REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.J.PERKINS,A.W.ASHTON,M.K.BOEHM,D.CHAMBERLAIN REMARK 1 TITL MOLECULAR STRUCTURES FROM LOW ANGLE X-RAY AND REMARK 1 TITL 2 NEUTRON SCATTERING STUDIES REMARK 1 REF INT.J.BIOL.MACROMOL. V. 22 1 1998 REMARK 1 REFN ISSN 0141-8130 REMARK 1 REFERENCE 2 REMARK 1 AUTH S.J.PERKINS,C.G.ULLMAN,N.C.BRISSETT,D.CHAMBERLAIN, REMARK 1 AUTH 2 M.K.BOEHM REMARK 1 TITL ANALOGY AND SOLUTION SCATTERING MODELLING: NEW REMARK 1 TITL 2 STRUCTURAL STRATEGIES FOR THE MULTIDOMAIN PROTEINS REMARK 1 TITL 3 OF COMPLEMENT, CARTILAGE AND THE IMMUNOGLOBULIN REMARK 1 TITL 4 SUPERFAMILY REMARK 1 REF IMMUNOL.REV. V. 163 237 1998 REMARK 1 REFN ISSN 0105-2896 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER V. 3.0 REMARK 3 AUTHORS : REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1378 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 1IGA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. 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 DARESBURY REMARK 265 SYNCHROTRON (Y/N) : Y REMARK 265 BEAMLINE TYPE : 2.1 REMARK 265 BEAMLINE INSTRUMENT : NULL REMARK 265 DETECTOR TYPE : QUADRANT DETECTOR REMARK 265 DETECTOR MANUFACTURER DETAILS : NULL REMARK 265 TEMPERATURE (KELVIN) : NULL REMARK 265 PH : NULL REMARK 265 NUMBER OF TIME FRAMES USED : 1 REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : NULL REMARK 265 SAMPLE BUFFER : NULL REMARK 265 DATA REDUCTION SOFTWARE : OTOKO REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : NULL 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) : NULL 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) : NULL REMARK 265 PH : NULL REMARK 265 NUMBER OF TIME FRAMES USED : 1 REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : NULL REMARK 265 SAMPLE BUFFER : NULL REMARK 265 DATA REDUCTION SOFTWARE : COLETTE REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : NULL 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) : NULL REMARK 265 REMARK 265 DATA ANALYSIS AND MODEL FITTING: REMARK 265 METHOD USED TO DETERMINE THE STRUCTURE: SCATTERING FITTING, REMARK 265 ENERGY MINIMIZATION REMARK 265 SOFTWARE USED : INSIGHT II, DISCOVERY 2.9.7, BIOSYM 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 : 1 REMARK 265 REMARK 265 OTHER DETAILS: THE MODEL OF HUMAN IGA1 WAS BASED ON SEVERAL REMARK 265 IMMUNOGLOBULIN CRYSTAL STRUCTURES FROM THE PDB. AN IGA1 REMARK 265 MONOMER CONTAINS TWELVE DOMAINS ON TWO FOUR-DOMAIN HEAVY REMARK 265 CHAINS AND TWO TWO-DOMAIN LIGHT CHAINS. THE CHAINS ASSOCIATE REMARK 265 TO FORM TWO FOUR-DOMAIN FAB FRAGMENTS AND ONE FOUR-DOMAIN FC REMARK 265 FRAGMENT. EACH FAB FRAGMENT IS JOINED TO THE FC FRAGMENT BY A REMARK 265 23-RESIDUE PEPTIDE LINKER. THERE ARE SIX DOMAIN TYPES IN IGA1 REMARK 265 (VH, CH1, CH2, CH3, VL AND CL), AND A MONOMER CONTAINS TWO REMARK 265 COPIES OF EACH DOMAIN-TYPE. THE SEQUENCES OF THE CH1, CH2 AND REMARK 265 CH3 DOMAINS ARE SPECIFIC TO IGA1. REFINEMENT WAS CARRIED OUT REMARK 265 USING DISCOVER 2.9.7, BIOSYM. ALSO USED ENERGY MINIMISATION. REMARK 265 THE IGA1 CH1 DOMAIN WAS MODELLED USING THE CORRESPONDING REMARK 265 DOMAIN FROM THE THE MOUSE IGA J539 FAB STRUCTURE (CODE: 2FBJ) REMARK 265 AND THE HUMAN IGG1 TR1.9 FAB STRUCTURE (CODE: 1VGE) AS REMARK 265 TEMPLATES. THE IGA1 CH2 AND CH3 DOMAINS WERE MODELLED USING REMARK 265 THE CORRESPONDING DOMAINS FROM THE HUMAN IGG1 FC STRUCTURE REMARK 265 (CODE: 1FC1) AS TEMPLATES. THE REMAINING DOMAINS IN THE IGA1 REMARK 265 MODEL (VL, CL AND VH) USED THE APPROPRIATE DOMAINS FROM THE REMARK 265 TR1.9 FAB STRUCTURE DIRECTLY. EACH FAB FRAGMENT CONTAINS A REMARK 265 SINGLE COPY OF THE VH, CH1, VL AND CL DOMAINS, AND THEIR REMARK 265 ARRANGEMENT WAS BASED DIRECTLY ON THE TR1.9 FAB STRUCTURE. IN REMARK 265 THE FC STRUCTURE, TWO COPIES OF THE CH2 AND CH3 DOMAINS WERE REMARK 265 USED. THEIR ARRANGEMENT WAS BASED ON THAT IN THE HUMAN IGG1 FC REMARK 265 STRUCTURE (CODE 1FC1) EXCEPT THAT THE TWO CH2 DOMAINS WERE REMARK 265 REORIENTATED AND REMODELLED SLIGHTLY TO ACCOMMODATE A PROPOSED REMARK 265 DISULPHIDE BRIDGING PATTERN. THE POSITIONS OF THE FAB REMARK 265 FRAGMENTS RELATIVE TO THE FC FRAGMENT WERE DETERMINED BY AN REMARK 265 APPROACH THAT COMBINED RANDOM HINGE PEPTIDE STRUCTURES REMARK 265 PRODUCED BY MOLECULAR DYNAMICS SIMULATIONS WITH CURVE-FITTING REMARK 265 TO EXPERIMENTAL SOLUTION SCATTERING DATA. A SINGLE ARRANGEMENT REMARK 265 OF THE FAB FRAGMENTS IS PRESENTED, WHICH IS REPRESENTATIVE OF REMARK 265 A FAMILY OF STRUCTURES THAT FIT THE SCATTERING DATA. IN REMARK 265 ADDITION, IGA1 CONTAINS AN 18-RESIDUE TAILPIECE PEPTIDE AT THE REMARK 265 C-TERMINAL OF EACH CH3 DOMAIN. THE TAILPIECE STRUCTURE REMARK 265 PRODUCED BY MOLECULAR DYNAMICS SIMULATIONS THAT BEST-FITTED REMARK 265 THE EXPERIMENTAL DATA IS SHOWN ON EACH MODEL. MORE DETAILS ON REMARK 265 THE 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