HEADER MEMBRANE PROTEIN 23-MAR-03 1OTT
TITLE STRUCTURE OF THE ESCHERICHIA COLI CLC CHLORIDE CHANNEL E148A MUTANT
TITLE 2 AND FAB COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VOLTAGE-GATED CLC-TYPE CHLORIDE CHANNEL ERIC;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: FAB FRAGMENT (HEAVY CHAIN);
COMPND 8 CHAIN: C, E;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: FAB FRAGMENT (LIGHT CHAIN);
COMPND 11 CHAIN: D, F
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ERIC OR B0155;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B+;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 CELL_LINE: HYBRIDOMA CELL LINE;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 17 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 18 ORGANISM_TAXID: 10090;
SOURCE 19 CELL_LINE: HYBRIDOMA CELL LINE
KEYWDS CHLORIDE CHANNEL, FAB COMPLEX, ION CHANNEL, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.DUTZLER,E.B.CAMPBELL,R.MACKINNON
REVDAT 4 16-AUG-23 1OTT 1 REMARK
REVDAT 3 27-OCT-21 1OTT 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1OTT 1 VERSN
REVDAT 1 15-APR-03 1OTT 0
JRNL AUTH R.DUTZLER,E.B.CAMPBELL,R.MACKINNON
JRNL TITL GATING THE SELECTIVITY FILTER IN CLC CHLORIDE CHANNELS
JRNL REF SCIENCE V. 300 108 2003
JRNL REFN ISSN 0036-8075
JRNL PMID 12649487
JRNL DOI 10.1126/SCIENCE.1082708
REMARK 2
REMARK 2 RESOLUTION. 3.00 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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 52105
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) : 0.296
REMARK 3 FREE R VALUE : 0.338
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2556
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6760
REMARK 3 BIN R VALUE (WORKING SET) : 0.5450
REMARK 3 BIN FREE R VALUE : 0.5340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 353
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13215
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 71.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -11.55000
REMARK 3 B22 (A**2) : 20.94000
REMARK 3 B33 (A**2) : -9.39000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 12.76000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.69
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.94
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.020
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) : 1.620 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.720 ; 2.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.070 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.340 ; 3.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.26
REMARK 3 BSOL : 20.87
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 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OTT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018661.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SDMS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52212
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.49200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE, DM
REMARK 200 STARTING MODEL: PDB ENTRY 1OTS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 300, SODIUM CHLORIDE, GLYCINE, PH
REMARK 280 9.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 115.80700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.85950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 115.80700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 47.85950
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 ASSEMBLY FOR
REMARK 300 THE CLC CHANNEL IS A DIMER FORMED BY CHAIN A AND B
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 LYS A 2
REMARK 465 THR A 3
REMARK 465 ASP A 4
REMARK 465 THR A 5
REMARK 465 PRO A 6
REMARK 465 SER A 7
REMARK 465 LEU A 8
REMARK 465 GLU A 9
REMARK 465 THR A 10
REMARK 465 PRO A 11
REMARK 465 GLN A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 ARG A 15
REMARK 465 LEU A 16
REMARK 465 LEU A 461
REMARK 465 ALA A 462
REMARK 465 ARG A 463
REMARK 465 SER A 464
REMARK 465 LYS A 465
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 THR B 3
REMARK 465 ASP B 4
REMARK 465 THR B 5
REMARK 465 PRO B 6
REMARK 465 SER B 7
REMARK 465 LEU B 8
REMARK 465 GLU B 9
REMARK 465 THR B 10
REMARK 465 PRO B 11
REMARK 465 GLN B 12
REMARK 465 ALA B 13
REMARK 465 ALA B 14
REMARK 465 ARG B 15
REMARK 465 LEU B 16
REMARK 465 ARG B 17
REMARK 465 GLU B 459
REMARK 465 GLN B 460
REMARK 465 LEU B 461
REMARK 465 ALA B 462
REMARK 465 ARG B 463
REMARK 465 SER B 464
REMARK 465 LYS B 465
REMARK 465 GLU C 1
REMARK 465 GLU E 1
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 ARG A 18 -19.13 -49.12
REMARK 500 ASP A 29 70.10 49.21
REMARK 500 TRP A 59 -39.62 -39.58
REMARK 500 ARG A 64 10.81 -59.43
REMARK 500 LEU A 78 -78.90 -66.18
REMARK 500 LEU A 79 -16.66 -37.87
REMARK 500 LEU A 96 -6.80 -55.23
REMARK 500 TYR A 100 -16.91 -144.01
REMARK 500 ALA A 101 75.84 -170.43
REMARK 500 ALA A 104 -80.20 -67.89
REMARK 500 SER A 107 -71.21 -34.56
REMARK 500 GLU A 111 -70.00 -56.14
REMARK 500 VAL A 122 76.78 -108.88
REMARK 500 LEU A 128 -70.11 -43.65
REMARK 500 VAL A 130 -71.92 -63.07
REMARK 500 PHE A 132 -78.40 -60.96
REMARK 500 ALA A 148 -92.40 -52.60
REMARK 500 ARG A 167 58.61 30.88
REMARK 500 ASP A 171 -41.74 -17.90
REMARK 500 ILE A 201 39.29 -88.23
REMARK 500 GLU A 202 -13.61 -156.69
REMARK 500 GLU A 203 -66.11 -142.92
REMARK 500 TYR A 210 148.37 -35.33
REMARK 500 LEU A 212 38.08 -88.96
REMARK 500 LYS A 216 -30.15 -36.45
REMARK 500 VAL A 236 100.38 -164.25
REMARK 500 VAL A 241 -2.87 -142.44
REMARK 500 TRP A 272 -71.64 -46.91
REMARK 500 ARG A 282 -72.13 -59.30
REMARK 500 VAL A 283 -45.67 -19.79
REMARK 500 TRP A 291 -75.45 -88.38
REMARK 500 PHE A 307 -4.25 -175.36
REMARK 500 ALA A 309 69.61 166.96
REMARK 500 SER A 313 -160.65 -101.62
REMARK 500 PHE A 317 -71.69 -41.14
REMARK 500 ASN A 318 -30.76 -35.08
REMARK 500 PHE A 337 -74.13 -54.28
REMARK 500 LEU A 345 -71.29 -45.71
REMARK 500 LEU A 346 -34.22 -39.19
REMARK 500 PRO A 353 86.98 -68.55
REMARK 500 ALA A 386 -24.90 -34.53
REMARK 500 ALA A 404 54.83 -119.63
REMARK 500 ILE A 409 -48.66 -27.81
REMARK 500 VAL A 412 -74.76 -56.39
REMARK 500 ASP A 417 49.29 34.68
REMARK 500 TYR A 419 -30.65 -36.67
REMARK 500 GLN A 437 -75.85 -83.67
REMARK 500 PHE A 438 4.95 -45.22
REMARK 500 THR A 439 53.46 -141.33
REMARK 500 PRO A 443 98.52 -45.90
REMARK 500
REMARK 500 THIS ENTRY HAS 219 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR F 139 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 466
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 468
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 466
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 468
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OTS RELATED DB: PDB
REMARK 900 ECCLC FAB COMPLEX WT
REMARK 900 RELATED ID: 1OTU RELATED DB: PDB
REMARK 900 ECCLC FAB COMPLEX E148Q MUTANT
DBREF 1OTT A 1 465 UNP P37019 CLCA_ECOLI 1 465
DBREF 1OTT B 1 465 UNP P37019 CLCA_ECOLI 1 465
DBREF 1OTT C 1 222 PDB 1OTT 1OTT 1 222
DBREF 1OTT D 1 211 PDB 1OTT 1OTT 1 211
DBREF 1OTT E 1 222 PDB 1OTT 1OTT 1 222
DBREF 1OTT F 1 211 PDB 1OTT 1OTT 1 211
SEQADV 1OTT ALA A 148 UNP P37019 GLU 148 ENGINEERED MUTATION
SEQADV 1OTT ALA B 148 UNP P37019 GLU 148 ENGINEERED MUTATION
SEQRES 1 A 465 MET LYS THR ASP THR PRO SER LEU GLU THR PRO GLN ALA
SEQRES 2 A 465 ALA ARG LEU ARG ARG ARG GLN LEU ILE ARG GLN LEU LEU
SEQRES 3 A 465 GLU ARG ASP LYS THR PRO LEU ALA ILE LEU PHE MET ALA
SEQRES 4 A 465 ALA VAL VAL GLY THR LEU VAL GLY LEU ALA ALA VAL ALA
SEQRES 5 A 465 PHE ASP LYS GLY VAL ALA TRP LEU GLN ASN GLN ARG MET
SEQRES 6 A 465 GLY ALA LEU VAL HIS THR ALA ASP ASN TYR PRO LEU LEU
SEQRES 7 A 465 LEU THR VAL ALA PHE LEU CYS SER ALA VAL LEU ALA MET
SEQRES 8 A 465 PHE GLY TYR PHE LEU VAL ARG LYS TYR ALA PRO GLU ALA
SEQRES 9 A 465 GLY GLY SER GLY ILE PRO GLU ILE GLU GLY ALA LEU GLU
SEQRES 10 A 465 ASP GLN ARG PRO VAL ARG TRP TRP ARG VAL LEU PRO VAL
SEQRES 11 A 465 LYS PHE PHE GLY GLY LEU GLY THR LEU GLY GLY GLY MET
SEQRES 12 A 465 VAL LEU GLY ARG ALA GLY PRO THR VAL GLN ILE GLY GLY
SEQRES 13 A 465 ASN ILE GLY ARG MET VAL LEU ASP ILE PHE ARG LEU LYS
SEQRES 14 A 465 GLY ASP GLU ALA ARG HIS THR LEU LEU ALA THR GLY ALA
SEQRES 15 A 465 ALA ALA GLY LEU ALA ALA ALA PHE ASN ALA PRO LEU ALA
SEQRES 16 A 465 GLY ILE LEU PHE ILE ILE GLU GLU MET ARG PRO GLN PHE
SEQRES 17 A 465 ARG TYR THR LEU ILE SER ILE LYS ALA VAL PHE ILE GLY
SEQRES 18 A 465 VAL ILE MET SER THR ILE MET TYR ARG ILE PHE ASN HIS
SEQRES 19 A 465 GLU VAL ALA LEU ILE ASP VAL GLY LYS LEU SER ASP ALA
SEQRES 20 A 465 PRO LEU ASN THR LEU TRP LEU TYR LEU ILE LEU GLY ILE
SEQRES 21 A 465 ILE PHE GLY ILE PHE GLY PRO ILE PHE ASN LYS TRP VAL
SEQRES 22 A 465 LEU GLY MET GLN ASP LEU LEU HIS ARG VAL HIS GLY GLY
SEQRES 23 A 465 ASN ILE THR LYS TRP VAL LEU MET GLY GLY ALA ILE GLY
SEQRES 24 A 465 GLY LEU CYS GLY LEU LEU GLY PHE VAL ALA PRO ALA THR
SEQRES 25 A 465 SER GLY GLY GLY PHE ASN LEU ILE PRO ILE ALA THR ALA
SEQRES 26 A 465 GLY ASN PHE SER MET GLY MET LEU VAL PHE ILE PHE VAL
SEQRES 27 A 465 ALA ARG VAL ILE THR THR LEU LEU CYS PHE SER SER GLY
SEQRES 28 A 465 ALA PRO GLY GLY ILE PHE ALA PRO MET LEU ALA LEU GLY
SEQRES 29 A 465 THR VAL LEU GLY THR ALA PHE GLY MET VAL ALA VAL GLU
SEQRES 30 A 465 LEU PHE PRO GLN TYR HIS LEU GLU ALA GLY THR PHE ALA
SEQRES 31 A 465 ILE ALA GLY MET GLY ALA LEU LEU ALA ALA SER ILE ARG
SEQRES 32 A 465 ALA PRO LEU THR GLY ILE ILE LEU VAL LEU GLU MET THR
SEQRES 33 A 465 ASP ASN TYR GLN LEU ILE LEU PRO MET ILE ILE THR GLY
SEQRES 34 A 465 LEU GLY ALA THR LEU LEU ALA GLN PHE THR GLY GLY LYS
SEQRES 35 A 465 PRO LEU TYR SER ALA ILE LEU ALA ARG THR LEU ALA LYS
SEQRES 36 A 465 GLN GLU ALA GLU GLN LEU ALA ARG SER LYS
SEQRES 1 B 465 MET LYS THR ASP THR PRO SER LEU GLU THR PRO GLN ALA
SEQRES 2 B 465 ALA ARG LEU ARG ARG ARG GLN LEU ILE ARG GLN LEU LEU
SEQRES 3 B 465 GLU ARG ASP LYS THR PRO LEU ALA ILE LEU PHE MET ALA
SEQRES 4 B 465 ALA VAL VAL GLY THR LEU VAL GLY LEU ALA ALA VAL ALA
SEQRES 5 B 465 PHE ASP LYS GLY VAL ALA TRP LEU GLN ASN GLN ARG MET
SEQRES 6 B 465 GLY ALA LEU VAL HIS THR ALA ASP ASN TYR PRO LEU LEU
SEQRES 7 B 465 LEU THR VAL ALA PHE LEU CYS SER ALA VAL LEU ALA MET
SEQRES 8 B 465 PHE GLY TYR PHE LEU VAL ARG LYS TYR ALA PRO GLU ALA
SEQRES 9 B 465 GLY GLY SER GLY ILE PRO GLU ILE GLU GLY ALA LEU GLU
SEQRES 10 B 465 ASP GLN ARG PRO VAL ARG TRP TRP ARG VAL LEU PRO VAL
SEQRES 11 B 465 LYS PHE PHE GLY GLY LEU GLY THR LEU GLY GLY GLY MET
SEQRES 12 B 465 VAL LEU GLY ARG ALA GLY PRO THR VAL GLN ILE GLY GLY
SEQRES 13 B 465 ASN ILE GLY ARG MET VAL LEU ASP ILE PHE ARG LEU LYS
SEQRES 14 B 465 GLY ASP GLU ALA ARG HIS THR LEU LEU ALA THR GLY ALA
SEQRES 15 B 465 ALA ALA GLY LEU ALA ALA ALA PHE ASN ALA PRO LEU ALA
SEQRES 16 B 465 GLY ILE LEU PHE ILE ILE GLU GLU MET ARG PRO GLN PHE
SEQRES 17 B 465 ARG TYR THR LEU ILE SER ILE LYS ALA VAL PHE ILE GLY
SEQRES 18 B 465 VAL ILE MET SER THR ILE MET TYR ARG ILE PHE ASN HIS
SEQRES 19 B 465 GLU VAL ALA LEU ILE ASP VAL GLY LYS LEU SER ASP ALA
SEQRES 20 B 465 PRO LEU ASN THR LEU TRP LEU TYR LEU ILE LEU GLY ILE
SEQRES 21 B 465 ILE PHE GLY ILE PHE GLY PRO ILE PHE ASN LYS TRP VAL
SEQRES 22 B 465 LEU GLY MET GLN ASP LEU LEU HIS ARG VAL HIS GLY GLY
SEQRES 23 B 465 ASN ILE THR LYS TRP VAL LEU MET GLY GLY ALA ILE GLY
SEQRES 24 B 465 GLY LEU CYS GLY LEU LEU GLY PHE VAL ALA PRO ALA THR
SEQRES 25 B 465 SER GLY GLY GLY PHE ASN LEU ILE PRO ILE ALA THR ALA
SEQRES 26 B 465 GLY ASN PHE SER MET GLY MET LEU VAL PHE ILE PHE VAL
SEQRES 27 B 465 ALA ARG VAL ILE THR THR LEU LEU CYS PHE SER SER GLY
SEQRES 28 B 465 ALA PRO GLY GLY ILE PHE ALA PRO MET LEU ALA LEU GLY
SEQRES 29 B 465 THR VAL LEU GLY THR ALA PHE GLY MET VAL ALA VAL GLU
SEQRES 30 B 465 LEU PHE PRO GLN TYR HIS LEU GLU ALA GLY THR PHE ALA
SEQRES 31 B 465 ILE ALA GLY MET GLY ALA LEU LEU ALA ALA SER ILE ARG
SEQRES 32 B 465 ALA PRO LEU THR GLY ILE ILE LEU VAL LEU GLU MET THR
SEQRES 33 B 465 ASP ASN TYR GLN LEU ILE LEU PRO MET ILE ILE THR GLY
SEQRES 34 B 465 LEU GLY ALA THR LEU LEU ALA GLN PHE THR GLY GLY LYS
SEQRES 35 B 465 PRO LEU TYR SER ALA ILE LEU ALA ARG THR LEU ALA LYS
SEQRES 36 B 465 GLN GLU ALA GLU GLN LEU ALA ARG SER LYS
SEQRES 1 C 222 GLU VAL ARG LEU LEU GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 C 222 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY
SEQRES 3 C 222 PHE ASP TYR SER ARG TYR TRP MET SER TRP VAL ARG GLN
SEQRES 4 C 222 ALA PRO GLY LYS GLY LEU LYS TRP ILE GLY GLU ILE ASN
SEQRES 5 C 222 PRO VAL SER SER THR ILE ASN TYR THR PRO SER LEU LYS
SEQRES 6 C 222 ASP LYS PHE ILE ILE SER ARG ASP ASN ALA LYS ASP THR
SEQRES 7 C 222 LEU TYR LEU GLN ILE SER LYS VAL ARG SER GLU ASP THR
SEQRES 8 C 222 ALA LEU TYR TYR CYS ALA ARG LEU TYR TYR GLY TYR GLY
SEQRES 9 C 222 TYR TRP TYR PHE ASP VAL TRP GLY ALA GLY THR THR VAL
SEQRES 10 C 222 THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR
SEQRES 11 C 222 PRO LEU ALA PRO GLY SER ALA ALA ALA ALA ALA SER MET
SEQRES 12 C 222 VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU
SEQRES 13 C 222 PRO VAL THR VAL THR TRP ASN SER GLY SER LEU ALA ALA
SEQRES 14 C 222 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN ALA ALA LEU
SEQRES 15 C 222 TYR THR LEU SER SER SER VAL THR VAL PRO SER SER SER
SEQRES 16 C 222 TRP PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO
SEQRES 17 C 222 ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG
SEQRES 18 C 222 ALA
SEQRES 1 D 211 ASP ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA
SEQRES 2 D 211 ALA PRO GLY ASP LYS VAL THR MET THR CYS SER ALA SER
SEQRES 3 D 211 SER SER VAL SER TYR ILE HIS TRP TYR GLN GLN LYS SER
SEQRES 4 D 211 GLY THR SER PRO LYS ARG TRP ILE TYR ASP THR SER LYS
SEQRES 5 D 211 LEU THR SER GLY VAL PRO VAL ARG PHE SER GLY SER GLY
SEQRES 6 D 211 SER GLY THR SER TYR SER LEU THR ILE ASN THR MET GLU
SEQRES 7 D 211 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER
SEQRES 8 D 211 SER HIS PRO GLN THR PHE GLY GLY GLY THR LYS LEU GLU
SEQRES 9 D 211 ILE LEU ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 D 211 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER
SEQRES 11 D 211 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE
SEQRES 12 D 211 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN
SEQRES 13 D 211 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP
SEQRES 14 D 211 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS
SEQRES 15 D 211 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA
SEQRES 16 D 211 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE
SEQRES 17 D 211 ASN ARG ALA
SEQRES 1 E 222 GLU VAL ARG LEU LEU GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 E 222 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY
SEQRES 3 E 222 PHE ASP TYR SER ARG TYR TRP MET SER TRP VAL ARG GLN
SEQRES 4 E 222 ALA PRO GLY LYS GLY LEU LYS TRP ILE GLY GLU ILE ASN
SEQRES 5 E 222 PRO VAL SER SER THR ILE ASN TYR THR PRO SER LEU LYS
SEQRES 6 E 222 ASP LYS PHE ILE ILE SER ARG ASP ASN ALA LYS ASP THR
SEQRES 7 E 222 LEU TYR LEU GLN ILE SER LYS VAL ARG SER GLU ASP THR
SEQRES 8 E 222 ALA LEU TYR TYR CYS ALA ARG LEU TYR TYR GLY TYR GLY
SEQRES 9 E 222 TYR TRP TYR PHE ASP VAL TRP GLY ALA GLY THR THR VAL
SEQRES 10 E 222 THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR
SEQRES 11 E 222 PRO LEU ALA PRO GLY SER ALA ALA ALA ALA ALA SER MET
SEQRES 12 E 222 VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU
SEQRES 13 E 222 PRO VAL THR VAL THR TRP ASN SER GLY SER LEU ALA ALA
SEQRES 14 E 222 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN ALA ALA LEU
SEQRES 15 E 222 TYR THR LEU SER SER SER VAL THR VAL PRO SER SER SER
SEQRES 16 E 222 TRP PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO
SEQRES 17 E 222 ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG
SEQRES 18 E 222 ALA
SEQRES 1 F 211 ASP ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA
SEQRES 2 F 211 ALA PRO GLY ASP LYS VAL THR MET THR CYS SER ALA SER
SEQRES 3 F 211 SER SER VAL SER TYR ILE HIS TRP TYR GLN GLN LYS SER
SEQRES 4 F 211 GLY THR SER PRO LYS ARG TRP ILE TYR ASP THR SER LYS
SEQRES 5 F 211 LEU THR SER GLY VAL PRO VAL ARG PHE SER GLY SER GLY
SEQRES 6 F 211 SER GLY THR SER TYR SER LEU THR ILE ASN THR MET GLU
SEQRES 7 F 211 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER
SEQRES 8 F 211 SER HIS PRO GLN THR PHE GLY GLY GLY THR LYS LEU GLU
SEQRES 9 F 211 ILE LEU ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 F 211 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER
SEQRES 11 F 211 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE
SEQRES 12 F 211 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN
SEQRES 13 F 211 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP
SEQRES 14 F 211 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS
SEQRES 15 F 211 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA
SEQRES 16 F 211 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE
SEQRES 17 F 211 ASN ARG ALA
HET CL A 466 1
HET CL A 467 1
HET CL A 468 1
HET CL B 466 1
HET CL B 467 1
HET CL B 468 1
HETNAM CL CHLORIDE ION
FORMUL 7 CL 6(CL 1-)
HELIX 1 1 ARG A 17 LEU A 26 1 10
HELIX 2 2 PRO A 32 ALA A 67 1 36
HELIX 3 3 LEU A 68 ALA A 72 5 5
HELIX 4 4 ASN A 74 LYS A 99 1 26
HELIX 5 5 GLY A 108 GLU A 117 1 10
HELIX 6 6 ARG A 123 GLY A 142 1 20
HELIX 7 7 ARG A 147 PHE A 166 1 20
HELIX 8 8 ASP A 171 ASN A 191 1 21
HELIX 9 9 ALA A 192 ILE A 201 1 10
HELIX 10 10 SER A 214 ASN A 233 1 20
HELIX 11 11 PRO A 248 THR A 251 5 4
HELIX 12 12 LEU A 252 GLY A 285 1 34
HELIX 13 13 ASN A 287 GLY A 306 1 20
HELIX 14 14 ALA A 309 SER A 313 5 5
HELIX 15 15 ASN A 318 GLY A 326 1 9
HELIX 16 16 SER A 329 SER A 349 1 21
HELIX 17 17 ILE A 356 PHE A 379 1 24
HELIX 18 18 PRO A 380 HIS A 383 5 4
HELIX 19 19 ALA A 386 GLY A 393 1 8
HELIX 20 20 ALA A 404 ASP A 417 1 14
HELIX 21 21 ASN A 418 GLN A 420 5 3
HELIX 22 22 LEU A 421 PHE A 438 1 18
HELIX 23 23 PRO A 443 GLU A 457 1 15
HELIX 24 24 ARG B 18 LEU B 26 1 9
HELIX 25 25 PRO B 32 VAL B 69 1 38
HELIX 26 26 ASN B 74 LYS B 99 1 26
HELIX 27 27 GLY B 108 GLU B 117 1 10
HELIX 28 28 ARG B 123 GLY B 142 1 20
HELIX 29 29 ARG B 147 PHE B 166 1 20
HELIX 30 30 ASP B 171 ASN B 191 1 21
HELIX 31 31 ALA B 192 ILE B 201 1 10
HELIX 32 32 SER B 214 HIS B 234 1 21
HELIX 33 33 PRO B 248 THR B 251 5 4
HELIX 34 34 LEU B 252 LEU B 279 1 28
HELIX 35 35 LEU B 280 GLY B 285 1 6
HELIX 36 36 ASN B 287 GLY B 306 1 20
HELIX 37 37 ASN B 318 GLY B 326 1 9
HELIX 38 38 SER B 329 SER B 349 1 21
HELIX 39 39 ILE B 356 PHE B 379 1 24
HELIX 40 40 PRO B 380 HIS B 383 5 4
HELIX 41 41 GLU B 385 GLY B 393 1 9
HELIX 42 42 ALA B 404 ASP B 417 1 14
HELIX 43 43 ASN B 418 GLN B 420 5 3
HELIX 44 44 LEU B 421 THR B 439 1 19
HELIX 45 45 PRO B 443 LYS B 455 1 13
HELIX 46 46 ARG C 87 THR C 91 5 5
HELIX 47 47 SER C 164 SER C 166 5 3
HELIX 48 48 SER C 194 TRP C 196 5 3
HELIX 49 49 SER D 120 THR D 125 1 6
HELIX 50 50 LYS D 182 ARG D 187 1 6
HELIX 51 51 ASN E 74 LYS E 76 5 3
HELIX 52 52 ARG E 87 THR E 91 5 5
HELIX 53 53 SER E 164 SER E 166 5 3
HELIX 54 54 SER E 194 TRP E 196 5 3
HELIX 55 55 GLU F 78 ALA F 82 5 5
HELIX 56 56 SER F 120 THR F 125 1 6
HELIX 57 57 LYS F 182 ARG F 187 1 6
SHEET 1 A 4 ARG C 3 SER C 7 0
SHEET 2 A 4 SER C 17 SER C 25 -1 O SER C 25 N ARG C 3
SHEET 3 A 4 THR C 78 SER C 84 -1 O LEU C 81 N LEU C 20
SHEET 4 A 4 PHE C 68 ASP C 73 -1 N SER C 71 O TYR C 80
SHEET 1 B 5 ILE C 58 TYR C 60 0
SHEET 2 B 5 LEU C 45 ILE C 51 -1 N GLU C 50 O ASN C 59
SHEET 3 B 5 TRP C 33 GLN C 39 -1 N TRP C 36 O ILE C 48
SHEET 4 B 5 ALA C 92 TYR C 100 -1 O LEU C 93 N GLN C 39
SHEET 5 B 5 TYR C 107 VAL C 110 -1 O TYR C 107 N TYR C 100
SHEET 1 C 6 ILE C 58 TYR C 60 0
SHEET 2 C 6 LEU C 45 ILE C 51 -1 N GLU C 50 O ASN C 59
SHEET 3 C 6 TRP C 33 GLN C 39 -1 N TRP C 36 O ILE C 48
SHEET 4 C 6 ALA C 92 TYR C 100 -1 O LEU C 93 N GLN C 39
SHEET 5 C 6 THR C 115 VAL C 119 -1 O THR C 115 N TYR C 94
SHEET 6 C 6 GLY C 10 VAL C 12 1 N GLY C 10 O THR C 118
SHEET 1 D 4 SER C 128 PRO C 131 0
SHEET 2 D 4 MET C 143 TYR C 153 -1 O LYS C 151 N SER C 128
SHEET 3 D 4 TYR C 183 PRO C 192 -1 O VAL C 191 N VAL C 144
SHEET 4 D 4 VAL C 171 THR C 173 -1 N HIS C 172 O SER C 188
SHEET 1 E 4 SER C 128 PRO C 131 0
SHEET 2 E 4 MET C 143 TYR C 153 -1 O LYS C 151 N SER C 128
SHEET 3 E 4 TYR C 183 PRO C 192 -1 O VAL C 191 N VAL C 144
SHEET 4 E 4 VAL C 177 LEU C 178 -1 N VAL C 177 O THR C 184
SHEET 1 F 3 THR C 161 TRP C 162 0
SHEET 2 F 3 THR C 202 HIS C 207 -1 O ASN C 204 N THR C 161
SHEET 3 F 3 THR C 212 LYS C 217 -1 O LYS C 216 N CYS C 203
SHEET 1 G 4 LYS D 44 ARG D 45 0
SHEET 2 G 4 HIS D 33 GLN D 37 -1 N GLN D 36 O LYS D 44
SHEET 3 G 4 ALA D 83 GLN D 89 -1 O TYR D 86 N TYR D 35
SHEET 4 G 4 THR D 96 PHE D 97 -1 O THR D 96 N GLN D 89
SHEET 1 H 5 LYS D 44 ARG D 45 0
SHEET 2 H 5 HIS D 33 GLN D 37 -1 N GLN D 36 O LYS D 44
SHEET 3 H 5 ALA D 83 GLN D 89 -1 O TYR D 86 N TYR D 35
SHEET 4 H 5 THR D 101 GLU D 104 -1 O LEU D 103 N ALA D 83
SHEET 5 H 5 ILE D 10 SER D 12 1 N MET D 11 O GLU D 104
SHEET 1 I 3 VAL D 19 SER D 24 0
SHEET 2 I 3 SER D 69 ILE D 74 -1 O ILE D 74 N VAL D 19
SHEET 3 I 3 PHE D 61 SER D 66 -1 N SER D 62 O THR D 73
SHEET 1 J 2 ILE D 47 TYR D 48 0
SHEET 2 J 2 LYS D 52 LEU D 53 -1 O LYS D 52 N TYR D 48
SHEET 1 K 4 THR D 113 ILE D 116 0
SHEET 2 K 4 GLY D 128 PHE D 138 -1 O PHE D 134 N SER D 115
SHEET 3 K 4 TYR D 172 THR D 181 -1 O LEU D 178 N VAL D 131
SHEET 4 K 4 VAL D 158 TRP D 162 -1 N LEU D 159 O THR D 177
SHEET 1 L 3 ILE D 143 ILE D 149 0
SHEET 2 L 3 SER D 190 HIS D 197 -1 O THR D 196 N ASN D 144
SHEET 3 L 3 ILE D 204 VAL D 205 -1 O ILE D 204 N ALA D 195
SHEET 1 M 3 ILE D 143 ILE D 149 0
SHEET 2 M 3 SER D 190 HIS D 197 -1 O THR D 196 N ASN D 144
SHEET 3 M 3 PHE D 208 ASN D 209 -1 O PHE D 208 N TYR D 191
SHEET 1 N 4 ARG E 3 LEU E 5 0
SHEET 2 N 4 LEU E 18 SER E 25 -1 O SER E 25 N ARG E 3
SHEET 3 N 4 THR E 78 ILE E 83 -1 O LEU E 79 N CYS E 22
SHEET 4 N 4 PHE E 68 ASP E 73 -1 N SER E 71 O TYR E 80
SHEET 1 O 5 ILE E 58 TYR E 60 0
SHEET 2 O 5 LEU E 45 ILE E 51 -1 N GLU E 50 O ASN E 59
SHEET 3 O 5 TRP E 33 GLN E 39 -1 N MET E 34 O ILE E 51
SHEET 4 O 5 ALA E 92 TYR E 100 -1 O LEU E 93 N GLN E 39
SHEET 5 O 5 TYR E 107 PHE E 108 -1 O TYR E 107 N TYR E 100
SHEET 1 P 6 ILE E 58 TYR E 60 0
SHEET 2 P 6 LEU E 45 ILE E 51 -1 N GLU E 50 O ASN E 59
SHEET 3 P 6 TRP E 33 GLN E 39 -1 N MET E 34 O ILE E 51
SHEET 4 P 6 ALA E 92 TYR E 100 -1 O LEU E 93 N GLN E 39
SHEET 5 P 6 THR E 116 VAL E 119 -1 O VAL E 117 N ALA E 92
SHEET 6 P 6 GLY E 10 VAL E 12 1 N GLY E 10 O THR E 118
SHEET 1 Q 4 SER E 128 PRO E 131 0
SHEET 2 Q 4 MET E 143 TYR E 153 -1 O LEU E 149 N TYR E 130
SHEET 3 Q 4 TYR E 183 PRO E 192 -1 O VAL E 191 N VAL E 144
SHEET 4 Q 4 VAL E 171 THR E 173 -1 N HIS E 172 O SER E 188
SHEET 1 R 4 SER E 128 PRO E 131 0
SHEET 2 R 4 MET E 143 TYR E 153 -1 O LEU E 149 N TYR E 130
SHEET 3 R 4 TYR E 183 PRO E 192 -1 O VAL E 191 N VAL E 144
SHEET 4 R 4 VAL E 177 LEU E 178 -1 N VAL E 177 O THR E 184
SHEET 1 S 3 THR E 159 TRP E 162 0
SHEET 2 S 3 THR E 202 HIS E 207 -1 O ASN E 204 N THR E 161
SHEET 3 S 3 THR E 212 LYS E 217 -1 O VAL E 214 N VAL E 205
SHEET 1 T 4 THR F 5 GLN F 6 0
SHEET 2 T 4 VAL F 19 SER F 24 -1 O SER F 24 N THR F 5
SHEET 3 T 4 SER F 69 ILE F 74 -1 O ILE F 74 N VAL F 19
SHEET 4 T 4 PHE F 61 SER F 64 -1 N SER F 62 O THR F 73
SHEET 1 U 5 ILE F 10 ALA F 13 0
SHEET 2 U 5 THR F 101 ILE F 105 1 O LYS F 102 N MET F 11
SHEET 3 U 5 THR F 84 GLN F 89 -1 N TYR F 85 O THR F 101
SHEET 4 U 5 HIS F 33 GLN F 37 -1 N TYR F 35 O TYR F 86
SHEET 5 U 5 LYS F 44 ARG F 45 -1 O LYS F 44 N GLN F 36
SHEET 1 V 4 ILE F 10 ALA F 13 0
SHEET 2 V 4 THR F 101 ILE F 105 1 O LYS F 102 N MET F 11
SHEET 3 V 4 THR F 84 GLN F 89 -1 N TYR F 85 O THR F 101
SHEET 4 V 4 THR F 96 PHE F 97 -1 O THR F 96 N GLN F 89
SHEET 1 W 2 ILE F 47 TYR F 48 0
SHEET 2 W 2 LYS F 52 LEU F 53 -1 O LYS F 52 N TYR F 48
SHEET 1 X 4 VAL F 114 PHE F 117 0
SHEET 2 X 4 GLY F 128 PHE F 138 -1 O VAL F 132 N PHE F 117
SHEET 3 X 4 TYR F 172 THR F 181 -1 O LEU F 178 N VAL F 131
SHEET 4 X 4 VAL F 158 TRP F 162 -1 N LEU F 159 O THR F 177
SHEET 1 Y 3 ILE F 143 ILE F 149 0
SHEET 2 Y 3 SER F 190 HIS F 197 -1 O THR F 196 N ASN F 144
SHEET 3 Y 3 ILE F 204 VAL F 205 -1 O ILE F 204 N ALA F 195
SHEET 1 Z 3 ILE F 143 ILE F 149 0
SHEET 2 Z 3 SER F 190 HIS F 197 -1 O THR F 196 N ASN F 144
SHEET 3 Z 3 PHE F 208 ASN F 209 -1 O PHE F 208 N TYR F 191
SSBOND 1 CYS C 22 CYS C 96 1555 1555 2.03
SSBOND 2 CYS C 148 CYS C 203 1555 1555 2.03
SSBOND 3 CYS D 23 CYS D 87 1555 1555 2.04
SSBOND 4 CYS D 133 CYS D 193 1555 1555 2.05
SSBOND 5 CYS E 22 CYS E 96 1555 1555 2.03
SSBOND 6 CYS E 148 CYS E 203 1555 1555 2.03
SSBOND 7 CYS F 23 CYS F 87 1555 1555 2.05
SSBOND 8 CYS F 133 CYS F 193 1555 1555 2.04
CISPEP 1 PHE C 154 PRO C 155 0 1.18
CISPEP 2 GLU C 156 PRO C 157 0 0.17
CISPEP 3 HIS D 93 PRO D 94 0 -0.08
CISPEP 4 TYR D 139 PRO D 140 0 -0.72
CISPEP 5 PHE E 154 PRO E 155 0 0.37
CISPEP 6 GLU E 156 PRO E 157 0 1.09
CISPEP 7 HIS F 93 PRO F 94 0 0.00
CISPEP 8 TYR F 139 PRO F 140 0 0.13
SITE 1 AC1 7 GLY A 146 ARG A 147 ALA A 148 GLY A 355
SITE 2 AC1 7 ILE A 356 PHE A 357 ALA A 358
SITE 1 AC2 5 SER A 107 GLY A 149 GLY A 355 ILE A 356
SITE 2 AC2 5 TYR A 445
SITE 1 AC3 2 GLY A 106 SER A 107
SITE 1 AC4 6 GLY B 146 ARG B 147 ALA B 148 GLY B 355
SITE 2 AC4 6 PHE B 357 ALA B 358
SITE 1 AC5 5 SER B 107 GLY B 149 GLY B 355 ILE B 356
SITE 2 AC5 5 TYR B 445
SITE 1 AC6 3 SER B 107 PRO B 110 ILE B 448
CRYST1 231.614 95.719 169.819 90.00 131.45 90.00 C 1 2 1 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 0.004318 0.000000 0.003814 0.00000
SCALE2 0.000000 0.010447 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007857 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
