REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : INSIGHTII 98 REMARK 3 AUTHORS : REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1956 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 2ESG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-05. REMARK 100 THE RCSB ID CODE IS RCSB035036. 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 : IDO2 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 : 7.4 REMARK 265 NUMBER OF TIME FRAMES USED : 1 REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 0.9-1.9 REMARK 265 SAMPLE BUFFER : 12.5 MM NA REMARK 265 PHOSPHATE 140 MM REMARK 265 NACL REMARK 265 DATA REDUCTION SOFTWARE : MULTICCD REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 7.47 REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.31 REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : 2.31 REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : 0.11 REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : 1.31 REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : 0.05 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 SYNCHROTRON (Y/N) : Y REMARK 265 BEAMLINE TYPE : LOQ REMARK 265 BEAMLINE INSTRUMENT : NULL REMARK 265 DETECTOR TYPE : HE-3 ORDELA REMARK 265 DETECTOR REMARK 265 DETECTOR MANUFACTURER DETAILS : NULL REMARK 265 TEMPERATURE (KELVIN) : 288 REMARK 265 PH : 7.4 REMARK 265 NUMBER OF TIME FRAMES USED : 1 REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 1.2-1.9 REMARK 265 SAMPLE BUFFER : 12.5 MM NA REMARK 265 PHOSPHATE 140 MM REMARK 265 NACL 99.9% D2O REMARK 265 DATA REDUCTION SOFTWARE : COLETTE REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 7.09 REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.10 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) : NULL 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 : 1 REMARK 265 CONFORMERS, SELECTION CRITERIA : NULL REMARK 265 REMARK 265 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 265 REMARK 265 OTHER DETAILS: 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, M, A, 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 ASP C 1 REMARK 465 ALA C 2 REMARK 465 HIS C 3 REMARK 465 LYS C 4 REMARK 465 LEU C 583 REMARK 465 GLY C 584 REMARK 465 LEU C 585 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 THR A 473 CA VAL C 77 1.12 REMARK 500 CA ASP A 471 CA LEU C 80 1.64 REMARK 500 CA SER A 464 CA GLU C 82 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1IGA RELATED DB: PDB REMARK 900 IMMUNOGLOBULIN IGA1 REMARK 900 RELATED ID: 1AO6 RELATED DB: PDB REMARK 900 HUMAN SERUM ALBUMIN REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE VH DOMAIN SEQUENCE (RESIDUES 1-122) IS THAT FROM THE REMARK 999 HUMAN TR1.9 FAB STRUCTURE (CODE: 1VGE). REMARK 999 THE LIGHT CHAIN SEQUENCE IS THAT FROM THE HUMAN TR1.9 REMARK 999 FAB STRUCTURE (CODE: 1VGE).