HEADER METAL TRANSPORT 19-SEP-01 1K0O
TITLE CRYSTAL STRUCTURE OF A SOLUBLE FORM OF CLIC1. AN INTRACELLULAR
TITLE 2 CHLORIDE ION CHANNEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHLORIDE INTRACELLULAR CHANNEL PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CLIC1;
COMPND 5 SYNONYM: CLIC1, NCC27;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS GLUTATHIONE-S-TRANSFERASE SUPERFAMILY, CLIC1, NCC27, CHLORIDE ION
KEYWDS 2 CHANNEL, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR S.J.HARROP,M.Z.DEMAERE,W.D.FAIRLIE,T.REZTSOVA,S.M.VALENZUELA,
AUTHOR 2 M.MAZZANTI,R.TONINI,M.R.QIU,L.JANKOVA,K.WARTON,A.R.BAUSKIN,W.M.WU,
AUTHOR 3 S.PANKHURST,T.J.CAMPBELL,S.N.BREIT,P.M.G.CURMI
REVDAT 5 07-FEB-24 1K0O 1 REMARK
REVDAT 4 27-OCT-21 1K0O 1 SEQADV
REVDAT 3 24-FEB-09 1K0O 1 VERSN
REVDAT 2 01-APR-03 1K0O 1 JRNL
REVDAT 1 12-DEC-01 1K0O 0
JRNL AUTH S.J.HARROP,M.Z.DEMAERE,W.D.FAIRLIE,T.REZTSOVA,
JRNL AUTH 2 S.M.VALENZUELA,M.MAZZANTI,R.TONINI,M.R.QIU,L.JANKOVA,
JRNL AUTH 3 K.WARTON,A.R.BAUSKIN,W.M.WU,S.PANKHURST,T.J.CAMPBELL,
JRNL AUTH 4 S.N.BREIT,P.M.CURMI
JRNL TITL CRYSTAL STRUCTURE OF A SOLUBLE FORM OF THE INTRACELLULAR
JRNL TITL 2 CHLORIDE ION CHANNEL CLIC1 (NCC27) AT 1.4-A RESOLUTION.
JRNL REF J.BIOL.CHEM. V. 276 44993 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11551966
JRNL DOI 10.1074/JBC.M107804200
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 46443
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) : 0.242
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2472
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3450
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 122
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.97000
REMARK 3 B22 (A**2) : -0.55000
REMARK 3 B33 (A**2) : -1.41000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K0O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014412.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
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 : YES
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 47410
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 80.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : 0.04400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : 0.46000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 5K, AMMONIUM SULPHATE, SODIUM
REMARK 280 ACETATE, PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 30.15550
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 GLN A 5
REMARK 465 VAL A 152
REMARK 465 ASP A 153
REMARK 465 GLU A 154
REMARK 465 THR A 155
REMARK 465 SER A 156
REMARK 465 ALA A 157
REMARK 465 GLU A 158
REMARK 465 ASP A 159
REMARK 465 GLU A 160
REMARK 465 GLY A 161
REMARK 465 VAL A 162
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 4
REMARK 465 GLN B 5
REMARK 465 PRO B 90
REMARK 465 PRO B 91
REMARK 465 ASN B 100
REMARK 465 PRO B 101
REMARK 465 GLU B 102
REMARK 465 LEU B 148
REMARK 465 PRO B 149
REMARK 465 GLU B 150
REMARK 465 GLY B 151
REMARK 465 VAL B 152
REMARK 465 ASP B 153
REMARK 465 GLU B 154
REMARK 465 THR B 155
REMARK 465 SER B 156
REMARK 465 ALA B 157
REMARK 465 GLU B 158
REMARK 465 ASP B 159
REMARK 465 GLU B 160
REMARK 465 GLY B 161
REMARK 465 VAL B 162
REMARK 465 SER B 163
REMARK 465 GLN B 164
REMARK 465 ARG B 165
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 225 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 169 CB - CG - OD2 ANGL. DEV. = 7.2 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 ALA A 19 -42.99 -130.19
REMARK 500 CYS A 24 112.89 -176.97
REMARK 500 THR A 48 -9.86 -53.41
REMARK 500 ARG A 50 67.50 -161.07
REMARK 500 ASP A 76 108.96 84.23
REMARK 500 ALA B 19 -45.30 -135.05
REMARK 500 CYS B 24 106.68 -172.15
REMARK 500 ARG B 50 70.09 -153.59
REMARK 500 PHE B 167 -162.44 -128.69
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1K0O A 1 241 UNP O00299 CLIC1_HUMAN 1 241
DBREF 1K0O B 1 241 UNP O00299 CLIC1_HUMAN 1 241
SEQADV 1K0O GLU A 63 UNP O00299 GLN 63 CONFLICT
SEQADV 1K0O GLY A 151 UNP O00299 GLU 151 ENGINEERED MUTATION
SEQADV 1K0O GLU B 63 UNP O00299 GLN 63 CONFLICT
SEQADV 1K0O GLY B 151 UNP O00299 GLU 151 ENGINEERED MUTATION
SEQRES 1 A 241 MET ALA GLU GLU GLN PRO GLN VAL GLU LEU PHE VAL LYS
SEQRES 2 A 241 ALA GLY SER ASP GLY ALA LYS ILE GLY ASN CYS PRO PHE
SEQRES 3 A 241 SER GLN ARG LEU PHE MET VAL LEU TRP LEU LYS GLY VAL
SEQRES 4 A 241 THR PHE ASN VAL THR THR VAL ASP THR LYS ARG ARG THR
SEQRES 5 A 241 GLU THR VAL GLN LYS LEU CYS PRO GLY GLY GLU LEU PRO
SEQRES 6 A 241 PHE LEU LEU TYR GLY THR GLU VAL HIS THR ASP THR ASN
SEQRES 7 A 241 LYS ILE GLU GLU PHE LEU GLU ALA VAL LEU CYS PRO PRO
SEQRES 8 A 241 ARG TYR PRO LYS LEU ALA ALA LEU ASN PRO GLU SER ASN
SEQRES 9 A 241 THR ALA GLY LEU ASP ILE PHE ALA LYS PHE SER ALA TYR
SEQRES 10 A 241 ILE LYS ASN SER ASN PRO ALA LEU ASN ASP ASN LEU GLU
SEQRES 11 A 241 LYS GLY LEU LEU LYS ALA LEU LYS VAL LEU ASP ASN TYR
SEQRES 12 A 241 LEU THR SER PRO LEU PRO GLU GLY VAL ASP GLU THR SER
SEQRES 13 A 241 ALA GLU ASP GLU GLY VAL SER GLN ARG LYS PHE LEU ASP
SEQRES 14 A 241 GLY ASN GLU LEU THR LEU ALA ASP CYS ASN LEU LEU PRO
SEQRES 15 A 241 LYS LEU HIS ILE VAL GLN VAL VAL CYS LYS LYS TYR ARG
SEQRES 16 A 241 GLY PHE THR ILE PRO GLU ALA PHE ARG GLY VAL HIS ARG
SEQRES 17 A 241 TYR LEU SER ASN ALA TYR ALA ARG GLU GLU PHE ALA SER
SEQRES 18 A 241 THR CYS PRO ASP ASP GLU GLU ILE GLU LEU ALA TYR GLU
SEQRES 19 A 241 GLN VAL ALA LYS ALA LEU LYS
SEQRES 1 B 241 MET ALA GLU GLU GLN PRO GLN VAL GLU LEU PHE VAL LYS
SEQRES 2 B 241 ALA GLY SER ASP GLY ALA LYS ILE GLY ASN CYS PRO PHE
SEQRES 3 B 241 SER GLN ARG LEU PHE MET VAL LEU TRP LEU LYS GLY VAL
SEQRES 4 B 241 THR PHE ASN VAL THR THR VAL ASP THR LYS ARG ARG THR
SEQRES 5 B 241 GLU THR VAL GLN LYS LEU CYS PRO GLY GLY GLU LEU PRO
SEQRES 6 B 241 PHE LEU LEU TYR GLY THR GLU VAL HIS THR ASP THR ASN
SEQRES 7 B 241 LYS ILE GLU GLU PHE LEU GLU ALA VAL LEU CYS PRO PRO
SEQRES 8 B 241 ARG TYR PRO LYS LEU ALA ALA LEU ASN PRO GLU SER ASN
SEQRES 9 B 241 THR ALA GLY LEU ASP ILE PHE ALA LYS PHE SER ALA TYR
SEQRES 10 B 241 ILE LYS ASN SER ASN PRO ALA LEU ASN ASP ASN LEU GLU
SEQRES 11 B 241 LYS GLY LEU LEU LYS ALA LEU LYS VAL LEU ASP ASN TYR
SEQRES 12 B 241 LEU THR SER PRO LEU PRO GLU GLY VAL ASP GLU THR SER
SEQRES 13 B 241 ALA GLU ASP GLU GLY VAL SER GLN ARG LYS PHE LEU ASP
SEQRES 14 B 241 GLY ASN GLU LEU THR LEU ALA ASP CYS ASN LEU LEU PRO
SEQRES 15 B 241 LYS LEU HIS ILE VAL GLN VAL VAL CYS LYS LYS TYR ARG
SEQRES 16 B 241 GLY PHE THR ILE PRO GLU ALA PHE ARG GLY VAL HIS ARG
SEQRES 17 B 241 TYR LEU SER ASN ALA TYR ALA ARG GLU GLU PHE ALA SER
SEQRES 18 B 241 THR CYS PRO ASP ASP GLU GLU ILE GLU LEU ALA TYR GLU
SEQRES 19 B 241 GLN VAL ALA LYS ALA LEU LYS
FORMUL 3 HOH *122(H2 O)
HELIX 1 1 CYS A 24 GLY A 38 1 15
HELIX 2 2 THR A 52 CYS A 59 1 8
HELIX 3 3 ASP A 76 LEU A 88 1 13
HELIX 4 4 ASN A 100 THR A 105 5 6
HELIX 5 5 ASP A 109 ASN A 120 1 12
HELIX 6 6 ASN A 122 SER A 146 1 25
HELIX 7 7 THR A 174 GLY A 196 1 23
HELIX 8 8 PHE A 203 ALA A 215 1 13
HELIX 9 9 ARG A 216 SER A 221 1 6
HELIX 10 10 ASP A 225 TYR A 233 1 9
HELIX 11 11 CYS B 24 GLY B 38 1 15
HELIX 12 12 THR B 52 CYS B 59 1 8
HELIX 13 13 ASP B 76 LEU B 88 1 13
HELIX 14 14 ASP B 109 ASN B 120 1 12
HELIX 15 15 ASN B 122 ALA B 124 5 3
HELIX 16 16 LEU B 125 SER B 146 1 22
HELIX 17 17 THR B 174 GLY B 196 1 23
HELIX 18 18 PHE B 203 ALA B 215 1 13
HELIX 19 19 ARG B 216 SER B 221 1 6
HELIX 20 20 ASP B 225 TYR B 233 1 9
SHEET 1 A 4 PHE A 41 VAL A 46 0
SHEET 2 A 4 VAL A 8 LYS A 13 1 N LEU A 10 O ASN A 42
SHEET 3 A 4 PHE A 66 TYR A 69 -1 O PHE A 66 N PHE A 11
SHEET 4 A 4 GLU A 72 THR A 75 -1 O HIS A 74 N LEU A 67
SHEET 1 B 4 ASN B 42 VAL B 46 0
SHEET 2 B 4 VAL B 8 LYS B 13 1 N VAL B 12 O VAL B 46
SHEET 3 B 4 PHE B 66 TYR B 69 -1 O LEU B 68 N GLU B 9
SHEET 4 B 4 GLU B 72 HIS B 74 -1 O GLU B 72 N TYR B 69
CISPEP 1 LEU A 64 PRO A 65 0 1.90
CISPEP 2 PRO A 90 PRO A 91 0 -5.12
CISPEP 3 LEU B 64 PRO B 65 0 -1.46
CRYST1 46.408 60.311 89.428 90.00 92.41 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 0.021548 0.000000 0.000907 0.00000
SCALE2 0.000000 0.016581 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011192 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
