REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : INSIGHTII (DISCOVER) REMARK 3 AUTHORS : REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1352 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 1R70 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-03. REMARK 100 THE RCSB ID CODE IS RCSB020514. 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 : SRS BEAMLINE 2.1 REMARK 265 SYNCHROTRON (Y/N) : Y REMARK 265 BEAMLINE TYPE : 2.1 REMARK 265 BEAMLINE INSTRUMENT : NULL REMARK 265 DETECTOR TYPE : 500-CHANNEL REMARK 265 QUADRANT REMARK 265 DETECTOR MANUFACTURER DETAILS : NULL REMARK 265 TEMPERATURE (KELVIN) : 288 REMARK 265 PH : 7.4 REMARK 265 NUMBER OF TIME FRAMES USED : 10 REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 2-15 REMARK 265 SAMPLE BUFFER : DULBECCO PBS REMARK 265 DATA REDUCTION SOFTWARE : OTOKO REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 5.17 REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.11 REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : 2.39 REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : 0.10 REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : 1.37 REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : 0.16 REMARK 265 P(R) PROTEIN LENGTH (NM) : 1 REMARK 265 REMARK 265 EXPERIMENT TYPE : SMALL ANGLE X-RAY SCATTERING REMARK 265 DATA ACQUISITION REMARK 265 RADIATION/NEUTRON SOURCE : ESRF BEAMLINE ID02 REMARK 265 SYNCHROTRON (Y/N) : Y REMARK 265 BEAMLINE TYPE : ID02 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 : 10 REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 0.55-1.12 REMARK 265 SAMPLE BUFFER : DULBECCO PBS REMARK 265 DATA REDUCTION SOFTWARE : MULTICCD REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 5.18 REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.09 REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : 2.47 REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : 0.09 REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : 1.47 REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : 0.08 REMARK 265 P(R) PROTEIN LENGTH (NM) : 16 REMARK 265 REMARK 265 EXPERIMENT TYPE : SMALL ANGLE NEUTRON SCATTERING REMARK 265 DATA ACQUISITION REMARK 265 RADIATION/NEUTRON SOURCE : ISIS REMARK 265 SYNCHROTRON (Y/N) : N REMARK 265 BEAMLINE TYPE : PULSED NEUTRON REMARK 265 BEAMLINE INSTRUMENT : LOQ REMARK 265 DETECTOR TYPE : AREA (TIME-OF- REMARK 265 FLIGHT) REMARK 265 DETECTOR MANUFACTURER DETAILS : NULL REMARK 265 TEMPERATURE (KELVIN) : 288 REMARK 265 PH : 7.4 REMARK 265 NUMBER OF TIME FRAMES USED : NULL REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 2.0-3.0 REMARK 265 SAMPLE BUFFER : PBS IN 99.9% D2O REMARK 265 DATA REDUCTION SOFTWARE : COLLETTE REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 5.03 REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.01 REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : 2.21 REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : 0.10 REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : 1.04 REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : 0.06 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: CONSTRAINED SCATTERING REMARK 265 FITTING OF HOMOLOGY REMARK 265 MODELS REMARK 265 SOFTWARE USED : INSIGHT II, HOMOLOGY, DISCOVERY, REMARK 265 BIOPOLYMER, DELPHI, O, SCTPL7, GNOM REMARK 265 SOFTWARE AUTHORS : ACCELRYS REMARK 265 STARTING MODEL : NULL REMARK 265 REMARK 265 CONFORMERS, NUMBER CALCULATED : 10000 REMARK 265 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 265 CONFORMERS, SELECTION CRITERIA : THE MODELLED SCATTERING REMARK 265 CURVES WERE ASSESSED BY CALCULATION OF THE RG, RSX-1 AND REMARK 265 VALUES IN THE SAME Q RANGES USED IN THE EXPERIMENTAL GUINIER REMARK 265 FITS. MODELS WERE THEN RANKED USING A GOODNESS-OF-FIT R-FACTOR REMARK 265 DEFINED BY ANALOGY WITH PROTEIN CRYSTALLOGRAPHY AND BASED ON REMARK 265 THE EXPERIMENTAL CURVES IN THE Q RANGE EXTENDING TO 2.2 NM-1 REMARK 265 (ESRF X-RAYS) AND 2.2 NM-1 (ISIS NEUTRONS). REMARK 265 REMARK 265 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 265 REMARK 265 OTHER DETAILS: HOMOLOGY MODELS WERE BUILT FOR THE IGA2 FAB AND REMARK 265 FC FRAGMENTS STARTING FROM THE IGA1 MODEL (PDB ENTRY 1IGA). REMARK 265 THE POSITIONS OF THE FAB FRAGMENTS RELATIVE TO THE FC FRAGMENT REMARK 265 WERE DETERMINED BY AN APPROACH THAT COMBINED RANDOM HINGE REMARK 265 PEPTIDE STRUCTURES PRODUCED BY MOLECULAR DYNAMICS SIMULATIONS REMARK 265 WITH CURVE-FITTING TO EXPERIMENTAL SOLUTION SCATTERING DATA. REMARK 265 THE X-RAY AND NEUTRON SCATTERING CURVE I(Q) WAS CALCULATED REMARK 265 ASSUMING A UNIFORM SCATTERING DENSITY FOR THE SPHERES USING REMARK 265 THE DEBYE EQUATION AS ADAPTED TO SPHERES. X-RAY CURVES WERE REMARK 265 CALCULATED FROM THE HYDRATED SPHERE MODELS WITHOUT CORRECTIONS REMARK 265 FOR WAVELENGTH SPREAD OR BEAM DIVERGENCE, WHILE THESE REMARK 265 CORRECTIONS WERE APPLIED FOR THE NEUTRON CURVES BUT NOW USING REMARK 265 UNHYDRATED MODELS. A SINGLE ARRANGEMENT OF THE FAB FRAGMENTS REMARK 265 IS PRESENTED, WHICH IS REPRESENTATIVE OF A FAMILY OF REMARK 265 STRUCTURES THAT FIT THE SCATTERING DATA. MORE DETAILS ON THE REMARK 265 MODELLING STRATEGY ARE CONTAINED IN THE PRIMARY REFERENCE. 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 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1VGE RELATED DB: PDB REMARK 900 HUMAN IGG1 TR1_9 FAB. USED AS TEMPLATE FOR VL, CL AND VH REMARK 900 DOMAINS REMARK 900 RELATED ID: 2FBJ RELATED DB: PDB REMARK 900 MOUSE IGA JS39 FAB. USED AS TEMPLATE FOR CH1 DOMAIN REMARK 900 RELATED ID: 1FC1 RELATED DB: PDB REMARK 900 HUMAN IGG FC (CHAIN A). USED AS TEMPLATE FOR CH2 AND CH3 REMARK 900 DOMAINS REMARK 999 REMARK 999 SEQUENCE REMARK 999 AT THE TIME OF PROCESSING, THERE WERE NO REMARK 999 SUITABLE SEQUENCE DATABASE REFERENCES FOR REMARK 999 THE PROTEINS IN THIS ENTRY.