HEADER MEMBRANE PROTEIN 26-JUL-06 2HTL
TITLE STRUCTURE OF THE ESCHERICHIA COLI CLC CHLORIDE CHANNEL Y445F MUTANT
TITLE 2 AND FAB COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H(+)/CL(-) EXCHANGE TRANSPORTER CLCA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 1ECCLC H+/CL- ANTIPORTER; CLC-EC1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: FAB FRAGMENT, HEAVY CHAIN;
COMPND 9 CHAIN: C, E;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: FAB FRAGMENT, LIGHT CHAIN;
COMPND 12 CHAIN: D, F
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: CLCA, ERIC;
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: PET 28B+;
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 CLC FAMILY OF CHANNEL AND TRANSPORTERS, H+/CL- ANTIPORTER, MEMBRANE
KEYWDS 2 PROTEIN, FAB COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ACCARDI,S.LOBET,C.WILLIAMS,C.MILLER,R.DUTZLER
REVDAT 3 20-OCT-21 2HTL 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2HTL 1 VERSN
REVDAT 1 19-SEP-06 2HTL 0
JRNL AUTH A.ACCARDI,S.LOBET,C.WILLIAMS,C.MILLER,R.DUTZLER
JRNL TITL SYNERGISM BETWEEN HALIDE BINDING AND PROTON TRANSPORT IN A
JRNL TITL 2 CLC-TYPE EXCHANGER.
JRNL REF J.MOL.BIOL. V. 362 691 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16949616
JRNL DOI 10.1016/J.JMB.2006.07.081
REMARK 2
REMARK 2 RESOLUTION. 3.40 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) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 37989
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) : 0.262
REMARK 3 R VALUE (WORKING SET) : 0.259
REMARK 3 FREE R VALUE : 0.302
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2040
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) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2730
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.4000
REMARK 3 BIN FREE R VALUE SET COUNT : 159
REMARK 3 BIN FREE R VALUE : 0.4280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13221
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 95.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 124.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.19000
REMARK 3 B22 (A**2) : 1.27000
REMARK 3 B33 (A**2) : -0.28000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.60000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.556
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.618
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 : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13549 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18448 ; 1.189 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1743 ; 5.375 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 479 ;34.394 ;22.985
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2145 ;18.890 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 67 ;17.093 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2121 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10077 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7337 ; 0.236 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 9321 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 458 ; 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): 21 ; 0.162 ; 0.200
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): 8655 ;18.656 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13908 ;25.539 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4894 ; 1.980 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4540 ; 2.340 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 18 A 458 5
REMARK 3 1 B 18 B 458 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1764 ; 0.03 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 1539 ; 0.42 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1764 ; 14.74 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1539 ; 15.72 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 2HTL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1000038745.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9193
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37989
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 39% PEG 300, 50MM TRIS, 150MM NAKTART,
REMARK 280 PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 116.26250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.43000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 116.26250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.43000
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: 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 ALA A 466
REMARK 465 ALA A 467
REMARK 465 SER A 468
REMARK 465 ALA A 469
REMARK 465 SER A 470
REMARK 465 GLU A 471
REMARK 465 ASN A 472
REMARK 465 THR A 473
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 ALA B 466
REMARK 465 ALA B 467
REMARK 465 SER B 468
REMARK 465 ALA B 469
REMARK 465 SER B 470
REMARK 465 GLU B 471
REMARK 465 ASN B 472
REMARK 465 THR B 473
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 LYS E 19 CE LYS E 19 NZ 0.154
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 73 -107.82 -82.14
REMARK 500 ASN A 74 92.16 -20.67
REMARK 500 ALA A 101 88.27 -168.39
REMARK 500 SER A 107 -76.59 -72.17
REMARK 500 VAL A 122 73.75 -109.24
REMARK 500 ARG A 126 -61.43 -98.57
REMARK 500 GLU A 202 -21.98 -144.52
REMARK 500 GLU A 203 -56.52 -135.49
REMARK 500 PHE A 307 -41.18 -131.37
REMARK 500 ALA A 309 68.62 -170.24
REMARK 500 SER A 313 -169.22 -101.57
REMARK 500 ALA A 404 77.25 -118.84
REMARK 500 PRO A 443 108.23 -51.30
REMARK 500 ASP B 73 -104.45 -85.93
REMARK 500 ASN B 74 96.38 -25.52
REMARK 500 ALA B 101 90.54 -164.73
REMARK 500 SER B 107 -79.14 -67.40
REMARK 500 ASP B 118 15.55 59.50
REMARK 500 VAL B 122 73.54 -108.97
REMARK 500 LEU B 128 -70.30 -36.33
REMARK 500 PHE B 132 -73.54 -42.80
REMARK 500 GLU B 202 -24.31 -142.54
REMARK 500 GLU B 203 -55.55 -134.94
REMARK 500 PHE B 219 -70.22 -47.51
REMARK 500 PHE B 307 -43.65 -132.03
REMARK 500 ALA B 309 67.96 -168.49
REMARK 500 ALA B 386 -38.24 -39.78
REMARK 500 PRO B 443 106.57 -52.57
REMARK 500 SER C 30 -172.60 -67.31
REMARK 500 ARG C 31 -30.06 64.51
REMARK 500 SER C 55 22.37 45.20
REMARK 500 PRO C 62 90.27 -42.90
REMARK 500 LYS C 67 -70.20 -47.88
REMARK 500 THR C 91 98.17 -57.32
REMARK 500 ASP C 109 -77.51 -58.75
REMARK 500 ALA C 140 93.39 -66.16
REMARK 500 ALA C 141 -138.65 -81.21
REMARK 500 LEU C 146 -155.96 -110.83
REMARK 500 ALA C 180 54.34 29.88
REMARK 500 SER D 27 -154.92 -151.05
REMARK 500 TYR D 31 70.72 44.48
REMARK 500 TRP D 46 -64.94 -105.02
REMARK 500 THR D 50 -25.37 61.41
REMARK 500 SER D 51 -10.61 -152.82
REMARK 500 SER D 62 141.58 -177.16
REMARK 500 SER D 64 -165.01 -172.29
REMARK 500 THR D 76 95.84 63.10
REMARK 500 GLU D 80 17.98 -63.20
REMARK 500 ALA D 83 -156.09 -156.87
REMARK 500 TRP D 90 31.97 -149.60
REMARK 500
REMARK 500 THIS ENTRY HAS 90 RAMACHANDRAN OUTLIERS.
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 BR A 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 475
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 475
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OTS RELATED DB: PDB
REMARK 900 STRUCTURE OF THE ESCHERICHIA COLI CLC CHLORIDE CHANNEL AND FAB
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 2HT2 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE ESCHERICHIA COLI CLC CHLORIDE CHANNEL Y445H MUTANT
REMARK 900 AND FAB COMPLEX
REMARK 900 RELATED ID: 2HT3 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE ESCHERICHIA COLI CLC CHLORIDE CHANNEL Y445L MUTANT
REMARK 900 AND FAB COMPLEX
REMARK 900 RELATED ID: 2HT4 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE ESCHERICHIA COLI CLC CHLORIDE CHANNEL Y445W MUTANT
REMARK 900 AND FAB COMPLEX
REMARK 900 RELATED ID: 2HTK RELATED DB: PDB
REMARK 900 STRUCTURE OF THE ESCHERICHIA COLI CLC CHLORIDE CHANNEL Y445A MUTANT
REMARK 900 AND FAB COMPLEX
REMARK 900 RELATED ID: 2HLF RELATED DB: PDB
REMARK 900 STRUCTURE OF THE ESCHERICHIA COLI CLC CHLORIDE CHANNEL Y445E MUTANT
REMARK 900 AND FAB COMPLEX
DBREF 2HTL A 1 473 UNP P37019 CLCA_ECOLI 1 473
DBREF 2HTL B 1 473 UNP P37019 CLCA_ECOLI 1 473
DBREF 2HTL C 2 222 PDB 2HTL 2HTL 2 222
DBREF 2HTL D 1 211 PDB 2HTL 2HTL 1 211
DBREF 2HTL E 2 222 PDB 2HTL 2HTL 2 222
DBREF 2HTL F 1 211 PDB 2HTL 2HTL 1 211
SEQADV 2HTL PHE A 445 UNP P37019 TYR 445 ENGINEERED MUTATION
SEQADV 2HTL PHE B 445 UNP P37019 TYR 445 ENGINEERED MUTATION
SEQRES 1 A 473 MET LYS THR ASP THR PRO SER LEU GLU THR PRO GLN ALA
SEQRES 2 A 473 ALA ARG LEU ARG ARG ARG GLN LEU ILE ARG GLN LEU LEU
SEQRES 3 A 473 GLU ARG ASP LYS THR PRO LEU ALA ILE LEU PHE MET ALA
SEQRES 4 A 473 ALA VAL VAL GLY THR LEU VAL GLY LEU ALA ALA VAL ALA
SEQRES 5 A 473 PHE ASP LYS GLY VAL ALA TRP LEU GLN ASN GLN ARG MET
SEQRES 6 A 473 GLY ALA LEU VAL HIS THR ALA ASP ASN TYR PRO LEU LEU
SEQRES 7 A 473 LEU THR VAL ALA PHE LEU CYS SER ALA VAL LEU ALA MET
SEQRES 8 A 473 PHE GLY TYR PHE LEU VAL ARG LYS TYR ALA PRO GLU ALA
SEQRES 9 A 473 GLY GLY SER GLY ILE PRO GLU ILE GLU GLY ALA LEU GLU
SEQRES 10 A 473 ASP GLN ARG PRO VAL ARG TRP TRP ARG VAL LEU PRO VAL
SEQRES 11 A 473 LYS PHE PHE GLY GLY LEU GLY THR LEU GLY GLY GLY MET
SEQRES 12 A 473 VAL LEU GLY ARG GLU GLY PRO THR VAL GLN ILE GLY GLY
SEQRES 13 A 473 ASN ILE GLY ARG MET VAL LEU ASP ILE PHE ARG LEU LYS
SEQRES 14 A 473 GLY ASP GLU ALA ARG HIS THR LEU LEU ALA THR GLY ALA
SEQRES 15 A 473 ALA ALA GLY LEU ALA ALA ALA PHE ASN ALA PRO LEU ALA
SEQRES 16 A 473 GLY ILE LEU PHE ILE ILE GLU GLU MET ARG PRO GLN PHE
SEQRES 17 A 473 ARG TYR THR LEU ILE SER ILE LYS ALA VAL PHE ILE GLY
SEQRES 18 A 473 VAL ILE MET SER THR ILE MET TYR ARG ILE PHE ASN HIS
SEQRES 19 A 473 GLU VAL ALA LEU ILE ASP VAL GLY LYS LEU SER ASP ALA
SEQRES 20 A 473 PRO LEU ASN THR LEU TRP LEU TYR LEU ILE LEU GLY ILE
SEQRES 21 A 473 ILE PHE GLY ILE PHE GLY PRO ILE PHE ASN LYS TRP VAL
SEQRES 22 A 473 LEU GLY MET GLN ASP LEU LEU HIS ARG VAL HIS GLY GLY
SEQRES 23 A 473 ASN ILE THR LYS TRP VAL LEU MET GLY GLY ALA ILE GLY
SEQRES 24 A 473 GLY LEU CYS GLY LEU LEU GLY PHE VAL ALA PRO ALA THR
SEQRES 25 A 473 SER GLY GLY GLY PHE ASN LEU ILE PRO ILE ALA THR ALA
SEQRES 26 A 473 GLY ASN PHE SER MET GLY MET LEU VAL PHE ILE PHE VAL
SEQRES 27 A 473 ALA ARG VAL ILE THR THR LEU LEU CYS PHE SER SER GLY
SEQRES 28 A 473 ALA PRO GLY GLY ILE PHE ALA PRO MET LEU ALA LEU GLY
SEQRES 29 A 473 THR VAL LEU GLY THR ALA PHE GLY MET VAL ALA VAL GLU
SEQRES 30 A 473 LEU PHE PRO GLN TYR HIS LEU GLU ALA GLY THR PHE ALA
SEQRES 31 A 473 ILE ALA GLY MET GLY ALA LEU LEU ALA ALA SER ILE ARG
SEQRES 32 A 473 ALA PRO LEU THR GLY ILE ILE LEU VAL LEU GLU MET THR
SEQRES 33 A 473 ASP ASN TYR GLN LEU ILE LEU PRO MET ILE ILE THR GLY
SEQRES 34 A 473 LEU GLY ALA THR LEU LEU ALA GLN PHE THR GLY GLY LYS
SEQRES 35 A 473 PRO LEU PHE SER ALA ILE LEU ALA ARG THR LEU ALA LYS
SEQRES 36 A 473 GLN GLU ALA GLU GLN LEU ALA ARG SER LYS ALA ALA SER
SEQRES 37 A 473 ALA SER GLU ASN THR
SEQRES 1 B 473 MET LYS THR ASP THR PRO SER LEU GLU THR PRO GLN ALA
SEQRES 2 B 473 ALA ARG LEU ARG ARG ARG GLN LEU ILE ARG GLN LEU LEU
SEQRES 3 B 473 GLU ARG ASP LYS THR PRO LEU ALA ILE LEU PHE MET ALA
SEQRES 4 B 473 ALA VAL VAL GLY THR LEU VAL GLY LEU ALA ALA VAL ALA
SEQRES 5 B 473 PHE ASP LYS GLY VAL ALA TRP LEU GLN ASN GLN ARG MET
SEQRES 6 B 473 GLY ALA LEU VAL HIS THR ALA ASP ASN TYR PRO LEU LEU
SEQRES 7 B 473 LEU THR VAL ALA PHE LEU CYS SER ALA VAL LEU ALA MET
SEQRES 8 B 473 PHE GLY TYR PHE LEU VAL ARG LYS TYR ALA PRO GLU ALA
SEQRES 9 B 473 GLY GLY SER GLY ILE PRO GLU ILE GLU GLY ALA LEU GLU
SEQRES 10 B 473 ASP GLN ARG PRO VAL ARG TRP TRP ARG VAL LEU PRO VAL
SEQRES 11 B 473 LYS PHE PHE GLY GLY LEU GLY THR LEU GLY GLY GLY MET
SEQRES 12 B 473 VAL LEU GLY ARG GLU GLY PRO THR VAL GLN ILE GLY GLY
SEQRES 13 B 473 ASN ILE GLY ARG MET VAL LEU ASP ILE PHE ARG LEU LYS
SEQRES 14 B 473 GLY ASP GLU ALA ARG HIS THR LEU LEU ALA THR GLY ALA
SEQRES 15 B 473 ALA ALA GLY LEU ALA ALA ALA PHE ASN ALA PRO LEU ALA
SEQRES 16 B 473 GLY ILE LEU PHE ILE ILE GLU GLU MET ARG PRO GLN PHE
SEQRES 17 B 473 ARG TYR THR LEU ILE SER ILE LYS ALA VAL PHE ILE GLY
SEQRES 18 B 473 VAL ILE MET SER THR ILE MET TYR ARG ILE PHE ASN HIS
SEQRES 19 B 473 GLU VAL ALA LEU ILE ASP VAL GLY LYS LEU SER ASP ALA
SEQRES 20 B 473 PRO LEU ASN THR LEU TRP LEU TYR LEU ILE LEU GLY ILE
SEQRES 21 B 473 ILE PHE GLY ILE PHE GLY PRO ILE PHE ASN LYS TRP VAL
SEQRES 22 B 473 LEU GLY MET GLN ASP LEU LEU HIS ARG VAL HIS GLY GLY
SEQRES 23 B 473 ASN ILE THR LYS TRP VAL LEU MET GLY GLY ALA ILE GLY
SEQRES 24 B 473 GLY LEU CYS GLY LEU LEU GLY PHE VAL ALA PRO ALA THR
SEQRES 25 B 473 SER GLY GLY GLY PHE ASN LEU ILE PRO ILE ALA THR ALA
SEQRES 26 B 473 GLY ASN PHE SER MET GLY MET LEU VAL PHE ILE PHE VAL
SEQRES 27 B 473 ALA ARG VAL ILE THR THR LEU LEU CYS PHE SER SER GLY
SEQRES 28 B 473 ALA PRO GLY GLY ILE PHE ALA PRO MET LEU ALA LEU GLY
SEQRES 29 B 473 THR VAL LEU GLY THR ALA PHE GLY MET VAL ALA VAL GLU
SEQRES 30 B 473 LEU PHE PRO GLN TYR HIS LEU GLU ALA GLY THR PHE ALA
SEQRES 31 B 473 ILE ALA GLY MET GLY ALA LEU LEU ALA ALA SER ILE ARG
SEQRES 32 B 473 ALA PRO LEU THR GLY ILE ILE LEU VAL LEU GLU MET THR
SEQRES 33 B 473 ASP ASN TYR GLN LEU ILE LEU PRO MET ILE ILE THR GLY
SEQRES 34 B 473 LEU GLY ALA THR LEU LEU ALA GLN PHE THR GLY GLY LYS
SEQRES 35 B 473 PRO LEU PHE SER ALA ILE LEU ALA ARG THR LEU ALA LYS
SEQRES 36 B 473 GLN GLU ALA GLU GLN LEU ALA ARG SER LYS ALA ALA SER
SEQRES 37 B 473 ALA SER GLU ASN THR
SEQRES 1 C 221 VAL ARG LEU LEU GLU SER GLY GLY GLY LEU VAL GLN PRO
SEQRES 2 C 221 GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY PHE
SEQRES 3 C 221 ASP TYR SER ARG TYR TRP MET SER TRP VAL ARG GLN ALA
SEQRES 4 C 221 PRO GLY LYS GLY LEU LYS TRP ILE GLY GLU ILE ASN PRO
SEQRES 5 C 221 VAL SER SER THR ILE ASN TYR THR PRO SER LEU LYS ASP
SEQRES 6 C 221 LYS PHE ILE ILE SER ARG ASP ASN ALA LYS ASP THR LEU
SEQRES 7 C 221 TYR LEU GLN ILE SER LYS VAL ARG SER GLU ASP THR ALA
SEQRES 8 C 221 LEU TYR TYR CYS ALA ARG LEU TYR TYR GLY TYR GLY TYR
SEQRES 9 C 221 TRP TYR PHE ASP VAL TRP GLY ALA GLY THR THR VAL THR
SEQRES 10 C 221 VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO
SEQRES 11 C 221 LEU ALA PRO GLY SER ALA ALA ALA ALA ALA SER MET VAL
SEQRES 12 C 221 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO
SEQRES 13 C 221 VAL THR VAL THR TRP ASN SER GLY SER LEU ALA ALA GLY
SEQRES 14 C 221 VAL HIS THR PHE PRO ALA VAL LEU GLN ALA ALA LEU TYR
SEQRES 15 C 221 THR LEU SER SER SER VAL THR VAL PRO SER SER SER TRP
SEQRES 16 C 221 PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA
SEQRES 17 C 221 SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG 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 221 VAL ARG LEU LEU GLU SER GLY GLY GLY LEU VAL GLN PRO
SEQRES 2 E 221 GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY PHE
SEQRES 3 E 221 ASP TYR SER ARG TYR TRP MET SER TRP VAL ARG GLN ALA
SEQRES 4 E 221 PRO GLY LYS GLY LEU LYS TRP ILE GLY GLU ILE ASN PRO
SEQRES 5 E 221 VAL SER SER THR ILE ASN TYR THR PRO SER LEU LYS ASP
SEQRES 6 E 221 LYS PHE ILE ILE SER ARG ASP ASN ALA LYS ASP THR LEU
SEQRES 7 E 221 TYR LEU GLN ILE SER LYS VAL ARG SER GLU ASP THR ALA
SEQRES 8 E 221 LEU TYR TYR CYS ALA ARG LEU TYR TYR GLY TYR GLY TYR
SEQRES 9 E 221 TRP TYR PHE ASP VAL TRP GLY ALA GLY THR THR VAL THR
SEQRES 10 E 221 VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO
SEQRES 11 E 221 LEU ALA PRO GLY SER ALA ALA ALA ALA ALA SER MET VAL
SEQRES 12 E 221 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO
SEQRES 13 E 221 VAL THR VAL THR TRP ASN SER GLY SER LEU ALA ALA GLY
SEQRES 14 E 221 VAL HIS THR PHE PRO ALA VAL LEU GLN ALA ALA LEU TYR
SEQRES 15 E 221 THR LEU SER SER SER VAL THR VAL PRO SER SER SER TRP
SEQRES 16 E 221 PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA
SEQRES 17 E 221 SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG 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 BR A 474 1
HET BR A 475 1
HET BR B 474 1
HET BR B 475 1
HETNAM BR BROMIDE ION
FORMUL 7 BR 4(BR 1-)
HELIX 1 1 ARG A 17 LEU A 26 1 10
HELIX 2 2 PRO A 32 THR A 71 1 40
HELIX 3 3 ASN A 74 ALA A 101 1 28
HELIX 4 4 PRO A 102 GLY A 105 5 4
HELIX 5 5 GLY A 108 GLU A 117 1 10
HELIX 6 6 ARG A 123 GLY A 141 1 19
HELIX 7 7 ARG A 147 PHE A 166 1 20
HELIX 8 8 GLY A 170 ASN A 191 1 22
HELIX 9 9 ALA A 192 ILE A 201 1 10
HELIX 10 10 SER A 214 HIS A 234 1 21
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 ALA A 309 1 23
HELIX 14 14 ASN A 318 ALA A 325 1 8
HELIX 15 15 SER A 329 SER A 349 1 21
HELIX 16 16 ILE A 356 PHE A 379 1 24
HELIX 17 17 PRO A 380 HIS A 383 5 4
HELIX 18 18 GLU A 385 GLY A 395 1 11
HELIX 19 19 GLY A 395 SER A 401 1 7
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 ALA A 458 1 16
HELIX 24 24 ARG B 18 LEU B 26 1 9
HELIX 25 25 PRO B 32 THR B 71 1 40
HELIX 26 26 ASN B 74 ALA B 101 1 28
HELIX 27 27 PRO B 102 GLY B 105 5 4
HELIX 28 28 GLY B 108 GLU B 117 1 10
HELIX 29 29 ARG B 123 GLY B 141 1 19
HELIX 30 30 ARG B 147 PHE B 166 1 20
HELIX 31 31 GLY B 170 ALA B 188 1 19
HELIX 32 32 ALA B 192 ILE B 201 1 10
HELIX 33 33 SER B 214 HIS B 234 1 21
HELIX 34 34 PRO B 248 ASN B 250 5 3
HELIX 35 35 THR B 251 GLY B 285 1 35
HELIX 36 36 ASN B 287 ALA B 309 1 23
HELIX 37 37 ASN B 318 ALA B 325 1 8
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 395 1 11
HELIX 42 42 GLY B 395 SER B 401 1 7
HELIX 43 43 ALA B 404 ASP B 417 1 14
HELIX 44 44 ASN B 418 GLN B 420 5 3
HELIX 45 45 LEU B 421 PHE B 438 1 18
HELIX 46 46 PRO B 443 ALA B 458 1 16
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 PRO C 208 SER C 211 5 4
HELIX 50 50 GLU D 78 ALA D 82 5 5
HELIX 51 51 SER D 120 THR D 125 1 6
HELIX 52 52 LYS D 182 ARG D 187 1 6
HELIX 53 53 ASN E 74 LYS E 76 5 3
HELIX 54 54 ARG E 87 THR E 91 5 5
HELIX 55 55 SER E 164 SER E 166 5 3
HELIX 56 56 SER E 194 TRP E 196 5 3
HELIX 57 57 PRO E 208 SER E 211 5 4
HELIX 58 58 GLU F 78 ALA F 82 5 5
HELIX 59 59 SER F 120 THR F 125 1 6
HELIX 60 60 LYS F 182 ARG F 187 1 6
SHEET 1 A 4 ARG C 3 SER C 7 0
SHEET 2 A 4 LEU C 18 SER C 25 -1 O SER C 25 N ARG C 3
SHEET 3 A 4 THR C 78 ILE C 83 -1 O LEU C 79 N CYS C 22
SHEET 4 A 4 PHE C 68 ASP C 73 -1 N SER C 71 O TYR C 80
SHEET 1 B 6 LEU C 11 VAL C 12 0
SHEET 2 B 6 THR C 115 VAL C 119 1 O THR C 118 N VAL C 12
SHEET 3 B 6 ALA C 92 TYR C 100 -1 N TYR C 94 O THR C 115
SHEET 4 B 6 TRP C 33 GLN C 39 -1 N SER C 35 O ALA C 97
SHEET 5 B 6 LEU C 45 ILE C 51 -1 O ILE C 51 N MET C 34
SHEET 6 B 6 ILE C 58 TYR C 60 -1 O ASN C 59 N GLU C 50
SHEET 1 C 4 LEU C 11 VAL C 12 0
SHEET 2 C 4 THR C 115 VAL C 119 1 O THR C 118 N VAL C 12
SHEET 3 C 4 ALA C 92 TYR C 100 -1 N TYR C 94 O THR C 115
SHEET 4 C 4 TYR C 107 TRP C 111 -1 O TYR C 107 N TYR C 100
SHEET 1 D 4 SER C 128 PRO C 131 0
SHEET 2 D 4 CYS C 148 TYR C 153 -1 O LEU C 149 N TYR C 130
SHEET 3 D 4 LEU C 182 PRO C 192 -1 O TYR C 183 N TYR C 153
SHEET 4 D 4 VAL C 171 THR C 173 -1 N HIS C 172 O SER C 188
SHEET 1 E 3 MET C 143 THR C 145 0
SHEET 2 E 3 LEU C 182 PRO C 192 -1 O VAL C 191 N VAL C 144
SHEET 3 E 3 VAL C 177 GLN C 179 -1 N GLN C 179 O LEU C 182
SHEET 1 F 3 THR C 159 TRP C 162 0
SHEET 2 F 3 THR C 202 HIS C 207 -1 O ALA C 206 N THR C 159
SHEET 3 F 3 THR C 212 LYS C 217 -1 O VAL C 214 N VAL C 205
SHEET 1 G 3 LEU D 4 THR D 5 0
SHEET 2 G 3 VAL D 19 VAL D 29 -1 O SER D 24 N THR D 5
SHEET 3 G 3 PHE D 61 ILE D 74 -1 O ILE D 74 N VAL D 19
SHEET 1 H 6 ILE D 10 ALA D 13 0
SHEET 2 H 6 THR D 101 ILE D 105 1 O GLU D 104 N MET D 11
SHEET 3 H 6 THR D 84 GLN D 89 -1 N TYR D 85 O THR D 101
SHEET 4 H 6 HIS D 33 GLN D 37 -1 N TYR D 35 O TYR D 86
SHEET 5 H 6 LYS D 44 TYR D 48 -1 O ILE D 47 N TRP D 34
SHEET 6 H 6 LYS D 52 LEU D 53 -1 O LYS D 52 N TYR D 48
SHEET 1 I 4 ILE D 10 ALA D 13 0
SHEET 2 I 4 THR D 101 ILE D 105 1 O GLU D 104 N MET D 11
SHEET 3 I 4 THR D 84 GLN D 89 -1 N TYR D 85 O THR D 101
SHEET 4 I 4 THR D 96 PHE D 97 -1 O THR D 96 N GLN D 89
SHEET 1 J 4 THR D 113 ILE D 116 0
SHEET 2 J 4 GLY D 128 PHE D 138 -1 O PHE D 134 N SER D 115
SHEET 3 J 4 TYR D 172 THR D 181 -1 O LEU D 178 N VAL D 131
SHEET 4 J 4 VAL D 158 TRP D 162 -1 N LEU D 159 O THR D 177
SHEET 1 K 4 SER D 152 ARG D 154 0
SHEET 2 K 4 ILE D 143 ILE D 149 -1 N TRP D 147 O ARG D 154
SHEET 3 K 4 SER D 190 HIS D 197 -1 O THR D 192 N LYS D 148
SHEET 4 K 4 ILE D 204 ASN D 209 -1 O PHE D 208 N TYR D 191
SHEET 1 L 4 ARG E 3 SER E 7 0
SHEET 2 L 4 LEU E 18 SER E 25 -1 O SER E 21 N SER E 7
SHEET 3 L 4 THR E 78 ILE E 83 -1 O LEU E 81 N LEU E 20
SHEET 4 L 4 PHE E 68 ASP E 73 -1 N ILE E 69 O GLN E 82
SHEET 1 M 6 GLY E 10 VAL E 12 0
SHEET 2 M 6 THR E 115 VAL E 119 1 O THR E 118 N GLY E 10
SHEET 3 M 6 ALA E 92 TYR E 101 -1 N TYR E 94 O THR E 115
SHEET 4 M 6 MET E 34 GLN E 39 -1 N VAL E 37 O TYR E 95
SHEET 5 M 6 LYS E 46 ILE E 51 -1 O LYS E 46 N ARG E 38
SHEET 6 M 6 ILE E 58 TYR E 60 -1 O ASN E 59 N GLU E 50
SHEET 1 N 4 GLY E 10 VAL E 12 0
SHEET 2 N 4 THR E 115 VAL E 119 1 O THR E 118 N GLY E 10
SHEET 3 N 4 ALA E 92 TYR E 101 -1 N TYR E 94 O THR E 115
SHEET 4 N 4 TRP E 106 TRP E 111 -1 O TYR E 107 N TYR E 100
SHEET 1 O 4 SER E 128 LEU E 132 0
SHEET 2 O 4 MET E 143 TYR E 153 -1 O LEU E 149 N TYR E 130
SHEET 3 O 4 TYR E 183 PRO E 192 -1 O VAL E 189 N LEU E 146
SHEET 4 O 4 VAL E 171 THR E 173 -1 N HIS E 172 O SER E 188
SHEET 1 P 4 SER E 128 LEU E 132 0
SHEET 2 P 4 MET E 143 TYR E 153 -1 O LEU E 149 N TYR E 130
SHEET 3 P 4 TYR E 183 PRO E 192 -1 O VAL E 189 N LEU E 146
SHEET 4 P 4 VAL E 177 LEU E 178 -1 N VAL E 177 O THR E 184
SHEET 1 Q 3 THR E 159 TRP E 162 0
SHEET 2 Q 3 THR E 202 HIS E 207 -1 O ASN E 204 N THR E 161
SHEET 3 Q 3 THR E 212 LYS E 217 -1 O LYS E 216 N CYS E 203
SHEET 1 R 3 LEU F 4 GLN F 6 0
SHEET 2 R 3 VAL F 19 VAL F 29 -1 O SER F 24 N THR F 5
SHEET 3 R 3 PHE F 61 ILE F 74 -1 O TYR F 70 N CYS F 23
SHEET 1 S 6 ILE F 10 ALA F 13 0
SHEET 2 S 6 THR F 101 ILE F 105 1 O GLU F 104 N MET F 11
SHEET 3 S 6 THR F 84 GLN F 89 -1 N TYR F 85 O THR F 101
SHEET 4 S 6 HIS F 33 GLN F 37 -1 N TYR F 35 O TYR F 86
SHEET 5 S 6 LYS F 44 TYR F 48 -1 O TRP F 46 N TRP F 34
SHEET 6 S 6 LYS F 52 LEU F 53 -1 O LYS F 52 N TYR F 48
SHEET 1 T 4 ILE F 10 ALA F 13 0
SHEET 2 T 4 THR F 101 ILE F 105 1 O GLU F 104 N MET F 11
SHEET 3 T 4 THR F 84 GLN F 89 -1 N TYR F 85 O THR F 101
SHEET 4 T 4 THR F 96 PHE F 97 -1 O THR F 96 N GLN F 89
SHEET 1 U 4 THR F 113 PHE F 117 0
SHEET 2 U 4 GLY F 128 PHE F 138 -1 O VAL F 132 N PHE F 117
SHEET 3 U 4 TYR F 172 THR F 181 -1 O MET F 174 N LEU F 135
SHEET 4 U 4 VAL F 158 TRP F 162 -1 N LEU F 159 O THR F 177
SHEET 1 V 4 SER F 152 ARG F 154 0
SHEET 2 V 4 ILE F 143 ILE F 149 -1 N TRP F 147 O ARG F 154
SHEET 3 V 4 SER F 190 HIS F 197 -1 O GLU F 194 N LYS F 146
SHEET 4 V 4 SER F 200 ASN F 209 -1 O ILE F 204 N ALA F 195
SSBOND 1 CYS C 22 CYS C 96 1555 1555 2.05
SSBOND 2 CYS C 148 CYS C 203 1555 1555 2.04
SSBOND 3 CYS D 23 CYS D 87 1555 1555 2.04
SSBOND 4 CYS D 133 CYS D 193 1555 1555 2.04
SSBOND 5 CYS E 22 CYS E 96 1555 1555 2.07
SSBOND 6 CYS E 148 CYS E 203 1555 1555 2.04
SSBOND 7 CYS F 23 CYS F 87 1555 1555 2.06
SSBOND 8 CYS F 133 CYS F 193 1555 1555 2.04
CISPEP 1 PHE C 154 PRO C 155 0 -7.28
CISPEP 2 GLU C 156 PRO C 157 0 -2.00
CISPEP 3 TRP C 196 PRO C 197 0 -6.30
CISPEP 4 HIS D 93 PRO D 94 0 3.59
CISPEP 5 TYR D 139 PRO D 140 0 0.92
CISPEP 6 PHE E 154 PRO E 155 0 -4.80
CISPEP 7 GLU E 156 PRO E 157 0 -6.52
CISPEP 8 TRP E 196 PRO E 197 0 3.30
CISPEP 9 HIS F 93 PRO F 94 0 -13.81
CISPEP 10 TYR F 139 PRO F 140 0 2.83
SITE 1 AC1 4 SER A 107 ILE A 109 PHE A 357 PHE A 445
SITE 1 AC2 2 SER A 107 PRO A 110
SITE 1 AC3 6 SER B 107 ILE B 109 GLU B 148 GLY B 149
SITE 2 AC3 6 GLY B 355 ILE B 356
SITE 1 AC4 4 SER B 107 GLY B 108 PRO B 110 PHE B 348
CRYST1 232.525 98.860 171.804 90.00 131.54 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 0.004301 0.000000 0.003810 0.00000
SCALE2 0.000000 0.010115 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007776 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
