HEADER TRANSPORT PROTEIN 19-FEB-20 6VW9
TITLE C-TERMINAL REGULATORY DOMAIN OF THE CHLORIDE TRANSPORTER KCC-1 FROM C.
TITLE 2 ELEGANS, PROTEOLYZED DURING CRYSTALLIZATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: K+/CL-COTRANSPORTER;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL REGULATORY DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: K+/CL-COTRANSPORTER;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: C-TERMINAL REGULATORY DOMAIN;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;
SOURCE 3 ORGANISM_TAXID: 6239;
SOURCE 4 GENE: KCC-1, CELE_R13A1.2, R13A1.2;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;
SOURCE 9 ORGANISM_TAXID: 6239;
SOURCE 10 GENE: KCC-1, CELE_R13A1.2, R13A1.2;
SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS CATION-CHLORIDE-COTRANSPORTER, SLC TRANSPORTER, CYTOSOLIC DOMAIN,
KEYWDS 2 TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.ZIMANYI,J.CHEUNG
REVDAT 4 06-MAR-24 6VW9 1 REMARK
REVDAT 3 09-SEP-20 6VW9 1 JRNL
REVDAT 2 29-JUL-20 6VW9 1 JRNL
REVDAT 1 15-JUL-20 6VW9 0
JRNL AUTH C.M.ZIMANYI,M.GUO,A.MAHMOOD,W.A.HENDRICKSON,D.HIRSH,J.CHEUNG
JRNL TITL STRUCTURE OF THE REGULATORY CYTOSOLIC DOMAIN OF A EUKARYOTIC
JRNL TITL 2 POTASSIUM-CHLORIDE COTRANSPORTER.
JRNL REF STRUCTURE V. 28 1051 2020
JRNL REFN ISSN 0969-2126
JRNL PMID 32679039
JRNL DOI 10.1016/J.STR.2020.06.009
REMARK 2
REMARK 2 RESOLUTION. 1.80 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 : GEOSTD + MONOMER LIBRARY
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 34612
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 1717
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 40.7900 - 4.1100 0.99 2814 161 0.1465 0.1792
REMARK 3 2 4.1100 - 3.2600 0.98 2761 147 0.1727 0.2007
REMARK 3 3 3.2600 - 2.8500 0.99 2812 148 0.2021 0.2437
REMARK 3 4 2.8500 - 2.5900 0.97 2728 139 0.2154 0.2424
REMARK 3 5 2.5900 - 2.4000 0.99 2783 131 0.1975 0.2198
REMARK 3 6 2.4000 - 2.2600 0.99 2762 129 0.1970 0.2295
REMARK 3 7 2.2600 - 2.1500 0.99 2785 169 0.2113 0.2525
REMARK 3 8 2.1500 - 2.0600 0.98 2743 129 0.2365 0.2859
REMARK 3 9 2.0600 - 1.9800 0.98 2745 142 0.2517 0.2990
REMARK 3 10 1.9800 - 1.9100 0.99 2751 155 0.2766 0.3109
REMARK 3 11 1.9100 - 1.8500 0.99 2776 143 0.3272 0.3219
REMARK 3 12 1.8500 - 1.8000 0.88 2435 124 0.3468 0.3643
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.221
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.62
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 : 0.010 2505
REMARK 3 ANGLE : 1.114 3376
REMARK 3 CHIRALITY : 0.267 387
REMARK 3 PLANARITY : 0.006 422
REMARK 3 DIHEDRAL : 13.829 953
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 660 THROUGH 819 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.8431 39.6016 14.5856
REMARK 3 T TENSOR
REMARK 3 T11: 0.3402 T22: 0.3214
REMARK 3 T33: 0.2724 T12: -0.0110
REMARK 3 T13: -0.0036 T23: -0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 4.7265 L22: 0.9585
REMARK 3 L33: 5.3913 L12: -0.7530
REMARK 3 L13: 1.4935 L23: -1.3829
REMARK 3 S TENSOR
REMARK 3 S11: -0.0972 S12: -0.1410 S13: 0.0313
REMARK 3 S21: 0.0629 S22: -0.0746 S23: -0.0954
REMARK 3 S31: 0.0536 S32: 0.1515 S33: 0.1616
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 820 THROUGH 879 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4369 48.7775 8.7975
REMARK 3 T TENSOR
REMARK 3 T11: 0.5258 T22: 0.6872
REMARK 3 T33: 0.5782 T12: 0.2204
REMARK 3 T13: 0.0031 T23: 0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 8.8660 L22: 4.6748
REMARK 3 L33: 5.3513 L12: -0.6464
REMARK 3 L13: -0.8834 L23: 1.0134
REMARK 3 S TENSOR
REMARK 3 S11: -0.1559 S12: -0.2005 S13: 0.0519
REMARK 3 S21: 0.2803 S22: 0.0509 S23: 0.9834
REMARK 3 S31: -0.1225 S32: -1.1887 S33: 0.0110
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 880 THROUGH 892) OR CHAIN 'B'
REMARK 3 AND (RESID 996 THROUGH 1063)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.1878 35.3679 9.8283
REMARK 3 T TENSOR
REMARK 3 T11: 0.2726 T22: 0.5631
REMARK 3 T33: 0.3685 T12: 0.0186
REMARK 3 T13: -0.0145 T23: -0.0648
REMARK 3 L TENSOR
REMARK 3 L11: 5.0307 L22: 7.0156
REMARK 3 L33: 4.6451 L12: 1.2502
REMARK 3 L13: 0.3799 L23: 0.7950
REMARK 3 S TENSOR
REMARK 3 S11: 0.0855 S12: -0.1058 S13: -0.1024
REMARK 3 S21: 0.2819 S22: -0.0352 S23: 0.4218
REMARK 3 S31: 0.2644 S32: -0.6283 S33: -0.1185
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6VW9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-20.
REMARK 100 THE DEPOSITION ID IS D_1000246796.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-17
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 : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97910
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34639
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.796
REMARK 200 RESOLUTION RANGE LOW (A) : 40.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 9.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.730
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 5% W/V PEG 8000,
REMARK 280 20% W/V PEG 300, 10% GLYCEROL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 52.16000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.77300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 52.16000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.77300
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 97.26124
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 56.08051
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 ASP A 782
REMARK 465 MET A 783
REMARK 465 GLU B 1064
REMARK 465 SER B 1065
REMARK 465 SER B 1066
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 HIS A 830 -79.68 -104.87
REMARK 500 ASP A 831 -139.34 50.59
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 P33 A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1104
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PROTEIN WAS INTERNALLY PROTEOLYZED DURING CRYSTALLIZATION, AS
REMARK 999 DEMONSTRATED BY GEL ELECTROPHORESIS. IT IS UNCERTAIN HOW MUCH WAS
REMARK 999 CLEAVED. IT IS ASSUMED THAT THE RESIDUES MISSING FROM THE ELECTRON
REMARK 999 DENSITY REPRESENT THE RESIDUES THAT WERE REMOVED PROTEOLYTICALLY
DBREF 6VW9 A 661 892 UNP S6FCX2 S6FCX2_CAEEL 661 892
DBREF 6VW9 B 996 1066 UNP S6FCX2 S6FCX2_CAEEL 996 1066
SEQADV 6VW9 SER A 660 UNP S6FCX2 EXPRESSION TAG
SEQRES 1 A 233 SER ASN TRP ARG PRO GLN LEU LEU LEU LEU LEU SER MET
SEQRES 2 A 233 GLN TRP SER LYS GLU ILE ILE ASP VAL ARG TYR LEU ASN
SEQRES 3 A 233 LEU LEU ASN LEU ALA SER GLN LEU LYS ALA GLY LYS GLY
SEQRES 4 A 233 LEU THR VAL VAL THR ALA PHE LEU GLN GLY ASP PRO THR
SEQRES 5 A 233 SER PRO ASP ASP LYS LYS LYS GLY GLU GLN VAL LYS ALA
SEQRES 6 A 233 ARG MET ASP PHE ASP MET ASN GLN VAL ARG LEU ARG GLY
SEQRES 7 A 233 PHE ALA LYS THR LEU VAL HIS SER GLU ASP GLN VAL ARG
SEQRES 8 A 233 GLY SER MET SER THR LEU VAL GLN SER VAL GLY LEU GLY
SEQRES 9 A 233 GLY LEU LYS PRO ASN THR MET LEU ILE SER TRP PRO VAL
SEQRES 10 A 233 HIS GLU ARG GLU GLU ASP MET THR GLU TYR ASN THR PHE
SEQRES 11 A 233 ILE GLU LYS VAL HIS ALA ALA SER ILE ASN ASP MET ALA
SEQRES 12 A 233 ILE VAL VAL ALA LYS GLY ILE ILE ASP PHE PRO SER ALA
SEQRES 13 A 233 VAL PHE ARG MET SER GLY MET ILE ASP VAL TYR TRP ILE
SEQRES 14 A 233 VAL HIS ASP GLY GLY LEU CYS LEU LEU MET GLY TYR LEU
SEQRES 15 A 233 LEU LYS GLN HIS LYS VAL TRP ARG GLY CYS LYS LEU ARG
SEQRES 16 A 233 VAL ILE GLY ILE ALA GLN GLU SER ASP ASN ASN VAL LYS
SEQRES 17 A 233 MET GLN GLU ASP LEU GLN LYS TYR VAL TYR GLN LEU ARG
SEQRES 18 A 233 ILE ASP ALA LYS ILE MET ILE VAL GLU LEU ALA ASP
SEQRES 1 B 71 SER LYS MET HIS THR ALA VAL ARG LEU ASN GLU LEU LEU
SEQRES 2 B 71 LEU GLN HIS SER ALA ASN SER GLN LEU ILE LEU LEU ASN
SEQRES 3 B 71 LEU PRO LYS PRO PRO VAL HIS LYS ASP GLN GLN ALA LEU
SEQRES 4 B 71 ASP ASP TYR VAL HIS TYR LEU GLU VAL MET THR ASP LYS
SEQRES 5 B 71 LEU ASN ARG VAL ILE PHE VAL ARG GLY THR GLY LYS GLU
SEQRES 6 B 71 VAL ILE THR GLU SER SER
HET P33 A1101 22
HET GOL A1102 6
HET GOL A1103 6
HET GOL A1104 6
HETNAM P33 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL
HETNAM GOL GLYCEROL
HETSYN P33 HEPTAETHYLENE GLYCOL; PEG330
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 P33 C14 H30 O8
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 7 HOH *67(H2 O)
HELIX 1 AA1 ASP A 680 ALA A 695 1 16
HELIX 2 AA2 SER A 712 VAL A 733 1 22
HELIX 3 AA3 SER A 745 ASP A 747 5 3
HELIX 4 AA4 GLN A 748 VAL A 760 1 13
HELIX 5 AA5 GLU A 785 ASN A 799 1 15
HELIX 6 AA6 GLY A 808 PHE A 812 5 5
HELIX 7 AA7 GLY A 833 HIS A 845 1 13
HELIX 8 AA8 ASN A 864 ARG A 880 1 17
HELIX 9 AA9 LYS B 997 ALA B 1013 1 17
HELIX 10 AB1 ASP B 1030 THR B 1045 1 16
SHEET 1 AA110 GLY A 737 HIS A 744 0
SHEET 2 AA110 THR A 700 GLN A 707 1 N VAL A 702 O PHE A 738
SHEET 3 AA110 LEU A 666 LEU A 670 1 N LEU A 668 O VAL A 701
SHEET 4 AA110 THR A 769 SER A 773 1 O LEU A 771 N LEU A 667
SHEET 5 AA110 ALA A 802 LYS A 807 1 O ALA A 802 N MET A 770
SHEET 6 AA110 VAL B1051 ARG B1055 -1 O VAL B1051 N LYS A 807
SHEET 7 AA110 LEU B1017 ASN B1021 1 N ILE B1018 O ILE B1052
SHEET 8 AA110 SER A 820 TRP A 827 1 N ASP A 824 O LEU B1019
SHEET 9 AA110 GLY A 850 ALA A 859 1 O ILE A 856 N VAL A 825
SHEET 10 AA110 LYS A 884 GLU A 889 1 O LYS A 884 N VAL A 855
SITE 1 AC1 7 LYS A 676 GLN A 721 ALA A 724 ARG A 725
SITE 2 AC1 7 PHE A 728 VAL A 816 HOH A1211
SITE 1 AC2 2 ASP A 811 ARG B1050
SITE 1 AC3 2 HIS A 777 GLU A 780
SITE 1 AC4 3 THR A 784 GLU A 785 THR A 788
CRYST1 104.320 65.546 56.523 90.00 97.17 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009586 0.000000 0.001207 0.00000
SCALE2 0.000000 0.015256 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017832 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
