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 : 1452 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 1ZVO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-05. REMARK 100 THE RCSB ID CODE IS RCSB033175. 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 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 : 7.2 REMARK 265 NUMBER OF TIME FRAMES USED : 1 REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 0.30-0.89 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) : 6.94 REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.12 REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : 1.93 REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : 0.04 REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : 1.24 REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : 0.15 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 : 8500 REMARK 265 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 265 CONFORMERS, SELECTION CRITERIA : THE MODELLED SCATTERING REMARK 265 CURVES WERE ASSESSED BY CALCULATION OF THE RG AND RXS-1 VALUES REMARK 265 IN THE SAME Q RANGES USED IN THE EXPERIMENTAL GUINIER FITS. REMARK 265 MODELS WERE THEN RANKED USING A GOODNESS-OF-FIT R-FACTOR REMARK 265 DEFINED BY ANALOGY WITH PROTEIN CRYSTALLOGRAPHY REMARK 265 REMARK 265 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 265 REMARK 265 OTHER DETAILS: HOMOLOGY MODELS WERE BUILT FOR THE FAB AND FC REMARK 265 FRAGMENTS BY TRIAL AND ERROR CONSTRAINED MODELLING. THE REMARK 265 POSITIONS OF THE FRAGMENTS WERE DETERMINED BY AN APPROACH THAT REMARK 265 COMBINED RANDOMISED HINGE PEPTIDE STRUCTURES PRODUCED BY REMARK 265 MOLECULAR DYNAMICS SIMULATIONS WITH CURVE-FITTING TO REMARK 265 EXPERIMENTAL X-RAY SOLUTION SCATTERING DATA. A SINGLE REMARK 265 ARRANGEMENT OF THE FAB AND FC FRAGMENTS IS PRESENTED, WHICH IS REMARK 265 REPRESENTATIVE OF A FAMILY OF STRUCTURES THAT FIT THE REMARK 265 SCATTERING DATA. MORE DETAILS ON THE MODELLING STRATEGY ARE REMARK 265 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 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 ASP C 325 CA GLU D 276 1.15 REMARK 500 CA GLU C 279 CA LEU D 385 1.55 REMARK 500 CA GLN C 295 CA GLU D 282 1.73 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 7FAB RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF IGG1 FAB NEW REMARK 900 RELATED ID: 1FC1 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN IGG FC REMARK 900 RELATED ID: 1IGA RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF IGA1 REMARK 900 RELATED ID: 1R70 RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF IGA2M(1)