HEADER CELL ADHESION 14-OCT-16 5M3D
TITLE STRUCTURAL TUNING OF CD81LEL (SPACE GROUP P31)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CD81 ANTIGEN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 112-201;
COMPND 5 SYNONYM: 26 KDA CELL SURFACE PROTEIN TAPA-1,TARGET OF THE
COMPND 6 ANTIPROLIFERATIVE ANTIBODY 1,TETRASPANIN-28,TSPAN-28;
COMPND 7 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: CD81, TAPA1, TSPAN28;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHLSEC
KEYWDS HUMAN CELLULAR RECEPTOR FOR HEPATITIS C VIRUS, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR E.S.CUNHA,P.SFRISO,A.L.ROJAS,P.ROVERSI,A.HOSPITAL,M.OROZCO,
AUTHOR 2 N.G.ABRESCIA
REVDAT 4 17-JAN-24 5M3D 1 REMARK
REVDAT 3 13-DEC-17 5M3D 1 AUTHOR JRNL
REVDAT 2 18-JAN-17 5M3D 1 JRNL
REVDAT 1 14-DEC-16 5M3D 0
JRNL AUTH E.S.CUNHA,P.SFRISO,A.L.ROJAS,P.ROVERSI,A.HOSPITAL,M.OROZCO,
JRNL AUTH 2 N.G.ABRESCIA
JRNL TITL MECHANISM OF STRUCTURAL TUNING OF THE HEPATITIS C VIRUS
JRNL TITL 2 HUMAN CELLULAR RECEPTOR CD81 LARGE EXTRACELLULAR LOOP.
JRNL REF STRUCTURE V. 25 53 2017
JRNL REFN ISSN 1878-4186
JRNL PMID 27916518
JRNL DOI 10.1016/J.STR.2016.11.003
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.KITADOKORO,D.BORDO,G.GALLI,R.PETRACCA,F.FALUGI,
REMARK 1 AUTH 2 S.ABRIGNANI,G.GRANDI,M.BOLOGNESI
REMARK 1 TITL CD81 EXTRACELLULAR DOMAIN 3D STRUCTURE: INSIGHT INTO THE
REMARK 1 TITL 2 TETRASPANIN SUPERFAMILY STRUCTURAL MOTIFS.
REMARK 1 REF EMBO J. V. 20 12 2001
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 11226150
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.KITADOKORO,M.PONASSI,G.GALLI,R.PETRACCA,F.FALUGI,G.GRANDI,
REMARK 1 AUTH 2 M.BOLOGNESI
REMARK 1 TITL SUBUNIT ASSOCIATION AND CONFORMATIONAL FLEXIBILITY IN THE
REMARK 1 TITL 2 HEAD SUBDOMAIN OF HUMAN CD81 LARGE EXTRACELLULAR LOOP.
REMARK 1 REF BIOL. CHEM. V. 383 1447 2002
REMARK 1 REFN ISSN 1431-6730
REMARK 1 PMID 12437138
REMARK 2
REMARK 2 RESOLUTION. 2.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.250
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 14539
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 740
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 48.9843 - 4.0693 0.96 2707 135 0.1636 0.2060
REMARK 3 2 4.0693 - 3.2301 0.98 2738 164 0.1628 0.2079
REMARK 3 3 3.2301 - 2.8219 0.99 2782 139 0.1909 0.2547
REMARK 3 4 2.8219 - 2.5639 0.99 2793 156 0.1940 0.2648
REMARK 3 5 2.5639 - 2.3801 0.99 2779 146 0.2350 0.2895
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.040
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 2810
REMARK 3 ANGLE : 1.009 3773
REMARK 3 CHIRALITY : 0.036 442
REMARK 3 PLANARITY : 0.004 489
REMARK 3 DIHEDRAL : 14.737 1005
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 113:157 OR RESID 189:202)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.9456 -21.0892 4.1491
REMARK 3 T TENSOR
REMARK 3 T11: 0.5959 T22: 0.4945
REMARK 3 T33: 0.6228 T12: 0.0932
REMARK 3 T13: 0.0273 T23: 0.0895
REMARK 3 L TENSOR
REMARK 3 L11: 6.7332 L22: 7.4793
REMARK 3 L33: 5.5403 L12: -2.3676
REMARK 3 L13: 0.0508 L23: -1.6865
REMARK 3 S TENSOR
REMARK 3 S11: 0.0434 S12: 0.2340 S13: 0.4144
REMARK 3 S21: -0.4586 S22: -0.3078 S23: -0.9503
REMARK 3 S31: -0.0918 S32: 0.6288 S33: 0.2395
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 158:188)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.5098 -32.8942 10.9578
REMARK 3 T TENSOR
REMARK 3 T11: 0.7139 T22: 0.6223
REMARK 3 T33: 0.6973 T12: 0.1339
REMARK 3 T13: 0.0890 T23: 0.1913
REMARK 3 L TENSOR
REMARK 3 L11: 5.5292 L22: 3.7022
REMARK 3 L33: 3.4252 L12: 0.5987
REMARK 3 L13: -1.2299 L23: -1.9372
REMARK 3 S TENSOR
REMARK 3 S11: -0.4684 S12: -0.7745 S13: -1.0698
REMARK 3 S21: 0.1258 S22: -0.1079 S23: -0.3008
REMARK 3 S31: 0.6533 S32: 0.0833 S33: 0.5647
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN B AND (RESID 113:157 OR RESID 189:202)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8504 -30.3073 -7.2844
REMARK 3 T TENSOR
REMARK 3 T11: 0.3232 T22: 0.5171
REMARK 3 T33: 0.5005 T12: -0.0199
REMARK 3 T13: -0.0640 T23: 0.0687
REMARK 3 L TENSOR
REMARK 3 L11: 9.0603 L22: 5.9552
REMARK 3 L33: 6.5206 L12: 0.5761
REMARK 3 L13: 0.8577 L23: 0.1926
REMARK 3 S TENSOR
REMARK 3 S11: -0.1845 S12: 0.6224 S13: 0.9159
REMARK 3 S21: -0.1268 S22: -0.3069 S23: -0.0525
REMARK 3 S31: -0.5465 S32: 0.3256 S33: 0.4396
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND (RESID 158:188)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7333 -38.5764 -0.5159
REMARK 3 T TENSOR
REMARK 3 T11: 0.5074 T22: 0.7335
REMARK 3 T33: 0.6532 T12: -0.0110
REMARK 3 T13: -0.1135 T23: 0.1568
REMARK 3 L TENSOR
REMARK 3 L11: 4.7777 L22: 2.9545
REMARK 3 L33: 4.5977 L12: 0.3327
REMARK 3 L13: 0.2902 L23: -2.4907
REMARK 3 S TENSOR
REMARK 3 S11: -0.0572 S12: -0.5891 S13: -0.0735
REMARK 3 S21: 0.2083 S22: -0.7031 S23: -0.6949
REMARK 3 S31: 0.2573 S32: 0.8147 S33: 0.5643
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN C AND (RESID 114:157 OR RESID 189:202)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4606 -33.0810 -13.2174
REMARK 3 T TENSOR
REMARK 3 T11: 0.3910 T22: 0.6501
REMARK 3 T33: 0.5192 T12: 0.1169
REMARK 3 T13: -0.0893 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 7.1886 L22: 6.1499
REMARK 3 L33: 5.4794 L12: 0.2392
REMARK 3 L13: 1.0105 L23: -0.1717
REMARK 3 S TENSOR
REMARK 3 S11: 0.0150 S12: 0.4284 S13: 0.6121
REMARK 3 S21: -0.3264 S22: -0.1896 S23: -0.0217
REMARK 3 S31: -0.1538 S32: -0.0068 S33: 0.2796
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN C AND (RESID 158:188)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6337 -41.9077 -9.3696
REMARK 3 T TENSOR
REMARK 3 T11: 0.6312 T22: 0.7207
REMARK 3 T33: 0.8526 T12: 0.0692
REMARK 3 T13: -0.0996 T23: -0.1040
REMARK 3 L TENSOR
REMARK 3 L11: 3.4225 L22: 4.3894
REMARK 3 L33: 4.0116 L12: 1.4232
REMARK 3 L13: 0.9808 L23: -0.8909
REMARK 3 S TENSOR
REMARK 3 S11: 0.0846 S12: -0.5780 S13: -0.4462
REMARK 3 S21: 0.0814 S22: -0.4686 S23: 0.8238
REMARK 3 S31: 0.6795 S32: -0.3344 S33: 0.2900
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN D AND (RESID 114:157 OR RESID 189:202)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.9047 -10.9892 -1.7281
REMARK 3 T TENSOR
REMARK 3 T11: 0.6623 T22: 0.3819
REMARK 3 T33: 0.5349 T12: 0.0131
REMARK 3 T13: -0.0262 T23: 0.0796
REMARK 3 L TENSOR
REMARK 3 L11: 6.5627 L22: 7.0008
REMARK 3 L33: 5.7007 L12: -1.5939
REMARK 3 L13: 0.1050 L23: -0.0081
REMARK 3 S TENSOR
REMARK 3 S11: -0.1422 S12: 0.3115 S13: 0.2562
REMARK 3 S21: -0.5756 S22: 0.0207 S23: -0.5069
REMARK 3 S31: -0.1300 S32: 0.1879 S33: 0.1600
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN D AND (RESID 158:188)
REMARK 3 ORIGIN FOR THE GROUP (A): -44.5872 -6.5503 2.0753
REMARK 3 T TENSOR
REMARK 3 T11: 0.6622 T22: 0.4958
REMARK 3 T33: 0.7157 T12: 0.0111
REMARK 3 T13: -0.1361 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 5.9927 L22: 3.5831
REMARK 3 L33: 4.8902 L12: -0.7752
REMARK 3 L13: 0.4391 L23: -0.6653
REMARK 3 S TENSOR
REMARK 3 S11: -0.4602 S12: -0.4947 S13: 0.1338
REMARK 3 S21: 0.2125 S22: 0.0435 S23: 0.5862
REMARK 3 S31: -0.0166 S32: -0.5277 S33: 0.3563
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 5M3D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1200001789.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14545
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.380
REMARK 200 RESOLUTION RANGE LOW (A) : 48.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.71200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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: 1G8Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 10 MG/ML BUFFER: 40% ETOH,
REMARK 280 0.097 M CITRATE PH 2.2, 0.113 M NA2HPO4 PH 9.3, (PH ~6) 2.5% PEG
REMARK 280 1000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 11.46967
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 22.93933
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 GLU A 110
REMARK 465 THR A 111
REMARK 465 GLY A 112
REMARK 465 THR A 203
REMARK 465 LYS A 204
REMARK 465 HIS A 205
REMARK 465 HIS A 206
REMARK 465 HIS A 207
REMARK 465 HIS A 208
REMARK 465 HIS A 209
REMARK 465 HIS A 210
REMARK 465 GLU B 110
REMARK 465 THR B 111
REMARK 465 THR B 203
REMARK 465 LYS B 204
REMARK 465 HIS B 205
REMARK 465 HIS B 206
REMARK 465 HIS B 207
REMARK 465 HIS B 208
REMARK 465 HIS B 209
REMARK 465 HIS B 210
REMARK 465 GLU C 110
REMARK 465 THR C 111
REMARK 465 GLY C 112
REMARK 465 PHE C 113
REMARK 465 THR C 203
REMARK 465 LYS C 204
REMARK 465 HIS C 205
REMARK 465 HIS C 206
REMARK 465 HIS C 207
REMARK 465 HIS C 208
REMARK 465 HIS C 209
REMARK 465 HIS C 210
REMARK 465 GLU D 110
REMARK 465 THR D 111
REMARK 465 GLY D 112
REMARK 465 PHE D 113
REMARK 465 THR D 203
REMARK 465 LYS D 204
REMARK 465 HIS D 205
REMARK 465 HIS D 206
REMARK 465 HIS D 207
REMARK 465 HIS D 208
REMARK 465 HIS D 209
REMARK 465 HIS D 210
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 O PRO C 176 OG SER C 179 2.18
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 CYS B 157 17.29 -144.73
REMARK 500 LYS C 171 58.66 -140.19
REMARK 500 ASP D 139 26.97 -143.47
REMARK 500 CYS D 157 18.36 -146.79
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 EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5M2C RELATED DB: PDB
REMARK 900 RELATED ID: 5M33 RELATED DB: PDB
REMARK 900 RELATED ID: 5M4R RELATED DB: PDB
REMARK 900 RELATED ID: 5M3T RELATED DB: PDB
REMARK 900 RELATED ID: 1G8Q RELATED DB: PDB
REMARK 900 RELATED ID: 1IV5 RELATED DB: PDB
DBREF 5M3D A 112 201 UNP P60033 CD81_HUMAN 112 201
DBREF 5M3D B 112 201 UNP P60033 CD81_HUMAN 112 201
DBREF 5M3D C 112 201 UNP P60033 CD81_HUMAN 112 201
DBREF 5M3D D 112 201 UNP P60033 CD81_HUMAN 112 201
SEQADV 5M3D GLU A 110 UNP P60033 EXPRESSION TAG
SEQADV 5M3D THR A 111 UNP P60033 EXPRESSION TAG
SEQADV 5M3D GLY A 202 UNP P60033 EXPRESSION TAG
SEQADV 5M3D THR A 203 UNP P60033 EXPRESSION TAG
SEQADV 5M3D LYS A 204 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS A 205 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS A 206 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS A 207 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS A 208 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS A 209 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS A 210 UNP P60033 EXPRESSION TAG
SEQADV 5M3D GLU B 110 UNP P60033 EXPRESSION TAG
SEQADV 5M3D THR B 111 UNP P60033 EXPRESSION TAG
SEQADV 5M3D GLY B 202 UNP P60033 EXPRESSION TAG
SEQADV 5M3D THR B 203 UNP P60033 EXPRESSION TAG
SEQADV 5M3D LYS B 204 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS B 205 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS B 206 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS B 207 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS B 208 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS B 209 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS B 210 UNP P60033 EXPRESSION TAG
SEQADV 5M3D GLU C 110 UNP P60033 EXPRESSION TAG
SEQADV 5M3D THR C 111 UNP P60033 EXPRESSION TAG
SEQADV 5M3D GLY C 202 UNP P60033 EXPRESSION TAG
SEQADV 5M3D THR C 203 UNP P60033 EXPRESSION TAG
SEQADV 5M3D LYS C 204 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS C 205 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS C 206 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS C 207 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS C 208 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS C 209 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS C 210 UNP P60033 EXPRESSION TAG
SEQADV 5M3D GLU D 110 UNP P60033 EXPRESSION TAG
SEQADV 5M3D THR D 111 UNP P60033 EXPRESSION TAG
SEQADV 5M3D GLY D 202 UNP P60033 EXPRESSION TAG
SEQADV 5M3D THR D 203 UNP P60033 EXPRESSION TAG
SEQADV 5M3D LYS D 204 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS D 205 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS D 206 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS D 207 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS D 208 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS D 209 UNP P60033 EXPRESSION TAG
SEQADV 5M3D HIS D 210 UNP P60033 EXPRESSION TAG
SEQRES 1 A 101 GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP
SEQRES 2 A 101 VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL
SEQRES 3 A 101 VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS
SEQRES 4 A 101 THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR
SEQRES 5 A 101 LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU
SEQRES 6 A 101 CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS
SEQRES 7 A 101 GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY
SEQRES 8 A 101 LYS GLY THR LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 101 GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP
SEQRES 2 B 101 VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL
SEQRES 3 B 101 VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS
SEQRES 4 B 101 THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR
SEQRES 5 B 101 LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU
SEQRES 6 B 101 CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS
SEQRES 7 B 101 GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY
SEQRES 8 B 101 LYS GLY THR LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 101 GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP
SEQRES 2 C 101 VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL
SEQRES 3 C 101 VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS
SEQRES 4 C 101 THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR
SEQRES 5 C 101 LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU
SEQRES 6 C 101 CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS
SEQRES 7 C 101 GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY
SEQRES 8 C 101 LYS GLY THR LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 D 101 GLU THR GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP
SEQRES 2 D 101 VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL
SEQRES 3 D 101 VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS
SEQRES 4 D 101 THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR
SEQRES 5 D 101 LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU
SEQRES 6 D 101 CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS
SEQRES 7 D 101 GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY
SEQRES 8 D 101 LYS GLY THR LYS HIS HIS HIS HIS HIS HIS
HET EDO A 301 10
HET EDO A 302 10
HET PO4 B 301 5
HET PO4 B 302 5
HET EDO B 303 10
HET PO4 C 301 5
HET PO4 C 302 5
HET EDO C 303 10
HET PO4 D 601 5
HET PO4 D 602 5
HET EDO D 603 10
HET EDO D 604 10
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PO4 PHOSPHATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 EDO 6(C2 H6 O2)
FORMUL 7 PO4 6(O4 P 3-)
FORMUL 17 HOH *10(H2 O)
HELIX 1 AA1 ASN A 115 ASP A 137 1 23
HELIX 2 AA2 ALA A 140 ASP A 155 1 16
HELIX 3 AA3 SER A 160 LYS A 171 1 12
HELIX 4 AA4 ASN A 172 CYS A 175 5 4
HELIX 5 AA5 ASN A 180 PHE A 186 5 7
HELIX 6 AA6 ASP A 189 GLY A 200 1 12
HELIX 7 AA7 ASN B 115 ASP B 137 1 23
HELIX 8 AA8 ALA B 140 ASP B 155 1 16
HELIX 9 AA9 SER B 160 LYS B 171 1 12
HELIX 10 AB1 ASN B 172 CYS B 175 5 4
HELIX 11 AB2 ILE B 182 LYS B 187 1 6
HELIX 12 AB3 ASP B 189 GLY B 200 1 12
HELIX 13 AB4 ASN C 115 VAL C 135 1 21
HELIX 14 AB5 ASN C 142 ASP C 155 1 14
HELIX 15 AB6 SER C 160 LYS C 171 1 12
HELIX 16 AB7 ASN C 172 CYS C 175 5 4
HELIX 17 AB8 ILE C 181 PHE C 186 5 6
HELIX 18 AB9 ASP C 189 GLY C 200 1 12
HELIX 19 AC1 ASN D 115 VAL D 136 1 22
HELIX 20 AC2 ASN D 142 ASP D 155 1 14
HELIX 21 AC3 SER D 160 LYS D 171 1 12
HELIX 22 AC4 ASN D 172 CYS D 175 5 4
HELIX 23 AC5 ILE D 181 PHE D 186 5 6
HELIX 24 AC6 ASP D 189 GLY D 200 1 12
SSBOND 1 CYS A 156 CYS A 190 1555 1555 2.02
SSBOND 2 CYS A 157 CYS A 175 1555 1555 2.01
SSBOND 3 CYS B 156 CYS B 190 1555 1555 2.01
SSBOND 4 CYS B 157 CYS B 175 1555 1555 2.00
SSBOND 5 CYS C 156 CYS C 190 1555 1555 2.03
SSBOND 6 CYS C 157 CYS C 175 1555 1555 2.03
SSBOND 7 CYS D 156 CYS D 190 1555 1555 2.02
SSBOND 8 CYS D 157 CYS D 175 1555 1555 2.02
CISPEP 1 GLY B 112 PHE B 113 0 4.45
SITE 1 AC1 5 ASN A 172 CYS A 175 PRO A 176 SER A 177
SITE 2 AC1 5 GLY A 178
SITE 1 AC2 4 GLN A 129 ALA A 130 GLN A 133 ASN A 142
SITE 1 AC3 5 SER B 159 SER B 160 ASP B 189 HIS B 191
SITE 2 AC3 5 THR D 161
SITE 1 AC4 6 ASN B 172 CYS B 175 PRO B 176 SER B 177
SITE 2 AC4 6 GLY B 178 SER B 179
SITE 1 AC5 1 GLN B 129
SITE 1 AC6 3 LYS A 121 LYS C 124 HIS C 191
SITE 1 AC7 2 ASP C 139 LYS C 144
SITE 1 AC8 5 ASN C 172 CYS C 175 PRO C 176 GLY C 178
SITE 2 AC8 5 SER C 179
SITE 1 AC9 4 LYS B 121 ASP B 138 LYS D 124 HIS D 191
SITE 1 AD1 2 ASP D 139 LYS D 144
SITE 1 AD2 4 ASN D 172 CYS D 175 PRO D 176 SER D 179
SITE 1 AD3 4 PHE D 126 GLN D 129 ALA D 130 ASN D 141
CRYST1 97.948 97.948 34.409 90.00 90.00 120.00 P 31 12
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 0.010209 0.005894 0.000000 0.00000
SCALE2 0.000000 0.011789 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029062 0.00000
(ATOM LINES ARE NOT SHOWN.)
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