HEADER METAL BINDING PROTEIN 16-DEC-04 1Y9U
TITLE BORDETELLA FERRIC BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE IRON BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BORDETELLA PERTUSSIS TOHAMA I;
SOURCE 3 ORGANISM_TAXID: 257313;
SOURCE 4 STRAIN: TOHAMA I;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS PERIPLASMIC BINDING PROTEIN, IRON TYROSINATE INTERACTION, METAL
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.A.L.TOM-YEW,D.T.CUI,E.G.BEKKER,M.E.P.MURPHY
REVDAT 4 04-APR-18 1Y9U 1 REMARK
REVDAT 3 24-FEB-09 1Y9U 1 VERSN
REVDAT 2 26-APR-05 1Y9U 1 JRNL
REVDAT 1 11-JAN-05 1Y9U 0
JRNL AUTH S.A.L.TOM-YEW,D.T.CUI,E.G.BEKKER,M.E.P.MURPHY
JRNL TITL ANION-INDEPENDENT IRON COORDINATION BY THE CAMPYLOBACTER
JRNL TITL 2 JEJUNI FERRIC BINDING PROTEIN
JRNL REF J.BIOL.CHEM. V. 280 9283 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15613474
JRNL DOI 10.1074/JBC.M412479200
REMARK 2
REMARK 2 RESOLUTION. 1.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 54837
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 + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4815
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.39
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.42
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3024
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 178
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2387
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 322
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.01000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.070
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.059
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.034
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.828
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2444 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2261 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3317 ; 1.393 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5251 ; 0.880 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 314 ; 5.832 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 376 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2747 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 477 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 583 ; 0.447 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2673 ; 0.294 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1422 ; 0.098 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 211 ; 0.163 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 10 ; 0.201 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 48 ; 0.257 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.122 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1560 ; 1.052 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2492 ; 1.669 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 884 ; 2.296 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 825 ; 3.521 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2444 ; 1.209 ; 2.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 322 ; 3.420 ; 2.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2399 ; 2.100 ; 2.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1Y9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031297.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59653
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.390
REMARK 200 RESOLUTION RANGE LOW (A) : 23.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.9
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1500, PH 6, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 292.15K
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 29.69500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.41000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.73500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.41000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.69500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.73500
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 300 REMARK: THE BIOLOGICAL UNIT IS THE MONOMER
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 GLY A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 SER A 5
REMARK 465 THR A 229
REMARK 465 ALA A 230
REMARK 465 LYS A 231
REMARK 465 ASP A 232
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 ND2 ASN A 197 OH TYR A 199 1.34
REMARK 500 OH TYR A 100 O HOH A 630 2.15
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 TYR A 199 N TYR A 199 CA 0.128
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 ASP A 52 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 69 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 127 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 TYR A 199 CB - CA - C ANGL. DEV. = 12.5 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 ASP A 63 123.83 87.53
REMARK 500 LEU A 117 105.03 -161.18
REMARK 500 ASN A 250 62.85 -118.26
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Y9U A 5 323 UNP Q7VXW9 Q7VXW9_BORPE 31 349
SEQADV 1Y9U GLY A 1 UNP Q7VXW9 CLONING ARTIFACT
SEQADV 1Y9U SER A 2 UNP Q7VXW9 CLONING ARTIFACT
SEQADV 1Y9U HIS A 3 UNP Q7VXW9 CLONING ARTIFACT
SEQADV 1Y9U MET A 4 UNP Q7VXW9 CLONING ARTIFACT
SEQRES 1 A 323 GLY SER HIS MET SER ASP GLU VAL SER LEU TYR THR THR
SEQRES 2 A 323 ARG GLU PRO LYS LEU ILE GLN PRO LEU LEU ASP ALA PHE
SEQRES 3 A 323 ALA LYS ASP SER GLY ILE LYS VAL ASN THR VAL PHE VAL
SEQRES 4 A 323 LYS ASP GLY LEU LEU GLU ARG VAL ARG ALA GLU GLY ASP
SEQRES 5 A 323 LYS SER PRO ALA ASP VAL LEU MET THR VAL ASP ILE GLY
SEQRES 6 A 323 ASN LEU ILE ASP LEU VAL ASN GLY GLY VAL THR GLN LYS
SEQRES 7 A 323 ILE GLN SER GLN THR LEU ASP SER VAL VAL PRO ALA ASN
SEQRES 8 A 323 LEU ARG GLY ALA GLU GLY SER TRP TYR ALA LEU SER LEU
SEQRES 9 A 323 ARG ASP ARG VAL LEU TYR VAL GLU LYS ASP LEU LYS LEU
SEQRES 10 A 323 ASP SER PHE ARG TYR GLY ASP LEU ALA ASP PRO LYS TRP
SEQRES 11 A 323 LYS GLY LYS VAL CYS ILE ARG SER GLY GLN HIS PRO TYR
SEQRES 12 A 323 ASN THR ALA LEU VAL ALA ALA MET ILE ALA HIS ASP GLY
SEQRES 13 A 323 ALA GLU ALA THR GLU LYS TRP LEU ARG GLY VAL LYS ALA
SEQRES 14 A 323 ASN LEU ALA ARG LYS ALA ALA GLY GLY ASP ARG ASP VAL
SEQRES 15 A 323 ALA ARG ASP ILE LEU GLY GLY ILE CYS ASP ILE GLY LEU
SEQRES 16 A 323 ALA ASN ALA TYR TYR VAL GLY HIS MET LYS ASN ALA GLU
SEQRES 17 A 323 PRO GLY THR ASP ALA ARG LYS TRP GLY ASP ALA ILE LYS
SEQRES 18 A 323 VAL VAL ARG PRO THR PHE ALA THR ALA LYS ASP GLY GLY
SEQRES 19 A 323 THR HIS VAL ASN ILE SER GLY ALA ALA VAL ALA ALA HIS
SEQRES 20 A 323 ALA PRO ASN LYS ALA ASN ALA VAL LYS LEU LEU GLU TYR
SEQRES 21 A 323 LEU VAL SER GLU PRO ALA GLN THR LEU TYR ALA GLN ALA
SEQRES 22 A 323 ASN TYR GLU TYR PRO VAL ARG ALA GLY VAL LYS LEU ASP
SEQRES 23 A 323 ALA VAL VAL ALA SER PHE GLY PRO LEU LYS VAL ASP THR
SEQRES 24 A 323 LEU PRO VAL ALA GLU ILE ALA LYS TYR ARG LYS GLN ALA
SEQRES 25 A 323 SER GLU LEU VAL ASP LYS VAL GLY PHE ASP ASN
FORMUL 2 HOH *322(H2 O)
HELIX 1 1 GLU A 15 LEU A 18 5 4
HELIX 2 2 ILE A 19 GLY A 31 1 13
HELIX 3 3 GLY A 42 GLY A 51 1 10
HELIX 4 4 ASP A 52 SER A 54 5 3
HELIX 5 5 ASP A 63 GLY A 73 1 11
HELIX 6 6 SER A 81 VAL A 88 1 8
HELIX 7 7 PRO A 89 ARG A 93 5 5
HELIX 8 8 GLY A 94 SER A 98 5 5
HELIX 9 9 ARG A 121 LYS A 131 5 11
HELIX 10 10 HIS A 141 GLY A 156 1 16
HELIX 11 11 GLY A 156 LEU A 171 1 16
HELIX 12 12 GLY A 178 GLY A 188 1 11
HELIX 13 13 ALA A 198 ALA A 207 1 10
HELIX 14 14 THR A 211 ALA A 219 1 9
HELIX 15 15 ASN A 250 VAL A 262 1 13
HELIX 16 16 SER A 263 ASN A 274 1 12
HELIX 17 17 ASP A 286 PHE A 292 1 7
HELIX 18 18 VAL A 302 VAL A 319 1 18
SHEET 1 A 7 LYS A 33 PHE A 38 0
SHEET 2 A 7 GLU A 7 THR A 12 1 N LEU A 10 O VAL A 37
SHEET 3 A 7 VAL A 58 VAL A 62 1 O VAL A 58 N TYR A 11
SHEET 4 A 7 VAL A 237 ALA A 245 -1 O ALA A 243 N LEU A 59
SHEET 5 A 7 TYR A 100 GLU A 112 -1 N ARG A 105 O ASN A 238
SHEET 6 A 7 ILE A 193 ASN A 197 -1 O GLY A 194 N TYR A 110
SHEET 7 A 7 VAL A 134 CYS A 135 1 N CYS A 135 O ILE A 193
SHEET 1 B 6 LYS A 33 PHE A 38 0
SHEET 2 B 6 GLU A 7 THR A 12 1 N LEU A 10 O VAL A 37
SHEET 3 B 6 VAL A 58 VAL A 62 1 O VAL A 58 N TYR A 11
SHEET 4 B 6 VAL A 237 ALA A 245 -1 O ALA A 243 N LEU A 59
SHEET 5 B 6 TYR A 100 GLU A 112 -1 N ARG A 105 O ASN A 238
SHEET 6 B 6 ILE A 220 VAL A 223 -1 O VAL A 223 N LEU A 109
SHEET 1 C 4 THR A 76 GLN A 77 0
SHEET 2 C 4 VAL A 237 ALA A 245 -1 O VAL A 244 N GLN A 77
SHEET 3 C 4 TYR A 100 GLU A 112 -1 N ARG A 105 O ASN A 238
SHEET 4 C 4 TYR A 277 PRO A 278 -1 O TYR A 277 N LEU A 104
SSBOND 1 CYS A 135 CYS A 191 1555 1555 2.11
CRYST1 59.390 71.470 74.820 90.00 90.00 90.00 P 21 21 21 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 0.016838 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013992 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013365 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
