HEADER MEMBRANE PROTEIN 24-JAN-03 1NRF
TITLE C-TERMINAL DOMAIN OF THE BACILLUS LICHENIFORMIS BLAR PENICILLIN-
TITLE 2 RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REGULATORY PROTEIN BLAR1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS;
SOURCE 3 ORGANISM_TAXID: 1402;
SOURCE 4 STRAIN: 749-I;
SOURCE 5 GENE: BLAR1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PIN3-OMPA
KEYWDS PENICILLIN-RECEPTOR, BETA-LACTAMASE INDUCTION, BACILLUS
KEYWDS 2 LICHENIFORMIS, PENICILLIN-BINDING PROTEIN, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.KERFF,P.CHARLIER,M.L.COLUMBO,E.SAUVAGE,A.BRANS,J.M.FRERE,B.JORIS,
AUTHOR 2 E.FONZE
REVDAT 4 03-APR-24 1NRF 1 REMARK
REVDAT 3 13-MAR-24 1NRF 1 SEQADV
REVDAT 2 24-FEB-09 1NRF 1 VERSN
REVDAT 1 24-JAN-04 1NRF 0
JRNL AUTH F.KERFF,P.CHARLIER,M.L.COLOMBO,E.SAUVAGE,A.BRANS,J.M.FRERE,
JRNL AUTH 2 B.JORIS,E.FONZE
JRNL TITL CRYSTAL STRUCTURE OF THE SENSOR DOMAIN OF THE BLAR
JRNL TITL 2 PENICILLIN RECEPTOR FROM BACILLUS LICHENIFORMIS.
JRNL REF BIOCHEMISTRY V. 42 12835 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14596597
JRNL DOI 10.1021/BI034976A
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.HARDT,B.JORIS,S.LEPAGE,R.BRASSEUR,J.O.LAMPEN,J.M.FRERE,
REMARK 1 AUTH 2 A.L.FINK,J.M.GHUYSEN
REMARK 1 TITL THE PENICILLIN SENSORY TRANSDUCER, BLAR, INVOLVED IN THE
REMARK 1 TITL 2 INDUCIBILITY OF BETA-LACTAMASE SYNTHESIS IN BACILLUS
REMARK 1 TITL 3 LICHENIFORMIS IS EMBEDDED IN THE PLASMA MEMBRANE VIA A
REMARK 1 TITL 4 FOUR-ALPHA-HELIX BUNDLE
REMARK 1 REF MOL.MICROBIOL. V. 23 935 1997
REMARK 1 REFN ISSN 0950-382X
REMARK 1 PMID 9076730
REMARK 1 DOI 10.1046/J.1365-2958.1997.2761642.X
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 8827
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) : 0.204
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 442
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.012
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1284
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE : 0.3120
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 77
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.036
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1990
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 81
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.85000
REMARK 3 B22 (A**2) : 1.85000
REMARK 3 B33 (A**2) : -3.69000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
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) : 1.720 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.790 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.950 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 53.74
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NRF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000018140.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-SEP-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.95
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9979
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.440
REMARK 200 RESOLUTION RANGE LOW (A) : 32.444
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.23200
REMARK 200 R SYM FOR SHELL (I) : 0.20100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: CLASS D BETA-LACTAMASE OXA-2 FROM SALMONELLA
REMARK 200 TYPHIMURIUM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 8000, 5% GLYCEROL, 50MM CACL2
REMARK 280 IN 0.1M CACODYLATE, PH 6.95, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
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 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 65.09900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 32.54950
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 97.64850
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLN A 340
REMARK 465 GLU A 341
REMARK 465 GLY A 342
REMARK 465 THR A 343
REMARK 465 SER A 344
REMARK 465 PRO A 345
REMARK 465 MET A 346
REMARK 465 GLN A 347
REMARK 465 LYS A 348
REMARK 465 GLU A 349
REMARK 465 THR A 350
REMARK 465 ARG A 351
REMARK 465 SER A 598
REMARK 465 VAL A 599
REMARK 465 SER A 600
REMARK 465 ARG A 601
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 C ASN A 546 CA GLY A 547 1.64
REMARK 500 CA ASN A 546 N GLY A 547 1.68
REMARK 500 O VAL A 544 N ILE A 545 1.73
REMARK 500
REMARK 500 REMARK: NULL
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 VAL A 544 C ILE A 545 N -0.201
REMARK 500 ASN A 546 C GLY A 547 N -0.238
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 VAL A 544 O - C - N ANGL. DEV. = -29.0 DEGREES
REMARK 500 ASN A 546 CA - C - N ANGL. DEV. = -38.9 DEGREES
REMARK 500 ASN A 546 O - C - N ANGL. DEV. = 30.9 DEGREES
REMARK 500 GLY A 547 C - N - CA ANGL. DEV. = -43.9 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 390 79.83 63.90
REMARK 500 ALA A 401 -149.04 54.54
REMARK 500 ASP A 428 -73.96 -36.78
REMARK 500 PRO A 433 -6.69 -58.95
REMARK 500 THR A 451 94.44 -67.67
REMARK 500 HIS A 475 67.49 39.75
REMARK 500 SER A 482 -81.42 -105.68
REMARK 500 ASP A 486 17.85 -147.15
REMARK 500 LEU A 489 -35.33 -130.32
REMARK 500 ASN A 532 -89.14 38.33
REMARK 500 ASN A 546 -112.16 -169.39
REMARK 500 GLU A 548 37.76 -77.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL A 544 34.33
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NRF A 346 601 UNP P12287 BLAR_BACLI 346 601
SEQADV 1NRF GLN A 340 UNP P12287 CLONING ARTIFACT
SEQADV 1NRF GLU A 341 UNP P12287 CLONING ARTIFACT
SEQADV 1NRF GLY A 342 UNP P12287 CLONING ARTIFACT
SEQADV 1NRF THR A 343 UNP P12287 CLONING ARTIFACT
SEQADV 1NRF SER A 344 UNP P12287 CLONING ARTIFACT
SEQADV 1NRF PRO A 345 UNP P12287 CLONING ARTIFACT
SEQRES 1 A 262 GLN GLU GLY THR SER PRO MET GLN LYS GLU THR ARG PHE
SEQRES 2 A 262 LEU PRO GLY THR ASN VAL GLU TYR GLU ASP TYR SER THR
SEQRES 3 A 262 PHE PHE ASP LYS PHE SER ALA SER GLY GLY PHE VAL LEU
SEQRES 4 A 262 PHE ASN SER ASN ARG LYS LYS TYR THR ILE TYR ASN ARG
SEQRES 5 A 262 LYS GLU SER THR SER ARG PHE ALA PRO ALA SER THR TYR
SEQRES 6 A 262 LYS VAL PHE SER ALA LEU LEU ALA LEU GLU SER GLY ILE
SEQRES 7 A 262 ILE THR LYS ASN ASP SER HIS MET THR TRP ASP GLY THR
SEQRES 8 A 262 GLN TYR PRO TYR LYS GLU TRP ASN GLN ASP GLN ASP LEU
SEQRES 9 A 262 PHE SER ALA MET SER SER SER THR THR TRP TYR PHE GLN
SEQRES 10 A 262 LYS LEU ASP ARG GLN ILE GLY GLU ASP HIS LEU ARG HIS
SEQRES 11 A 262 TYR LEU LYS SER ILE HIS TYR GLY ASN GLU ASP PHE SER
SEQRES 12 A 262 VAL PRO ALA ASP TYR TRP LEU ASP GLY SER LEU GLN ILE
SEQRES 13 A 262 SER PRO LEU GLU GLN VAL ASN ILE LEU LYS LYS PHE TYR
SEQRES 14 A 262 ASP ASN GLU PHE ASP PHE LYS GLN SER ASN ILE GLU THR
SEQRES 15 A 262 VAL LYS ASP SER ILE ARG LEU GLU GLU SER ASN GLY ARG
SEQRES 16 A 262 VAL LEU SER GLY LYS THR GLY THR SER VAL ILE ASN GLY
SEQRES 17 A 262 GLU LEU HIS ALA GLY TRP PHE ILE GLY TYR VAL GLU THR
SEQRES 18 A 262 ALA ASP ASN THR PHE PHE PHE ALA VAL HIS ILE GLN GLY
SEQRES 19 A 262 GLU LYS ARG ALA ALA GLY SER SER ALA ALA GLU ILE ALA
SEQRES 20 A 262 LEU SER ILE LEU ASP LYS LYS GLY ILE TYR PRO SER VAL
SEQRES 21 A 262 SER ARG
FORMUL 2 HOH *81(H2 O)
HELIX 1 1 TYR A 363 LYS A 369 1 7
HELIX 2 2 ASN A 390 SER A 396 1 7
HELIX 3 3 PRO A 400 THR A 403 5 4
HELIX 4 4 TYR A 404 SER A 415 1 12
HELIX 5 5 ASP A 442 SER A 450 1 9
HELIX 6 6 THR A 451 GLY A 463 1 13
HELIX 7 7 GLY A 463 ILE A 474 1 12
HELIX 8 8 SER A 496 ASP A 509 1 14
HELIX 9 9 LYS A 515 ILE A 526 1 12
HELIX 10 10 ALA A 577 LYS A 593 1 17
SHEET 1 A 7 ASN A 357 TYR A 360 0
SHEET 2 A 7 LYS A 385 TYR A 389 1 O TYR A 386 N GLU A 359
SHEET 3 A 7 ALA A 372 ASN A 380 -1 N ASN A 380 O LYS A 385
SHEET 4 A 7 THR A 564 GLY A 573 -1 O PHE A 566 N PHE A 379
SHEET 5 A 7 HIS A 550 GLU A 559 -1 N VAL A 558 O PHE A 565
SHEET 6 A 7 ARG A 534 VAL A 544 -1 N SER A 543 O ALA A 551
SHEET 7 A 7 ARG A 527 SER A 531 -1 N SER A 531 O ARG A 534
CRYST1 45.848 45.848 130.198 90.00 90.00 90.00 P 41 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 0.021811 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021811 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007681 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
