HEADER METAL TRANSPORT 28-JUL-05 2AHE
TITLE CRYSTAL STRUCTURE OF A SOLUBLE FORM OF CLIC4. INTERCELLULAR CHLORIDE
TITLE 2 ION CHANNEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHLORIDE INTRACELLULAR CHANNEL PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: INTRACELLULAR CHLORIDE ION CHANNEL PROTEIN P64H1;
COMPND 5 ENGINEERED: 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-2T
KEYWDS GLUTATHIONE-S-TRANSFERASE SUPERFAMILY, CLIC4, NCC27, CHLORIDE ION
KEYWDS 2 CHANNEL, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.LITTLER,N.N.ASSAAD,S.J.HARROP,L.J.BROWN,G.J.PANKHURST,P.LUCIANI,
AUTHOR 2 M.-I.AGUILAR,M.MAZZANTI,M.A.BERRYMAN,S.N.BREIT,P.M.G.CURMI
REVDAT 4 25-OCT-23 2AHE 1 SEQADV
REVDAT 3 24-FEB-09 2AHE 1 VERSN
REVDAT 2 01-NOV-05 2AHE 1 JRNL
REVDAT 1 16-AUG-05 2AHE 0
JRNL AUTH D.R.LITTLER,N.N.ASSAAD,S.J.HARROP,L.J.BROWN,G.J.PANKHURST,
JRNL AUTH 2 P.LUCIANI,M.-I.AGUILAR,M.MAZZANTI,M.A.BERRYMAN,S.N.BREIT,
JRNL AUTH 3 P.M.G.CURMI
JRNL TITL CRYSTAL STRUCTURE OF THE SOLUBLE FORM OF THE REDOX-REGULATED
JRNL TITL 2 CHLORIDE ION CHANNEL PROTEIN CLIC4.
JRNL REF FEBS J. V. 272 4996 2005
JRNL REFN ISSN 1742-464X
JRNL PMID 16176272
JRNL DOI 10.1111/J.1742-4658.2005.04909.X
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 23815
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1281
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1720
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1820
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 196
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47000
REMARK 3 B22 (A**2) : 0.13000
REMARK 3 B33 (A**2) : -0.60000
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): 0.128
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.122
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.623
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1861 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1711 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2518 ; 1.536 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4020 ; 0.855 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 226 ; 5.650 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 79 ;31.741 ;24.684
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 342 ;13.373 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;17.571 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 283 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2006 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 349 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 383 ; 0.224 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1659 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 925 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1006 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 150 ; 0.140 ; 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): 9 ; 0.299 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 39 ; 0.218 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.127 ; 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): 1478 ; 1.427 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 450 ; 0.298 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1867 ; 1.677 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 838 ; 3.050 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 651 ; 4.208 ; 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): 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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 2AHE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033897.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 : ENRAF-NONIUS FR571
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
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 : 25137
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 55.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.650
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3584
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.56
REMARK 200 R MERGE FOR SHELL (I) : 0.58000
REMARK 200 R SYM FOR SHELL (I) : 0.58000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: 1KOM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 38.85850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.73900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.85850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.73900
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 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 MET A 5
REMARK 465 PRO A 6
REMARK 465 LEU A 7
REMARK 465 ASN A 8
REMARK 465 GLY A 9
REMARK 465 LEU A 10
REMARK 465 LYS A 11
REMARK 465 GLU A 12
REMARK 465 GLU A 13
REMARK 465 ASP A 14
REMARK 465 LYS A 15
REMARK 465 PRO A 160
REMARK 465 ASP A 161
REMARK 465 GLU A 162
REMARK 465 ILE A 163
REMARK 465 ASP A 164
REMARK 465 GLU A 165
REMARK 465 ASN A 166
REMARK 465 SER A 167
REMARK 465 MET A 168
REMARK 465 GLU A 169
REMARK 465 ASP A 170
REMARK 465 ILE A 171
REMARK 465 LYS A 172
REMARK 465 PHE A 173
REMARK 465 GLY A 258
REMARK 465 GLU A 259
REMARK 465 PHE A 260
REMARK 465 GLN A 261
REMARK 465 HIS A 262
REMARK 465 THR A 263
REMARK 465 GLY A 264
REMARK 465 GLY A 265
REMARK 465 ARG A 266
REMARK 465 TYR A 267
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 CYS A 234 CA - CB - SG ANGL. DEV. = 6.7 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 CYS A 35 109.98 -177.88
REMARK 500 ARG A 61 54.31 -145.49
REMARK 500 SER A 82 -3.19 80.26
REMARK 500 ASP A 87 107.90 77.40
REMARK 500 LEU A 99 75.52 -101.75
REMARK 500 ASN A 207 41.73 39.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K0M RELATED DB: PDB
DBREF 2AHE A 1 251 UNP Q9Y696 CLIC4_HUMAN 1 251
SEQADV 2AHE PRO A 252 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE SER A 253 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE LYS A 254 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE VAL A 255 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE PRO A 256 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE LYS A 257 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE GLY A 258 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE GLU A 259 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE PHE A 260 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE GLN A 261 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE HIS A 262 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE THR A 263 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE GLY A 264 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE GLY A 265 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE ARG A 266 UNP Q9Y696 CLONING ARTIFACT
SEQADV 2AHE TYR A 267 UNP Q9Y696 CLONING ARTIFACT
SEQRES 1 A 267 MET ALA LEU SER MET PRO LEU ASN GLY LEU LYS GLU GLU
SEQRES 2 A 267 ASP LYS GLU PRO LEU ILE GLU LEU PHE VAL LYS ALA GLY
SEQRES 3 A 267 SER ASP GLY GLU SER ILE GLY ASN CYS PRO PHE SER GLN
SEQRES 4 A 267 ARG LEU PHE MET ILE LEU TRP LEU LYS GLY VAL VAL PHE
SEQRES 5 A 267 SER VAL THR THR VAL ASP LEU LYS ARG LYS PRO ALA ASP
SEQRES 6 A 267 LEU GLN ASN LEU ALA PRO GLY THR HIS PRO PRO PHE ILE
SEQRES 7 A 267 THR PHE ASN SER GLU VAL LYS THR ASP VAL ASN LYS ILE
SEQRES 8 A 267 GLU GLU PHE LEU GLU GLU VAL LEU CYS PRO PRO LYS TYR
SEQRES 9 A 267 LEU LYS LEU SER PRO LYS HIS PRO GLU SER ASN THR ALA
SEQRES 10 A 267 GLY MET ASP ILE PHE ALA LYS PHE SER ALA TYR ILE LYS
SEQRES 11 A 267 ASN SER ARG PRO GLU ALA ASN GLU ALA LEU GLU ARG GLY
SEQRES 12 A 267 LEU LEU LYS THR LEU GLN LYS LEU ASP GLU TYR LEU ASN
SEQRES 13 A 267 SER PRO LEU PRO ASP GLU ILE ASP GLU ASN SER MET GLU
SEQRES 14 A 267 ASP ILE LYS PHE SER THR ARG LYS PHE LEU ASP GLY ASN
SEQRES 15 A 267 GLU MET THR LEU ALA ASP CYS ASN LEU LEU PRO LYS LEU
SEQRES 16 A 267 HIS ILE VAL LYS VAL VAL ALA LYS LYS TYR ARG ASN PHE
SEQRES 17 A 267 ASP ILE PRO LYS GLU MET THR GLY ILE TRP ARG TYR LEU
SEQRES 18 A 267 THR ASN ALA TYR SER ARG ASP GLU PHE THR ASN THR CYS
SEQRES 19 A 267 PRO SER ASP LYS GLU VAL GLU ILE ALA TYR SER ASP VAL
SEQRES 20 A 267 ALA LYS ARG LEU PRO SER LYS VAL PRO LYS GLY GLU PHE
SEQRES 21 A 267 GLN HIS THR GLY GLY ARG TYR
FORMUL 2 HOH *196(H2 O)
HELIX 1 1 CYS A 35 GLY A 49 1 15
HELIX 2 2 PRO A 63 ALA A 70 1 8
HELIX 3 3 ASP A 87 LEU A 99 1 13
HELIX 4 4 HIS A 111 THR A 116 5 6
HELIX 5 5 ASP A 120 ASN A 131 1 12
HELIX 6 6 ARG A 133 GLU A 135 5 3
HELIX 7 7 ALA A 136 SER A 157 1 22
HELIX 8 8 THR A 185 ASN A 207 1 23
HELIX 9 9 MET A 214 SER A 226 1 13
HELIX 10 10 ARG A 227 ASN A 232 1 6
HELIX 11 11 SER A 236 TYR A 244 1 9
SHEET 1 A 4 SER A 53 VAL A 57 0
SHEET 2 A 4 ILE A 19 LYS A 24 1 N LEU A 21 O THR A 55
SHEET 3 A 4 PHE A 77 PHE A 80 -1 O PHE A 77 N PHE A 22
SHEET 4 A 4 GLU A 83 LYS A 85 -1 O LYS A 85 N ILE A 78
CISPEP 1 PRO A 75 PRO A 76 0 1.64
CISPEP 2 PRO A 101 PRO A 102 0 5.35
CRYST1 77.717 79.478 42.600 90.00 90.00 90.00 P 21 21 2 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 0.012867 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012582 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023474 0.00000
(ATOM LINES ARE NOT SHOWN.)
END