328 -119.28 -120.07
REMARK 500 TYR A 339 55.66 -92.76
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 ADE A 599
DBREF 2PUB A 2 341 UNP P0ACP7 PURR_ECOLI 1 340
DBREF 2PUB B 699 715 PDB 2PUB 2PUB 699 715
SEQADV 2PUB ALA A 190 UNP P0ACP7 ARG 189 ENGINEERED MUTATION
SEQRES 1 B 17 DT DA DC DG DC DA DA DA DC DG DT DT DT
SEQRES 2 B 17 DG DC DG DT
SEQRES 1 A 340 ALA THR ILE LYS ASP VAL ALA LYS ARG ALA ASN VAL SER
SEQRES 2 A 340 THR THR THR VAL SER HIS VAL ILE ASN LYS THR ARG PHE
SEQRES 3 A 340 VAL ALA GLU GLU THR ARG ASN ALA VAL TRP ALA ALA ILE
SEQRES 4 A 340 LYS GLU LEU HIS TYR SER PRO SER ALA VAL ALA ARG SER
SEQRES 5 A 340 LEU LYS VAL ASN HIS THR LYS SER ILE GLY LEU LEU ALA
SEQRES 6 A 340 THR SER SER GLU ALA ALA TYR PHE ALA GLU ILE ILE GLU
SEQRES 7 A 340 ALA VAL GLU LYS ASN CYS PHE GLN LYS GLY TYR THR LEU
SEQRES 8 A 340 ILE LEU GLY ASN ALA TRP ASN ASN LEU GLU LYS GLN ARG
SEQRES 9 A 340 ALA TYR LEU SER MET MET ALA GLN LYS ARG VAL ASP GLY
SEQRES 10 A 340 LEU LEU VAL MET CYS SER GLU TYR PRO GLU PRO LEU LEU
SEQRES 11 A 340 ALA MET LEU GLU GLU TYR ARG HIS ILE PRO MET VAL VAL
SEQRES 12 A 340 MET ASP TRP GLY GLU ALA LYS ALA ASP PHE THR ASP ALA
SEQRES 13 A 340 VAL ILE ASP ASN ALA PHE GLU GLY GLY TYR MET ALA GLY
SEQRES 14 A 340 ARG TYR LEU ILE GLU ARG GLY HIS ARG GLU ILE GLY VAL
SEQRES 15 A 340 ILE PRO GLY PRO LEU GLU ALA ASN THR GLY ALA GLY ARG
SEQRES 16 A 340 LEU ALA GLY PHE MET LYS ALA MET GLU GLU ALA MET ILE
SEQRES 17 A 340 LYS VAL PRO GLU SER TRP ILE VAL GLN GLY ASP PHE GLU
SEQRES 18 A 340 PRO GLU SER GLY TYR ARG ALA MET GLN GLN ILE LEU SER
SEQRES 19 A 340 GLN PRO HIS ARG PRO THR ALA VAL PHE CYS GLY GLY ASP
SEQRES 20 A 340 ILE MET ALA MET GLY ALA LEU CYS ALA ALA ASP GLU MET
SEQRES 21 A 340 GLY LEU ARG VAL PRO GLN ASP VAL SER LEU ILE GLY TYR
SEQRES 22 A 340 ASP ASN VAL ARG ASN ALA ARG TYR PHE THR PRO ALA LEU
SEQRES 23 A 340 THR THR ILE HIS GLN PRO LYS ASP SER LEU GLY GLU THR
SEQRES 24 A 340 ALA PHE ASN MET LEU LEU ASP ARG ILE VAL ASN LYS ARG
SEQRES 25 A 340 GLU GLU PRO GLN SER ILE GLU VAL HIS PRO ARG LEU ILE
SEQRES 26 A 340 GLU ARG ARG SER VAL ALA ASP GLY PRO PHE ARG ASP TYR
SEQRES 27 A 340 ARG ARG
HET ADE A 599 10
HETNAM ADE ADENINE
FORMUL 3 ADE C5 H5 N5
FORMUL 4 HOH *53(H2 O)
HELIX 1 1 ILE A 4 ARG A 10 1 7
HELIX 2 2 THR A 15 ASN A 23 1 9
HELIX 3 3 GLU A 30 GLU A 42 1 13
HELIX 4 4 ALA A 49 VAL A 56 1 8
HELIX 5 5 ALA A 72 LYS A 88 1 17
HELIX 6 6 LEU A 101 GLN A 113 1 13
HELIX 7 7 GLU A 128 TYR A 137 1 10
HELIX 8 8 ALA A 162 ARG A 176 1 15
HELIX 9 9 ASN A 191 ALA A 207 1 17
HELIX 10 10 GLU A 213 TRP A 215 5 3
HELIX 11 11 PRO A 223 LEU A 234 1 12
HELIX 12 12 ASP A 248 MET A 261 1 14
HELIX 13 13 ALA A 280 TYR A 282 5 3
HELIX 14 14 LYS A 294 VAL A 310 1 17
SHEET 1 A 4 THR A 91 ASN A 96 0
SHEET 2 A 4 SER A 61 ALA A 66 1 N ILE A 62 O THR A 91
SHEET 3 A 4 GLY A 118 MET A 122 1 N GLY A 118 O GLY A 63
SHEET 4 A 4 PRO A 141 VAL A 144 1 N PRO A 141 O LEU A 119
SHEET 1 B 2 ALA A 157 ILE A 159 0
SHEET 2 B 2 SER A 318 GLU A 320 1 N ILE A 319 O ALA A 157
SHEET 1 C 3 ILE A 181 ILE A 184 0
SHEET 2 C 3 ALA A 242 CYS A 245 1 N ALA A 242 O GLY A 182
SHEET 3 C 3 SER A 270 ILE A 272 1 N SER A 270 O VAL A 243
SHEET 1 D 3 GLY A 273 ASP A 275 0
SHEET 2 D 3 THR A 289 HIS A 291 1 N ILE A 290 O GLY A 273
SHEET 3 D 3 ARG A 324 ILE A 326 -1 N ILE A 326 O THR A 289
CISPEP 1 VAL A 265 PRO A 266 0 4.44
CISPEP 2 THR A 284 PRO A 285 0 0.40
SITE 1 AC1 8 TYR A 73 PHE A 74 SER A 124 THR A 192
SITE 2 AC1 8 ARG A 196 PHE A 221 ASP A 275 HOH A 764
CRYST1 175.810 94.870 81.750 90.00 90.00 90.00 C 2 2 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 0.005688 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010541 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012232 0.00000
(ATOM LINES ARE NOT SHOWN.)
END