HEADER TRANSPORT PROTEIN 31-JUL-18 6ADA
TITLE CRYSTAL STRUCTURE OF THE E148D MUTANT CLC-EC1 IN 200MM BROMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H(+)/CL(-) EXCHANGE TRANSPORTER CLCA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CLC-EC1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: SF FILE CONTAINS FRIEDEL PAIRS.;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ANTIBODY FAB FRAGMENT, HEAVY CHAIN;
COMPND 10 CHAIN: C, E;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: ANTIBODY FAB FRAGMENT, LIGHT CHAIN;
COMPND 13 CHAIN: D, F
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: CLCA, ERIC, YADQ, B0155, JW5012;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_TAXID: 10090;
SOURCE 11 CELL_LINE: HYBRIDOMA CELL LINE;
SOURCE 12 MOL_ID: 3;
SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 CELL_LINE: HYBRIDOMA CELL LINE
KEYWDS CLC CL-/H+ ANTIPORTER, INTERMEDIATE STRUCTURE, EXTERNAL GLUTAMATE,
KEYWDS 2 TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-H.LIM,K.PARK
REVDAT 3 22-NOV-23 6ADA 1 REMARK
REVDAT 2 11-SEP-19 6ADA 1 JRNL
REVDAT 1 28-AUG-19 6ADA 0
JRNL AUTH K.PARK,B.C.LEE,H.H.LIM
JRNL TITL MUTATION OF EXTERNAL GLUTAMATE RESIDUE REVEALS A NEW
JRNL TITL 2 INTERMEDIATE TRANSPORT STATE AND ANION BINDING SITE IN A CLC
JRNL TITL 3 CL-/H+ANTIPORTER.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 116 17345 2019
JRNL REFN ESSN 1091-6490
JRNL PMID 31409705
JRNL DOI 10.1073/PNAS.1901822116
REMARK 2
REMARK 2 RESOLUTION. 3.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.070
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 98022
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 4865
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.9705 - 9.7224 0.95 2984 143 0.2367 0.2934
REMARK 3 2 9.7224 - 7.7471 0.99 3161 124 0.1648 0.2203
REMARK 3 3 7.7471 - 6.7766 1.00 3045 195 0.1715 0.2055
REMARK 3 4 6.7766 - 6.1611 1.00 3127 172 0.1900 0.2385
REMARK 3 5 6.1611 - 5.7217 1.00 3156 116 0.1942 0.2446
REMARK 3 6 5.7217 - 5.3858 1.00 3123 182 0.1853 0.2609
REMARK 3 7 5.3858 - 5.1170 1.00 3086 194 0.1787 0.2329
REMARK 3 8 5.1170 - 4.8949 1.00 3071 187 0.1970 0.2231
REMARK 3 9 4.8949 - 4.7070 1.00 3074 183 0.1802 0.2768
REMARK 3 10 4.7070 - 4.5449 1.00 3109 181 0.1963 0.2720
REMARK 3 11 4.5449 - 4.4031 1.00 3076 204 0.2060 0.2593
REMARK 3 12 4.4031 - 4.2775 1.00 3117 204 0.2037 0.2766
REMARK 3 13 4.2775 - 4.1651 1.00 3082 188 0.2209 0.2870
REMARK 3 14 4.1651 - 4.0637 1.00 3168 118 0.2440 0.3027
REMARK 3 15 4.0637 - 3.9714 1.00 3094 164 0.2660 0.3745
REMARK 3 16 3.9714 - 3.8870 1.00 3095 182 0.2656 0.3380
REMARK 3 17 3.8870 - 3.8094 1.00 3145 114 0.2790 0.3204
REMARK 3 18 3.8094 - 3.7376 1.00 3193 140 0.2718 0.2978
REMARK 3 19 3.7376 - 3.6709 1.00 3115 144 0.2791 0.3668
REMARK 3 20 3.6709 - 3.6088 1.00 3105 168 0.2938 0.3583
REMARK 3 21 3.6088 - 3.5506 1.00 3174 123 0.2885 0.3791
REMARK 3 22 3.5506 - 3.4960 1.00 3146 117 0.2942 0.3469
REMARK 3 23 3.4960 - 3.4447 1.00 3117 118 0.2835 0.3983
REMARK 3 24 3.4447 - 3.3962 1.00 3099 209 0.3168 0.3689
REMARK 3 25 3.3962 - 3.3503 0.99 3089 159 0.3266 0.3618
REMARK 3 26 3.3503 - 3.3069 1.00 3157 196 0.3362 0.4408
REMARK 3 27 3.3069 - 3.2656 1.00 3040 181 0.3529 0.4211
REMARK 3 28 3.2656 - 3.2263 1.00 3067 156 0.3642 0.4357
REMARK 3 29 3.2263 - 3.1888 1.00 3166 147 0.3737 0.3811
REMARK 3 30 3.1888 - 3.1530 0.95 2976 156 0.4029 0.4788
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.490
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 87.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 92.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND RESID 30 THROUGH 450)
REMARK 3 SELECTION : (CHAIN B AND RESID 30 THROUGH 450)
REMARK 3 ATOM PAIRS NUMBER : 2550
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6ADA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1300008574.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-18
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9190
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 98122
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.57000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4ENE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400 26%(W/V), 100MM TRIS-SO4, 200MM
REMARK 280 NABR, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 116.20450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.97800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 116.20450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.97800
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 465 GLU E 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NE2 GLN D 6 O TYR D 85 2.07
REMARK 500 O ALA D 25 OG1 THR D 68 2.14
REMARK 500 NZ LYS D 18 OD1 ASN D 75 2.17
REMARK 500 O GLU F 186 NH2 ARG F 210 2.18
REMARK 500 O VAL D 29 OH TYR D 70 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 423 CB - CG - CD2 ANGL. DEV. = -15.7 DEGREES
REMARK 500 LEU B 139 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 LEU C 185 CB - CG - CD2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 CYS E 148 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 CYS F 23 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 29 85.41 41.36
REMARK 500 LYS A 30 53.98 -143.04
REMARK 500 ALA A 101 91.71 -164.28
REMARK 500 ARG A 167 57.04 37.93
REMARK 500 ASN A 233 -4.72 -150.19
REMARK 500 HIS A 234 170.53 -59.90
REMARK 500 GLU A 235 -12.53 72.09
REMARK 500 ALA A 309 68.53 -170.64
REMARK 500 ALA A 404 72.78 -118.55
REMARK 500 ASN A 418 62.43 -112.87
REMARK 500 ALA A 450 -74.11 -55.78
REMARK 500 GLN A 456 34.29 -73.24
REMARK 500 GLU A 457 -36.96 -161.54
REMARK 500 ASP B 29 70.23 39.70
REMARK 500 LEU B 96 -18.70 -49.22
REMARK 500 ALA B 101 89.05 -162.18
REMARK 500 VAL B 144 76.17 -68.94
REMARK 500 ARG B 167 54.07 39.31
REMARK 500 ASN B 233 -6.31 -150.13
REMARK 500 GLU B 235 -9.56 70.98
REMARK 500 ALA B 309 67.68 -176.14
REMARK 500 ASN B 418 60.47 -112.04
REMARK 500 GLN B 456 31.24 -88.74
REMARK 500 GLU B 457 27.90 -167.25
REMARK 500 SER C 25 111.18 -160.93
REMARK 500 ARG C 31 -9.16 67.40
REMARK 500 ILE C 48 -72.26 -79.22
REMARK 500 SER C 55 19.81 59.98
REMARK 500 PRO C 62 82.71 -57.48
REMARK 500 LEU C 64 -175.61 51.32
REMARK 500 LYS C 65 -86.31 -87.48
REMARK 500 LYS C 85 66.71 39.11
REMARK 500 ALA C 137 46.78 -99.79
REMARK 500 ALA C 140 93.22 -48.42
REMARK 500 PRO C 155 -153.46 -94.32
REMARK 500 LEU C 167 36.68 -86.73
REMARK 500 PRO C 197 30.74 -90.32
REMARK 500 SER C 210 15.71 -141.71
REMARK 500 SER D 7 -72.05 -89.53
REMARK 500 ALA D 13 144.04 -173.97
REMARK 500 TYR D 31 100.38 46.97
REMARK 500 SER D 39 107.61 -48.73
REMARK 500 THR D 50 -35.17 53.77
REMARK 500 SER D 69 114.28 -175.63
REMARK 500 SER D 71 147.14 -172.14
REMARK 500 THR D 76 113.99 59.50
REMARK 500 GLU D 80 0.69 -63.09
REMARK 500 ALA D 83 -170.19 -171.81
REMARK 500 ASN D 137 73.37 62.99
REMARK 500 PRO D 140 -164.16 -75.80
REMARK 500
REMARK 500 THIS ENTRY HAS 74 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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 502
DBREF 6ADA A 1 473 UNP P37019 CLCA_ECOLI 1 473
DBREF 6ADA B 1 473 UNP P37019 CLCA_ECOLI 1 473
DBREF 6ADA C 1 222 PDB 6ADA 6ADA 1 222
DBREF 6ADA D 1 211 PDB 6ADA 6ADA 1 211
DBREF 6ADA E 1 222 PDB 6ADA 6ADA 1 222
DBREF 6ADA F 1 211 PDB 6ADA 6ADA 1 211
SEQADV 6ADA ASP A 148 UNP P37019 GLU 148 ENGINEERED MUTATION
SEQADV 6ADA ASP B 148 UNP P37019 GLU 148 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 ASP 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 TYR 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 ASP 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 TYR 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 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 BR A 501 1
HET BR A 502 1
HET BR B 501 1
HET BR B 502 1
HETNAM BR BROMIDE ION
FORMUL 7 BR 4(BR 1-)
HELIX 1 AA1 ARG A 17 GLU A 27 1 11
HELIX 2 AA2 PRO A 32 THR A 71 1 40
HELIX 3 AA3 ASN A 74 ALA A 101 1 28
HELIX 4 AA4 PRO A 102 GLY A 105 5 4
HELIX 5 AA5 GLY A 108 ASP A 118 1 11
HELIX 6 AA6 ARG A 123 GLY A 141 1 19
HELIX 7 AA7 ARG A 147 ARG A 167 1 21
HELIX 8 AA8 GLY A 170 PHE A 190 1 21
HELIX 9 AA9 ALA A 192 GLU A 203 1 12
HELIX 10 AB1 SER A 214 PHE A 232 1 19
HELIX 11 AB2 PRO A 248 ASN A 250 5 3
HELIX 12 AB3 THR A 251 GLY A 285 1 35
HELIX 13 AB4 ASN A 287 ALA A 309 1 23
HELIX 14 AB5 PRO A 310 SER A 313 5 4
HELIX 15 AB6 ASN A 318 ALA A 325 1 8
HELIX 16 AB7 SER A 329 SER A 350 1 22
HELIX 17 AB8 ILE A 356 PHE A 379 1 24
HELIX 18 AB9 PRO A 380 HIS A 383 5 4
HELIX 19 AC1 GLU A 385 GLY A 395 1 11
HELIX 20 AC2 GLY A 395 ARG A 403 1 9
HELIX 21 AC3 ALA A 404 ASP A 417 1 14
HELIX 22 AC4 ASN A 418 GLN A 420 5 3
HELIX 23 AC5 LEU A 421 THR A 439 1 19
HELIX 24 AC6 PRO A 443 GLU A 459 1 17
HELIX 25 AC7 ARG B 18 LEU B 26 1 9
HELIX 26 AC8 PRO B 32 LEU B 68 1 37
HELIX 27 AC9 ASN B 74 ALA B 101 1 28
HELIX 28 AD1 PRO B 102 GLY B 105 5 4
HELIX 29 AD2 GLY B 108 GLU B 117 1 10
HELIX 30 AD3 ARG B 123 GLY B 141 1 19
HELIX 31 AD4 ARG B 147 ARG B 167 1 21
HELIX 32 AD5 GLY B 170 ASN B 191 1 22
HELIX 33 AD6 ALA B 192 GLU B 203 1 12
HELIX 34 AD7 SER B 214 PHE B 232 1 19
HELIX 35 AD8 PRO B 248 ASN B 250 5 3
HELIX 36 AD9 THR B 251 GLY B 285 1 35
HELIX 37 AE1 ASN B 287 ALA B 309 1 23
HELIX 38 AE2 PRO B 310 SER B 313 5 4
HELIX 39 AE3 ASN B 318 ALA B 325 1 8
HELIX 40 AE4 SER B 329 SER B 349 1 21
HELIX 41 AE5 ILE B 356 PHE B 379 1 24
HELIX 42 AE6 PRO B 380 HIS B 383 5 4
HELIX 43 AE7 GLU B 385 GLY B 395 1 11
HELIX 44 AE8 GLY B 395 SER B 401 1 7
HELIX 45 AE9 ALA B 404 ASP B 417 1 14
HELIX 46 AF1 ASN B 418 GLN B 420 5 3
HELIX 47 AF2 LEU B 421 PHE B 438 1 18
HELIX 48 AF3 PRO B 443 LYS B 455 1 13
HELIX 49 AF4 ARG C 87 THR C 91 5 5
HELIX 50 AF5 SER C 164 SER C 166 5 3
HELIX 51 AF6 SER C 194 TRP C 196 5 3
HELIX 52 AF7 PRO C 208 SER C 211 5 4
HELIX 53 AF8 SER D 120 GLY D 127 1 8
HELIX 54 AF9 LYS D 182 ARG D 187 1 6
HELIX 55 AG1 ASN E 74 LYS E 76 5 3
HELIX 56 AG2 ARG E 87 THR E 91 5 5
HELIX 57 AG3 SER E 194 TRP E 196 5 3
HELIX 58 AG4 PRO E 208 SER E 211 5 4
HELIX 59 AG5 GLU F 78 ALA F 82 5 5
HELIX 60 AG6 SER F 120 THR F 125 1 6
HELIX 61 AG7 LYS F 182 ARG F 187 1 6
SHEET 1 AA1 4 ARG C 3 SER C 7 0
SHEET 2 AA1 4 SER C 17 SER C 25 -1 O ALA C 23 N LEU C 5
SHEET 3 AA1 4 THR C 78 SER C 84 -1 O LEU C 79 N CYS C 22
SHEET 4 AA1 4 PHE C 68 ASP C 73 -1 N SER C 71 O TYR C 80
SHEET 1 AA2 6 LEU C 11 VAL C 12 0
SHEET 2 AA2 6 THR C 115 VAL C 119 1 O THR C 118 N VAL C 12
SHEET 3 AA2 6 ALA C 92 TYR C 100 -1 N TYR C 94 O THR C 115
SHEET 4 AA2 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 95
SHEET 5 AA2 6 LEU C 45 ILE C 51 -1 O LYS C 46 N ARG C 38
SHEET 6 AA2 6 ILE C 58 TYR C 60 -1 O ASN C 59 N GLU C 50
SHEET 1 AA3 4 LEU C 11 VAL C 12 0
SHEET 2 AA3 4 THR C 115 VAL C 119 1 O THR C 118 N VAL C 12
SHEET 3 AA3 4 ALA C 92 TYR C 100 -1 N TYR C 94 O THR C 115
SHEET 4 AA3 4 TYR C 107 TRP C 111 -1 O TYR C 107 N TYR C 100
SHEET 1 AA4 4 SER C 128 LEU C 132 0
SHEET 2 AA4 4 MET C 143 TYR C 153 -1 O LEU C 149 N TYR C 130
SHEET 3 AA4 4 LEU C 182 PRO C 192 -1 O LEU C 185 N VAL C 150
SHEET 4 AA4 4 HIS C 172 THR C 173 -1 N HIS C 172 O SER C 188
SHEET 1 AA5 4 SER C 128 LEU C 132 0
SHEET 2 AA5 4 MET C 143 TYR C 153 -1 O LEU C 149 N TYR C 130
SHEET 3 AA5 4 LEU C 182 PRO C 192 -1 O LEU C 185 N VAL C 150
SHEET 4 AA5 4 VAL C 177 GLN C 179 -1 N GLN C 179 O LEU C 182
SHEET 1 AA6 3 THR C 159 TRP C 162 0
SHEET 2 AA6 3 THR C 202 HIS C 207 -1 O ASN C 204 N THR C 161
SHEET 3 AA6 3 THR C 212 LYS C 217 -1 O LYS C 216 N CYS C 203
SHEET 1 AA7 2 ILE D 10 ALA D 13 0
SHEET 2 AA7 2 LYS D 102 ILE D 105 1 O GLU D 104 N MET D 11
SHEET 1 AA8 3 VAL D 19 CYS D 23 0
SHEET 2 AA8 3 SER D 69 ILE D 74 -1 O ILE D 74 N VAL D 19
SHEET 3 AA8 3 PHE D 61 SER D 66 -1 N SER D 66 O SER D 69
SHEET 1 AA9 4 LYS D 44 ILE D 47 0
SHEET 2 AA9 4 HIS D 33 GLN D 37 -1 N TRP D 34 O ILE D 47
SHEET 3 AA9 4 THR D 84 GLN D 89 -1 O TYR D 86 N TYR D 35
SHEET 4 AA9 4 THR D 96 PHE D 97 -1 O THR D 96 N GLN D 89
SHEET 1 AB1 4 THR D 113 PHE D 117 0
SHEET 2 AB1 4 GLY D 128 PHE D 138 -1 O PHE D 134 N SER D 115
SHEET 3 AB1 4 TYR D 172 THR D 181 -1 O LEU D 180 N ALA D 129
SHEET 4 AB1 4 VAL D 158 TRP D 162 -1 N LEU D 159 O THR D 177
SHEET 1 AB2 4 SER D 152 ARG D 154 0
SHEET 2 AB2 4 ASN D 144 ILE D 149 -1 N ILE D 149 O SER D 152
SHEET 3 AB2 4 SER D 190 THR D 196 -1 O THR D 192 N LYS D 148
SHEET 4 AB2 4 ILE D 204 ASN D 209 -1 O LYS D 206 N CYS D 193
SHEET 1 AB3 4 ARG E 3 SER E 7 0
SHEET 2 AB3 4 LEU E 18 SER E 25 -1 O ALA E 23 N LEU E 5
SHEET 3 AB3 4 THR E 78 ILE E 83 -1 O LEU E 81 N LEU E 20
SHEET 4 AB3 4 PHE E 68 ASP E 73 -1 N SER E 71 O TYR E 80
SHEET 1 AB4 2 LEU E 11 VAL E 12 0
SHEET 2 AB4 2 THR E 118 VAL E 119 1 O THR E 118 N VAL E 12
SHEET 1 AB5 5 ILE E 58 TYR E 60 0
SHEET 2 AB5 5 LEU E 45 ILE E 51 -1 N GLU E 50 O ASN E 59
SHEET 3 AB5 5 MET E 34 GLN E 39 -1 N TRP E 36 O ILE E 48
SHEET 4 AB5 5 LEU E 93 TYR E 101 -1 O TYR E 95 N VAL E 37
SHEET 5 AB5 5 TRP E 106 TRP E 111 -1 O TYR E 107 N TYR E 100
SHEET 1 AB6 5 ILE E 58 TYR E 60 0
SHEET 2 AB6 5 LEU E 45 ILE E 51 -1 N GLU E 50 O ASN E 59
SHEET 3 AB6 5 MET E 34 GLN E 39 -1 N TRP E 36 O ILE E 48
SHEET 4 AB6 5 LEU E 93 TYR E 101 -1 O TYR E 95 N VAL E 37
SHEET 5 AB6 5 THR E 115 THR E 116 -1 O THR E 115 N TYR E 94
SHEET 1 AB7 4 SER E 128 LEU E 132 0
SHEET 2 AB7 4 MET E 143 TYR E 153 -1 O LEU E 149 N TYR E 130
SHEET 3 AB7 4 TYR E 183 PRO E 192 -1 O VAL E 191 N VAL E 144
SHEET 4 AB7 4 VAL E 171 THR E 173 -1 N HIS E 172 O SER E 188
SHEET 1 AB8 4 SER E 128 LEU E 132 0
SHEET 2 AB8 4 MET E 143 TYR E 153 -1 O LEU E 149 N TYR E 130
SHEET 3 AB8 4 TYR E 183 PRO E 192 -1 O VAL E 191 N VAL E 144
SHEET 4 AB8 4 VAL E 177 LEU E 178 -1 N VAL E 177 O THR E 184
SHEET 1 AB9 3 THR E 159 TRP E 162 0
SHEET 2 AB9 3 THR E 202 HIS E 207 -1 O ASN E 204 N THR E 161
SHEET 3 AB9 3 THR E 212 LYS E 217 -1 O THR E 212 N HIS E 207
SHEET 1 AC1 4 LEU F 4 GLN F 6 0
SHEET 2 AC1 4 LYS F 18 ALA F 25 -1 O SER F 24 N THR F 5
SHEET 3 AC1 4 SER F 69 ASN F 75 -1 O TYR F 70 N CYS F 23
SHEET 4 AC1 4 PHE F 61 SER F 66 -1 N SER F 62 O THR F 73
SHEET 1 AC2 6 ILE F 10 ALA F 13 0
SHEET 2 AC2 6 THR F 101 ILE F 105 1 O GLU F 104 N MET F 11
SHEET 3 AC2 6 THR F 84 GLN F 89 -1 N TYR F 85 O THR F 101
SHEET 4 AC2 6 HIS F 33 GLN F 37 -1 N TYR F 35 O TYR F 86
SHEET 5 AC2 6 LYS F 44 TYR F 48 -1 O ILE F 47 N TRP F 34
SHEET 6 AC2 6 LYS F 52 LEU F 53 -1 O LYS F 52 N TYR F 48
SHEET 1 AC3 4 ILE F 10 ALA F 13 0
SHEET 2 AC3 4 THR F 101 ILE F 105 1 O GLU F 104 N MET F 11
SHEET 3 AC3 4 THR F 84 GLN F 89 -1 N TYR F 85 O THR F 101
SHEET 4 AC3 4 THR F 96 PHE F 97 -1 O THR F 96 N GLN F 89
SHEET 1 AC4 4 THR F 113 PHE F 117 0
SHEET 2 AC4 4 GLY F 128 PHE F 138 -1 O PHE F 134 N SER F 115
SHEET 3 AC4 4 TYR F 172 THR F 181 -1 O LEU F 180 N ALA F 129
SHEET 4 AC4 4 VAL F 158 TRP F 162 -1 N LEU F 159 O THR F 177
SHEET 1 AC5 4 SER F 152 ARG F 154 0
SHEET 2 AC5 4 ASN F 144 ILE F 149 -1 N TRP F 147 O ARG F 154
SHEET 3 AC5 4 SER F 190 HIS F 197 -1 O GLU F 194 N LYS F 146
SHEET 4 AC5 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 2.03
SSBOND 2 CYS C 148 CYS C 203 1555 1555 2.06
SSBOND 3 CYS D 23 CYS D 87 1555 1555 2.07
SSBOND 4 CYS D 133 CYS D 193 1555 1555 2.05
SSBOND 5 CYS E 22 CYS E 96 1555 1555 2.09
SSBOND 6 CYS E 148 CYS E 203 1555 1555 2.06
SSBOND 7 CYS F 23 CYS F 87 1555 1555 2.10
SSBOND 8 CYS F 133 CYS F 193 1555 1555 2.05
CISPEP 1 PHE C 154 PRO C 155 0 -6.74
CISPEP 2 GLU C 156 PRO C 157 0 -0.22
CISPEP 3 TRP C 196 PRO C 197 0 4.52
CISPEP 4 HIS D 93 PRO D 94 0 1.15
CISPEP 5 TYR D 139 PRO D 140 0 -3.42
CISPEP 6 PHE E 154 PRO E 155 0 0.00
CISPEP 7 GLU E 156 PRO E 157 0 0.14
CISPEP 8 TRP E 196 PRO E 197 0 6.44
CISPEP 9 HIS F 93 PRO F 94 0 -15.53
CISPEP 10 TYR F 139 PRO F 140 0 -0.47
SITE 1 AC1 1 ARG A 147
SITE 1 AC2 1 SER A 107
SITE 1 AC3 1 ARG B 147
SITE 1 AC4 2 SER B 107 PHE B 348
CRYST1 232.409 99.956 170.811 90.00 131.88 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 0.004303 0.000000 0.003858 0.00000
SCALE2 0.000000 0.010004 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007863 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
