REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.BONNER,P.B.FURTADO,A.ALMOGREN,M.A.KERR,S.J.PERKINS REMARK 1 TITL IMPLICATIONS OF THE NEAR-PLANAR SOLUTION STRUCTURE OF HUMAN REMARK 1 TITL 2 MYELOMA DIMERIC IGA1 FOR MUCOSAL IMMUNITY AND IGA REMARK 1 TITL 3 NEPHROPATHY REMARK 1 REF J. IMMUNOL. V. 180 1008 2008 REMARK 1 REFN ISSN 0022-1767 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.K.BOEHM,J.M.WOOF,M.A.KERR,S.J.PERKINS REMARK 1 TITL THE FAB AND FC FRAGMENTS OF IGA1 EXHIBIT A DIFFERENT REMARK 1 TITL 2 ARRANGEMENT FROM THAT IN IGG: A STUDY BY X-RAY AND NEUTRON REMARK 1 TITL 3 SOLUTION SCATTERING AND HOMOLOGY MODELLING REMARK 1 REF J.MOL.BIOL. V. 286 1421 1999 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 3 REMARK 1 AUTH A.BONNER,C.PERRIER,B.CORTHESY,S.J.PERKINS REMARK 1 TITL SOLUTION STRUCTURE OF HUMAN SECRETORY COMPONENT AND REMARK 1 TITL 2 IMPLICATION FOR BIOLOGICAL FUNCTION REMARK 1 REF J.BIOL.CHEM. V. 282 16969 2007 REMARK 1 REFN ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : INSIGHT II 98 REMARK 3 AUTHORS : REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3447 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3CHN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-08. REMARK 100 THE RCSB ID CODE IS RCSB046786. REMARK 265 REMARK 265 EXPERIMENTAL DETAILS REMARK 265 REMARK 265 EXPERIMENT TYPE : SMALL ANGLE X-RAY SCATTERING REMARK 265 DATA ACQUISITION REMARK 265 RADIATION/NEUTRON SOURCE : ESRF GRENOBLE REMARK 265 SYNCHROTRON (Y/N) : Y REMARK 265 BEAMLINE TYPE : ID2 REMARK 265 BEAMLINE INSTRUMENT : NULL REMARK 265 DETECTOR TYPE : FRELON CCD CAMERA REMARK 265 DETECTOR MANUFACTURER DETAILS : NULL REMARK 265 TEMPERATURE (KELVIN) : 288 REMARK 265 PH : 7.5 REMARK 265 NUMBER OF TIME FRAMES USED : 10 REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 0.30-0.60 REMARK 265 SAMPLE BUFFER : 140 MM NACL 12.5 MM REMARK 265 NAHPO4 0.5 MM EDTA REMARK 265 0.02% NA AZIDE REMARK 265 DATA REDUCTION SOFTWARE : MULTICCD REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 8.29 REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.20 REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : 3.95 REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : 0.13 REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : 1.30 REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : 0.06 REMARK 265 P(R) PROTEIN LENGTH (NM) : 1 REMARK 265 REMARK 265 EXPERIMENT TYPE : SMALL ANGLE NEUTRON SCATTERING REMARK 265 DATA ACQUISITION REMARK 265 RADIATION/NEUTRON SOURCE : ISIS RUTHERFORD- REMARK 265 APPLETON LAB REMARK 265 SYNCHROTRON (Y/N) : Y REMARK 265 BEAMLINE TYPE : LOQ REMARK 265 BEAMLINE INSTRUMENT : NULL REMARK 265 DETECTOR TYPE : HE-3 ORDELA DETECTOR REMARK 265 DETECTOR MANUFACTURER DETAILS : NULL REMARK 265 TEMPERATURE (KELVIN) : 288 REMARK 265 PH : 7.5 REMARK 265 NUMBER OF TIME FRAMES USED : 1 REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 0.60 REMARK 265 SAMPLE BUFFER : 140 MM NACL 12.5 MM REMARK 265 NAHPO4 0.5 MM EDTA REMARK 265 0.02% NA AZIDE REMARK 265 DATA REDUCTION SOFTWARE : COLETTE REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 7.22 REMARK 265 SIGMA MEAN RADIUS OF GYRATION : NULL REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : NULL REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : NULL REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : NULL REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : NULL REMARK 265 P(R) PROTEIN LENGTH (NM) : 1 REMARK 265 REMARK 265 DATA ANALYSIS AND MODEL FITTING: REMARK 265 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 265 SOFTWARE USED : INSIGHT II, SCTPL7, GNOM REMARK 265 SOFTWARE AUTHORS : NULL REMARK 265 STARTING MODEL : NULL REMARK 265 REMARK 265 CONFORMERS, NUMBER CALCULATED : NULL REMARK 265 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 265 CONFORMERS, SELECTION CRITERIA : NULL REMARK 265 REMARK 265 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 265 REMARK 265 OTHER DETAILS: THE COORDINATES CONTAIN ONLY CA ATOMS. THE TEN REMARK 265 BEST-FIT SOLUTION STRUCTURES HAVE BEEN DEPOSITED, WHERE MODEL 1 REMARK 265 IS THE BEST-FIT SIGA1 SOLUTION STRUCTURE AND MODELS 2 TO 10 REMARK 265 REPRESENT THE REST OF THE FAMILY OF BEST-FIT STRUCTURES. 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 300 REMARK: THE BIOLOGICAL ASSEMBLY OF SIGA1 CONSISTS OF FOUR IGA1 REMARK 300 HEAVY CHAINS (A,B,C AND D), FOUR LIGHT CHAINS (L, M, N AND O), J REMARK 300 CHAIN (J) AND SECRETORY COMPONENT (S). 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: DECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, M, N, O, A, B, D, C, J, S 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 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 CA GLY S 450 CA ARG S 547 0.89 REMARK 500 CA LYS S 447 CA VAL S 544 1.04 REMARK 500 CA SER J 348 CA LEU S 153 1.05 REMARK 500 CA GLY D 313 CA SER S 496 1.20 REMARK 500 CA LYS D 290 CA TRP S 477 1.24 REMARK 500 CA PRO D 312 CA PRO S 495 1.38 REMARK 500 CA PRO D 286 CA SER S 490 1.41 REMARK 500 CA SER D 243 CA SER C 243 1.41 REMARK 500 CA SER A 243 CA SER B 243 1.42 REMARK 500 CA CYS D 474 CA GLY S 375 1.43 REMARK 500 CA GLU B 469 CA ARG S 174 1.52 REMARK 500 CA LEU D 311 CA GLY S 494 1.62 REMARK 500 CA GLY J 385 CA TYR S 169 1.70 REMARK 500 CA ARG S 298 CA LEU S 326 1.71 REMARK 500 CA GLN S 111 CA LEU S 184 1.72 REMARK 500 CA ARG J 394 CA GLN S 150 1.73 REMARK 500 CA VAL B 465 CA VAL S 165 1.82 REMARK 500 CA LYS D 322 CA VAL S 500 1.83 REMARK 500 CA TYR S 391 CA LEU S 569 1.87 REMARK 500 CA GLU S 108 CA GLN S 182 1.89 REMARK 500 CA ALA D 292 CA LEU S 488 1.97 REMARK 500 CA LYS D 322 CA PHE S 499 2.03 REMARK 500 CA GLU B 392 CA GLY S 205 2.04 REMARK 500 CA VAL D 144 CA PRO D 226 2.07 REMARK 500 CA VAL A 144 CA PRO A 226 2.07 REMARK 500 CA ASP S 125 CA GLY S 242 2.08 REMARK 500 CA ASN J 374 CA GLY S 303 2.08 REMARK 500 CA GLY J 393 CA LYS S 149 2.09 REMARK 500 CA LYS S 299 CA LEU S 326 2.12 REMARK 500 CA CYS D 314 CA LEU S 511 2.12 REMARK 500 CA SER J 383 CA PRO S 167 2.14 REMARK 500 CA VAL C 144 CA PRO C 226 2.19 REMARK 500 CA VAL B 144 CA PRO B 226 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2QTJ RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF DIMERIC IGA1 REMARK 900 RELATED ID: 1IGA RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF MONOMERIC IGA1 REMARK 900 RELATED ID: 2OCW RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF SECRETORY COMPONENT REMARK 900 RELATED ID: 3CM9 RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF HUMAN SIGA2 REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE PART OF SEQUENCE BELONGS TO IGA VARIABLE HEAVY CHAIN.