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full entry to diskHEADER DNA REPAIR 09-JUL-98 1BKN
TITLE CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI
TITLE 2 DNA MISMATCH REPAIR PROTEIN MUTL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MUTL;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL 40KD FRAGMENT;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 STRAIN: K-12;
SOURCE 4 PLASMID: PTX418;
SOURCE 5 GENE: MUTL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HMS174 (LAMBDA DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTX418;
SOURCE 10 EXPRESSION_SYSTEM_GENE: MUTL
KEYWDS DNA REPAIR, ATPASE, DNA BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR W.YANG,C.BAN
REVDAT 1 11-MAY-99 1BKN 0
JRNL AUTH C.BAN,W.YANG
JRNL TITL CRYSTAL STRUCTURE AND ATPASE ACTIVITY OF MUTL:
JRNL TITL 2 IMPLICATIONS FOR DNA REPAIR AND MUTAGENESIS
JRNL REF CELL(CAMBRIDGE,MASS.) V. 95 541 1998
JRNL REFN ASTM CELLB5 US ISSN 0092-8674 0998
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.9 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.9
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.00
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.001000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 19961
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 SET) : 0.248
REMARK 3 FREE R VALUE : 0.300
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.8
REMARK 3 FREE R VALUE TEST SET COUNT : 963
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.4
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3117
REMARK 3 BIN R VALUE (WORKING SET) : 0.362
REMARK 3 BIN FREE R VALUE : 0.388
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.6
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 151
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4237
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 165
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 84.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.2
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.0
REMARK 3 B22 (A**2) : 0.0
REMARK 3 B33 (A**2) : 0.0
REMARK 3 B12 (A**2) : 0.0
REMARK 3 B13 (A**2) : 0.0
REMARK 3 B23 (A**2) : 0.0
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM SIGMAA (A) : 0.65
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.51
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.73
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 0.9
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.0
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.49
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.53 ; 1.5
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.79 ; 2.0
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.77 ; 2.0
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.78 ; 2.5
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPPAR:TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BKN COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 6
REMARK 6 THE FIRST THREE RESIDUES IN THE SEQUENCE ARE NOT ENCODED BY
REMARK 6 E. COLI MUTL GENE. THEY ARE FUSED INTO MUTL PROTEIN DUE TO
REMARK 6 CLONING AND EXPRESSION.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : AUG-1997
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : R-AXIS IPII
REMARK 200 DETECTOR MANUFACTURER : MSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23519
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.7
REMARK 200 RESOLUTION RANGE LOW (A) : 20.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 4.5
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.074
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.7
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.8
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.7
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.7
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.1
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: CCP4, MAMA
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: DATA TO 2.9A ARE USED FOR THE STRUCTURE REFINEMENT.
REMARK 200 THE LAST SHELL (2.9A TO 3.0A) HAS RSYM OF 0.50,
REMARK 200 COMPLETENESS OF 98.3% AND I/SIGI OF 2.1.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BIS-TRIS PROPANE (PH
REMARK 280 6.6), 100MM MG ACETATE 100MM MGSO4 2MM DTT 20% PEG 8000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,1/2+Z
REMARK 290 6555 -X,1/2-Y,Z
REMARK 290 7555 1/2-X,Y,-Z
REMARK 290 8555 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 43.59958
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 110.84017
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.59832
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 110.84017
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.59958
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.59832
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 43.59958
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.59832
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 110.84017
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.59832
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.59958
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 110.84017
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 A 20 .. 331 B 420 .. 731 2.899
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK: THE NCS RELATIONSHIP IS NOT STRICT. THE A AND B
REMARK 295 CHAINS ARE GENERALLY RELATED BY THE ABOVE NCS MATRIX AND
REMARK 295 VECTOR.
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU B 561 CG CD1 CD2
REMARK 470 ARG B 562 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CG2 VAL B 420 CG2 VAL B 420 6855 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1BKN A PIR PH0853 1 - 19 NOT IN ATOMS LIST
REMARK 999 1BKN A PIR PH0853 332 - 918 NOT IN ATOMS LIST
REMARK 999 1BKN B PIR PH0853 1 - 19 NOT IN ATOMS LIST
REMARK 999 1BKN B PIR PH0853 332 - 918 NOT IN ATOMS LIST
REMARK 999
REMARK 999 THE FIRST 3 RESIDUES IN THE SEQUENCE (GLY-SER-HIS) ARE
REMARK 999 FROM A CLONING-EXPRESSION VECTOR. THEY ARE NOT ENCODED BY
REMARK 999 THE E. COLI MUTL GENE. THERE ARE SIX DISORDERED LOOPS,
REMARK 999 INCLUDING THE N- AND C-TERMINI, IN THE CRYSTAL STRUCTURE
REMARK 999 OF MUTL.
DBREF 1BKN A 20 73 PIR PH0853 PH0853 20 73
DBREF 1BKN A 80 125 PIR PH0853 PH0853 80 125
DBREF 1BKN A 132 149 PIR PH0853 PH0853 132 149
DBREF 1BKN A 163 299 PIR PH0853 PH0853 163 299
DBREF 1BKN A 315 331 PIR PH0853 PH0853 315 331
DBREF 1BKN B 420 473 PIR PH0853 PH0853 20 73
DBREF 1BKN B 487 524 PIR PH0853 PH0853 87 124
DBREF 1BKN B 530 550 PIR PH0853 PH0853 130 150
DBREF 1BKN B 561 699 PIR PH0853 PH0853 161 299
DBREF 1BKN B 713 731 PIR PH0853 PH0853 313 331
SEQADV 1BKN A PIR PH0853 ARG 74 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 HIS 75 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ALA 76 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 THR 77 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 SER 78 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 LYS 79 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 GLU 126 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 GLY 127 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ARG 128 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ASP 129 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 MET 130 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ASN 131 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 LEU 150 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 PHE 151 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 TYR 152 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ASN 153 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 THR 154 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 PRO 155 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ALA 156 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ARG 157 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ARG 158 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 LYS 159 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 PHE 160 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 LEU 161 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ARG 162 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ASP 300 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 VAL 301 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ASN 302 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 VAL 303 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 HIS 304 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 PRO 305 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ALA 306 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 LYS 307 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 HIS 308 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 GLU 309 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 VAL 310 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 ARG 311 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 PHE 312 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 HIS 313 GAP IN PDB ENTRY
SEQADV 1BKN A PIR PH0853 GLN 314 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ARG 74 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 HIS 75 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ALA 76 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 THR 77 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 SER 78 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 LYS 79 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ILE 80 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ALA 81 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 SER 82 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 LEU 83 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ASP 84 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ASP 85 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 LEU 86 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ALA 125 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 GLU 126 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 GLY 127 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ARG 128 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ASP 129 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 PHE 151 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 TYR 152 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ASN 153 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 THR 154 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 PRO 155 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ALA 156 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ARG 157 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ARG 158 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 LYS 159 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 PHE 160 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ASP 300 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 VAL 301 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ASN 302 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 VAL 303 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 HIS 304 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 PRO 305 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ALA 306 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 LYS 307 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 HIS 308 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 GLU 309 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 VAL 310 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 ARG 311 GAP IN PDB ENTRY
SEQADV 1BKN B PIR PH0853 PHE 312 GAP IN PDB ENTRY
SEQRES 1 A 352 GLY SER HIS MET PRO ILE GLN VAL LEU PRO PRO GLN LEU
SEQRES 2 A 352 ALA ASN GLN ILE ALA ALA GLY GLU VAL VAL GLU ARG PRO
SEQRES 3 A 352 ALA SER VAL VAL LYS GLU LEU VAL GLU ASN SER LEU ASP
SEQRES 4 A 352 ALA GLY ALA THR ARG ILE ASP ILE ASP ILE GLU ARG GLY
SEQRES 5 A 352 GLY ALA LYS LEU ILE ARG ILE ARG ASP ASN GLY CYS GLY
SEQRES 6 A 352 ILE LYS LYS ASP GLU LEU ALA LEU ALA LEU ALA ARG HIS
SEQRES 7 A 352 ALA THR SER LYS ILE ALA SER LEU ASP ASP LEU GLU ALA
SEQRES 8 A 352 ILE ILE SER LEU GLY PHE ARG GLY GLU ALA LEU ALA SER
SEQRES 9 A 352 ILE SER SER VAL SER ARG LEU THR LEU THR SER ARG THR
SEQRES 10 A 352 ALA GLU GLN GLN GLU ALA TRP GLN ALA TYR ALA GLU GLY
SEQRES 11 A 352 ARG ASP MET ASN VAL THR VAL LYS PRO ALA ALA HIS PRO
SEQRES 12 A 352 VAL GLY THR THR LEU GLU VAL LEU ASP LEU PHE TYR ASN
SEQRES 13 A 352 THR PRO ALA ARG ARG LYS PHE LEU ARG THR GLU LYS THR
SEQRES 14 A 352 GLU PHE ASN HIS ILE ASP GLU ILE ILE ARG ARG ILE ALA
SEQRES 15 A 352 LEU ALA ARG PHE ASP VAL THR ILE ASN LEU SER HIS ASN
SEQRES 16 A 352 GLY LYS ILE VAL ARG GLN TYR ARG ALA VAL PRO GLU GLY
SEQRES 17 A 352 GLY GLN LYS GLU ARG ARG LEU GLY ALA ILE CYS GLY THR
SEQRES 18 A 352 ALA PHE LEU GLU GLN ALA LEU ALA ILE GLU TRP GLN HIS
SEQRES 19 A 352 GLY ASP LEU THR LEU ARG GLY TRP VAL ALA ASP PRO ASN
SEQRES 20 A 352 HIS THR THR PRO ALA LEU ALA GLU ILE GLN TYR CYS TYR
SEQRES 21 A 352 VAL ASN GLY ARG MET MET ARG ASP ARG LEU ILE ASN HIS
SEQRES 22 A 352 ALA ILE ARG GLN ALA CYS GLU ASP LYS LEU GLY ALA ASP
SEQRES 23 A 352 GLN GLN PRO ALA PHE VAL LEU TYR LEU GLU ILE ASP PRO
SEQRES 24 A 352 HIS GLN VAL ASP VAL ASN VAL HIS PRO ALA LYS HIS GLU
SEQRES 25 A 352 VAL ARG PHE HIS GLN SER ARG LEU VAL HIS ASP PHE ILE
SEQRES 26 A 352 TYR GLN GLY VAL LEU SER VAL LEU GLN GLN GLN LEU GLU
SEQRES 27 A 352 THR PRO LEU PRO LEU ASP ASP GLU PRO GLN PRO ALA PRO
SEQRES 28 A 352 ARG
SEQRES 1 B 352 GLY SER HIS MET PRO ILE GLN VAL LEU PRO PRO GLN LEU
SEQRES 2 B 352 ALA ASN GLN ILE ALA ALA GLY GLU VAL VAL GLU ARG PRO
SEQRES 3 B 352 ALA SER VAL VAL LYS GLU LEU VAL GLU ASN SER LEU ASP
SEQRES 4 B 352 ALA GLY ALA THR ARG ILE ASP ILE ASP ILE GLU ARG GLY
SEQRES 5 B 352 GLY ALA LYS LEU ILE ARG ILE ARG ASP ASN GLY CYS GLY
SEQRES 6 B 352 ILE LYS LYS ASP GLU LEU ALA LEU ALA LEU ALA ARG HIS
SEQRES 7 B 352 ALA THR SER LYS ILE ALA SER LEU ASP ASP LEU GLU ALA
SEQRES 8 B 352 ILE ILE SER LEU GLY PHE ARG GLY GLU ALA LEU ALA SER
SEQRES 9 B 352 ILE SER SER VAL SER ARG LEU THR LEU THR SER ARG THR
SEQRES 10 B 352 ALA GLU GLN GLN GLU ALA TRP GLN ALA TYR ALA GLU GLY
SEQRES 11 B 352 ARG ASP MET ASN VAL THR VAL LYS PRO ALA ALA HIS PRO
SEQRES 12 B 352 VAL GLY THR THR LEU GLU VAL LEU ASP LEU PHE TYR ASN
SEQRES 13 B 352 THR PRO ALA ARG ARG LYS PHE LEU ARG THR GLU LYS THR
SEQRES 14 B 352 GLU PHE ASN HIS ILE ASP GLU ILE ILE ARG ARG ILE ALA
SEQRES 15 B 352 LEU ALA ARG PHE ASP VAL THR ILE ASN LEU SER HIS ASN
SEQRES 16 B 352 GLY LYS ILE VAL ARG GLN TYR ARG ALA VAL PRO GLU GLY
SEQRES 17 B 352 GLY GLN LYS GLU ARG ARG LEU GLY ALA ILE CYS GLY THR
SEQRES 18 B 352 ALA PHE LEU GLU GLN ALA LEU ALA ILE GLU TRP GLN HIS
SEQRES 19 B 352 GLY ASP LEU THR LEU ARG GLY TRP VAL ALA ASP PRO ASN
SEQRES 20 B 352 HIS THR THR PRO ALA LEU ALA GLU ILE GLN TYR CYS TYR
SEQRES 21 B 352 VAL ASN GLY ARG MET MET ARG ASP ARG LEU ILE ASN HIS
SEQRES 22 B 352 ALA ILE ARG GLN ALA CYS GLU ASP LYS LEU GLY ALA ASP
SEQRES 23 B 352 GLN GLN PRO ALA PHE VAL LEU TYR LEU GLU ILE ASP PRO
SEQRES 24 B 352 HIS GLN VAL ASP VAL ASN VAL HIS PRO ALA LYS HIS GLU
SEQRES 25 B 352 VAL ARG PHE HIS GLN SER ARG LEU VAL HIS ASP PHE ILE
SEQRES 26 B 352 TYR GLN GLY VAL LEU SER VAL LEU GLN GLN GLN LEU GLU
SEQRES 27 B 352 THR PRO LEU PRO LEU ASP ASP GLU PRO GLN PRO ALA PRO
SEQRES 28 B 352 ARG
FORMUL 3 HOH *55(H2 O1)
HELIX 1 1 PRO A 23 ASP A 36 1 14
HELIX 2 2 LYS A 65 LEU A 72 1 8
HELIX 3 3 ALA A 81 LEU A 86 5 6
HELIX 4 4 ILE A 90 LEU A 92 5 3
HELIX 5 5 PHE A 94 VAL A 105 1 12
HELIX 6 6 THR A 166 ALA A 181 1 16
HELIX 7 7 LYS A 208 GLN A 223 1 16
HELIX 8 8 PRO A 243 HIS A 245 5 3
HELIX 9 9 LEU A 250 GLU A 252 5 3
HELIX 10 10 ARG A 266 LYS A 279 1 14
HELIX 11 11 ARG A 316 VAL A 329 1 14
HELIX 12 12 PRO B 423 ASP B 436 1 14
HELIX 13 13 LYS B 465 LEU B 472 1 8
HELIX 14 14 ILE B 490 LEU B 492 5 3
HELIX 15 15 PHE B 494 VAL B 505 1 12
HELIX 16 16 LYS B 565 ALA B 581 1 17
HELIX 17 17 LYS B 608 GLN B 623 1 16
HELIX 18 18 PRO B 643 HIS B 645 5 3
HELIX 19 19 LEU B 650 GLU B 652 5 3
HELIX 20 20 ARG B 666 LYS B 679 1 14
HELIX 21 21 ARG B 716 VAL B 729 1 14
SHEET 1 A 6 THR A 109 SER A 112 0
SHEET 2 A 6 THR A 143 GLU A 146 -1 N GLU A 146 O THR A 109
SHEET 3 A 6 LEU A 53 ASP A 58 -1 N ASP A 58 O THR A 143
SHEET 4 A 6 ARG A 41 GLU A 47 -1 N GLU A 47 O LEU A 53
SHEET 5 A 6 THR A 186 HIS A 191 1 N THR A 186 O ILE A 42
SHEET 6 A 6 LYS A 194 TYR A 199 -1 N TYR A 199 O ILE A 187
SHEET 1 B 2 ALA A 120 GLN A 122 0
SHEET 2 B 2 LYS A 135 ALA A 137 -1 N ALA A 137 O ALA A 120
SHEET 1 C 5 ALA A 224 HIS A 231 0
SHEET 2 C 5 LEU A 234 ALA A 241 -1 N VAL A 240 O LEU A 225
SHEET 3 C 5 PHE A 288 GLU A 293 -1 N GLU A 293 O THR A 235
SHEET 4 C 5 GLN A 254 VAL A 258 1 N TYR A 255 O PHE A 288
SHEET 5 C 5 ARG A 261 MET A 263 -1 N MET A 263 O CYS A 256
SHEET 1 D 4 LEU B 453 ASP B 458 0
SHEET 2 D 4 ARG B 441 GLU B 447 -1 N GLU B 447 O LEU B 453
SHEET 3 D 4 THR B 586 HIS B 591 1 N THR B 586 O ILE B 442
SHEET 4 D 4 LYS B 594 TYR B 599 -1 N TYR B 599 O ILE B 587
SHEET 1 E 2 THR B 509 ARG B 513 0
SHEET 2 E 2 GLY B 542 GLU B 546 -1 N GLU B 546 O THR B 509
SHEET 1 F 2 ALA B 520 GLN B 522 0
SHEET 2 F 2 LYS B 535 ALA B 537 -1 N ALA B 537 O ALA B 520
SHEET 1 G 5 ALA B 624 HIS B 631 0
SHEET 2 G 5 LEU B 634 ALA B 641 -1 N VAL B 640 O LEU B 625
SHEET 3 G 5 PHE B 688 GLU B 693 -1 N GLU B 693 O THR B 635
SHEET 4 G 5 GLN B 654 VAL B 658 1 N TYR B 655 O PHE B 688
SHEET 5 G 5 ARG B 661 MET B 663 -1 N MET B 663 O CYS B 656
CRYST1 87.200 93.200 221.700 90.00 90.00 90.00 I 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 0.011468 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010730 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004511 0.00000
MTRIX1 1 0.041784 0.989309 -0.139721 68.73042 1
MTRIX2 1 0.999101 -0.040365 0.012974 -63.03986 1
MTRIX3 1 0.007196 -0.140137 -0.990106 173.24435 1
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