HEADER TRANSPORT PROTEIN 09-JUN-18 6GR7
TITLE CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH 2,4,5-
TITLE 2 TRICHLOROPHENOXYACETIC ACID (2,4,5-T)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSTHYRETIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ATTR,PREALBUMIN,TBPA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TTR, PALB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSTHYRETIN, TRANSPORT PROTEIN, THYROXINE DISRUPTING CHEMICALS,
KEYWDS 2 TDCS, 2, 4, 5-TRICHLOROPHENOXYACETIC ACID, 5-T
EXPDTA X-RAY DIFFRACTION
AUTHOR C.GRUNDSTROM,J.ZHANG,A.OLOFSSON,P.L.ANDERSSON,A.E.SAUER-ERIKSSON
REVDAT 5 17-JAN-24 6GR7 1 JRNL
REVDAT 4 24-APR-19 6GR7 1 JRNL
REVDAT 3 26-SEP-18 6GR7 1 JRNL
REVDAT 2 25-JUL-18 6GR7 1 JRNL
REVDAT 1 11-JUL-18 6GR7 0
JRNL AUTH J.ZHANG,C.GRUNDSTROM,K.BRANNSTROM,I.IAKOVLEVA,M.LINDBERG,
JRNL AUTH 2 A.OLOFSSON,P.L.ANDERSSON,A.E.SAUER-ERIKSSON
JRNL TITL INTERSPECIES VARIATION BETWEEN FISH AND HUMAN TRANSTHYRETINS
JRNL TITL 2 IN THEIR BINDING OF THYROID-DISRUPTING CHEMICALS.
JRNL REF ENVIRON. SCI. TECHNOL. V. 52 11865 2018
JRNL REFN ESSN 1520-5851
JRNL PMID 30226982
JRNL DOI 10.1021/ACS.EST.8B03581
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.ZHANG,A.BEGUM,K.BRANNSTROM,C.GRUNDSTROM,I.IAKOVLEVA,
REMARK 1 AUTH 2 A.OLOFSSON,A.E.SAUER-ERIKSSON,P.L.ANDERSSON
REMARK 1 TITL STRUCTURE-BASED VIRTUAL SCREENING PROTOCOL FOR IN SILICO
REMARK 1 TITL 2 IDENTIFICATION OF POTENTIAL THYROID DISRUPTING CHEMICALS
REMARK 1 TITL 3 TARGETING TRANSTHYRETIN.
REMARK 1 REF ENVIRON. SCI. TECHNOL. V. 50 11984 2016
REMARK 1 REFN ESSN 1520-5851
REMARK 1 PMID 27668830
REMARK 1 DOI 10.1021/ACS.EST.6B02771
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 46647
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.780
REMARK 3 FREE R VALUE TEST SET COUNT : 2231
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 42.7629 - 3.5272 0.99 3016 154 0.1591 0.1756
REMARK 3 2 3.5272 - 2.7998 1.00 2900 149 0.1640 0.1653
REMARK 3 3 2.7998 - 2.4459 0.98 2819 129 0.1593 0.1749
REMARK 3 4 2.4459 - 2.2223 0.94 2679 128 0.1551 0.1730
REMARK 3 5 2.2223 - 2.0630 1.00 2808 141 0.1550 0.1881
REMARK 3 6 2.0630 - 1.9414 1.00 2831 120 0.1562 0.1978
REMARK 3 7 1.9414 - 1.8442 1.00 2828 134 0.1669 0.1786
REMARK 3 8 1.8442 - 1.7639 1.00 2793 155 0.1825 0.1976
REMARK 3 9 1.7639 - 1.6960 0.99 2758 140 0.1820 0.2236
REMARK 3 10 1.6960 - 1.6375 0.99 2796 138 0.1860 0.2142
REMARK 3 11 1.6375 - 1.5863 0.99 2752 141 0.1906 0.2193
REMARK 3 12 1.5863 - 1.5409 0.99 2750 154 0.2038 0.2249
REMARK 3 13 1.5409 - 1.5003 0.99 2768 132 0.2117 0.2528
REMARK 3 14 1.5003 - 1.4637 0.99 2744 147 0.2239 0.2201
REMARK 3 15 1.4637 - 1.4305 0.97 2674 125 0.2502 0.3244
REMARK 3 16 1.4305 - 1.4000 0.90 2500 144 0.2690 0.3086
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.009 2092
REMARK 3 ANGLE : 0.914 2884
REMARK 3 CHIRALITY : 0.084 313
REMARK 3 PLANARITY : 0.009 386
REMARK 3 DIHEDRAL : 14.981 757
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6GR7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1200010436.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.968
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46647
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 42.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 13.30
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.9
REMARK 200 DATA REDUNDANCY IN SHELL : 10.80
REMARK 200 R MERGE FOR SHELL (I) : 1.07000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 1F41
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PURIFIED HUMAN TTR WAS DIALYZED
REMARK 280 AGAINST 10 MM NA-PHOSPHATE BUFFER WITH 100 MM KCL (PH 7.6) AND
REMARK 280 CONCENTRATED TO 5 MG/ML THE RESERVOIR CONTAINED 28% PEG 4K, 0.1M
REMARK 280 NAAC PH 4.5, 0.2M AMAC. DROP SIZE 3 PLUS 3 MICROLITER., VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 21.43900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.74300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.43900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.74300
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: 6710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 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 85.75600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 421 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 400 LIES ON A SPECIAL POSITION.
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 GLY A 1
REMARK 465 PRO A 2
REMARK 465 THR A 3
REMARK 465 GLY A 4
REMARK 465 THR A 5
REMARK 465 GLY A 6
REMARK 465 GLU A 7
REMARK 465 SER A 8
REMARK 465 LYS A 9
REMARK 465 LYS A 126
REMARK 465 GLU A 127
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 THR B 3
REMARK 465 GLY B 4
REMARK 465 THR B 5
REMARK 465 GLY B 6
REMARK 465 GLU B 7
REMARK 465 SER B 8
REMARK 465 LYS B 9
REMARK 465 LYS B 126
REMARK 465 GLU B 127
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 GLU A 66 150.42 -45.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 420 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A 421 DISTANCE = 6.44 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F52 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F52 B 201
DBREF 6GR7 A 1 127 UNP P02766 TTHY_HUMAN 21 147
DBREF 6GR7 B 1 127 UNP P02766 TTHY_HUMAN 21 147
SEQRES 1 A 127 GLY PRO THR GLY THR GLY GLU SER LYS CYS PRO LEU MET
SEQRES 2 A 127 VAL LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE
SEQRES 3 A 127 ASN VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP
SEQRES 4 A 127 THR TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER
SEQRES 5 A 127 GLY GLU LEU HIS GLY LEU THR THR GLU GLU GLU PHE VAL
SEQRES 6 A 127 GLU GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR
SEQRES 7 A 127 TRP LYS ALA LEU GLY ILE SER PRO PHE HIS GLU HIS ALA
SEQRES 8 A 127 GLU VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG
SEQRES 9 A 127 TYR THR ILE ALA ALA LEU LEU SER PRO TYR SER TYR SER
SEQRES 10 A 127 THR THR ALA VAL VAL THR ASN PRO LYS GLU
SEQRES 1 B 127 GLY PRO THR GLY THR GLY GLU SER LYS CYS PRO LEU MET
SEQRES 2 B 127 VAL LYS VAL LEU ASP ALA VAL ARG GLY SER PRO ALA ILE
SEQRES 3 B 127 ASN VAL ALA VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP
SEQRES 4 B 127 THR TRP GLU PRO PHE ALA SER GLY LYS THR SER GLU SER
SEQRES 5 B 127 GLY GLU LEU HIS GLY LEU THR THR GLU GLU GLU PHE VAL
SEQRES 6 B 127 GLU GLY ILE TYR LYS VAL GLU ILE ASP THR LYS SER TYR
SEQRES 7 B 127 TRP LYS ALA LEU GLY ILE SER PRO PHE HIS GLU HIS ALA
SEQRES 8 B 127 GLU VAL VAL PHE THR ALA ASN ASP SER GLY PRO ARG ARG
SEQRES 9 B 127 TYR THR ILE ALA ALA LEU LEU SER PRO TYR SER TYR SER
SEQRES 10 B 127 THR THR ALA VAL VAL THR ASN PRO LYS GLU
HET F52 A 201 14
HET F52 B 201 14
HETNAM F52 2-[2,4,5-TRIS(CHLORANYL)PHENOXY]ETHANOIC ACID
FORMUL 3 F52 2(C8 H5 CL3 O3)
FORMUL 5 HOH *238(H2 O)
HELIX 1 AA1 ASP A 74 LEU A 82 1 9
HELIX 2 AA2 ASP B 74 LEU B 82 1 9
SHEET 1 AA1 8 SER A 23 PRO A 24 0
SHEET 2 AA1 8 LEU A 12 ASP A 18 -1 N ASP A 18 O SER A 23
SHEET 3 AA1 8 ARG A 104 SER A 112 1 O LEU A 111 N LEU A 17
SHEET 4 AA1 8 SER A 115 THR A 123 -1 O THR A 123 N ARG A 104
SHEET 5 AA1 8 SER B 115 THR B 123 -1 O TYR B 116 N THR A 118
SHEET 6 AA1 8 ARG B 104 SER B 112 -1 N ARG B 104 O THR B 123
SHEET 7 AA1 8 LEU B 12 ASP B 18 1 N LEU B 17 O LEU B 111
SHEET 8 AA1 8 SER B 23 PRO B 24 -1 O SER B 23 N ASP B 18
SHEET 1 AA2 8 GLU A 54 LEU A 55 0
SHEET 2 AA2 8 LEU A 12 ASP A 18 -1 N VAL A 14 O LEU A 55
SHEET 3 AA2 8 ARG A 104 SER A 112 1 O LEU A 111 N LEU A 17
SHEET 4 AA2 8 SER A 115 THR A 123 -1 O THR A 123 N ARG A 104
SHEET 5 AA2 8 SER B 115 THR B 123 -1 O TYR B 116 N THR A 118
SHEET 6 AA2 8 ARG B 104 SER B 112 -1 N ARG B 104 O THR B 123
SHEET 7 AA2 8 LEU B 12 ASP B 18 1 N LEU B 17 O LEU B 111
SHEET 8 AA2 8 GLU B 54 LEU B 55 -1 O LEU B 55 N VAL B 14
SHEET 1 AA3 8 TRP A 41 LYS A 48 0
SHEET 2 AA3 8 ALA A 29 LYS A 35 -1 N VAL A 32 O ALA A 45
SHEET 3 AA3 8 GLY A 67 ILE A 73 -1 O GLU A 72 N HIS A 31
SHEET 4 AA3 8 HIS A 88 ALA A 97 -1 O ALA A 91 N ILE A 73
SHEET 5 AA3 8 HIS B 88 ALA B 97 -1 O GLU B 89 N VAL A 94
SHEET 6 AA3 8 GLY B 67 ILE B 73 -1 N ILE B 73 O ALA B 91
SHEET 7 AA3 8 ALA B 29 LYS B 35 -1 N HIS B 31 O GLU B 72
SHEET 8 AA3 8 TRP B 41 LYS B 48 -1 O ALA B 45 N VAL B 32
SITE 1 AC1 6 LYS A 15 LEU A 17 ALA A 108 ALA A 109
SITE 2 AC1 6 LEU A 110 HOH A 398
SITE 1 AC2 7 LYS B 15 LEU B 17 ALA B 108 ALA B 109
SITE 2 AC2 7 LEU B 110 HOH B 391 HOH B 400
CRYST1 42.878 85.486 64.488 90.00 90.00 90.00 P 21 21 2 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 0.023322 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011698 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015507 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
