HEADER IMMUNE SYSTEM 18-FEB-09 3GAV
TITLE SOLUTION STRUCTURE OF HUMAN COMPLEMENT FACTOR H IN 137 MM NACL BUFFER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COMPLEMENT FACTOR H;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: H FACTOR 1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 OTHER_DETAILS: PURIFIED FROM POOLED PLASMA
KEYWDS X-RAY SOLUTION SCATTERING, COMPLEMENT FACTOR H, SCR DOMAIN, AGE-
KEYWDS 2 RELATED MACULAR DEGENERATION, COMPLEMENT ALTERNATE PATHWAY, DISEASE
KEYWDS 3 MUTATION, GLYCOPROTEIN, IMMUNE RESPONSE, INNATE IMMUNITY, SECRETED,
KEYWDS 4 SUSHI, IMMUNE SYSTEM
EXPDTA SOLUTION SCATTERING
NUMMDL 8
MDLTYP CA ATOMS ONLY, CHAIN A
AUTHOR A.I.OKEMEFUNA,R.NAN,J.GOR,S.J.PERKINS
REVDAT 8 21-FEB-24 3GAV 1 SEQADV
REVDAT 7 01-NOV-17 3GAV 1 REMARK
REVDAT 6 27-JUL-11 3GAV 1 REVDAT
REVDAT 5 13-JUL-11 3GAV 1 VERSN
REVDAT 4 07-APR-10 3GAV 1 REMARK
REVDAT 3 11-AUG-09 3GAV 1 JRNL
REVDAT 2 16-JUN-09 3GAV 1 CRYST1
REVDAT 1 09-JUN-09 3GAV 0
JRNL AUTH A.I.OKEMEFUNA,R.NAN,J.GOR,S.J.PERKINS
JRNL TITL ELECTROSTATIC INTERACTIONS CONTRIBUTE TO THE FOLDED-BACK
JRNL TITL 2 CONFORMATION OF WILD TYPE HUMAN FACTOR H.
JRNL REF J.MOL.BIOL. V. 391 98 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19505476
JRNL DOI 10.1016/J.JMB.2009.06.010
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 : 1213
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE COORDINATES CONTAIN ONLY CA ATOMS.
REMARK 4
REMARK 4 3GAV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1000051637.
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) : 293
REMARK 265 PH : 7.4
REMARK 265 NUMBER OF TIME FRAMES USED : 10
REMARK 265 PROTEIN CONCENTRATION RANGE (MG/ML) : 0.40
REMARK 265 SAMPLE BUFFER : 137 MM NACL 10 MM
REMARK 265 HEPES 0.5 MM EDTA
REMARK 265 DATA REDUCTION SOFTWARE : MULTICCD
REMARK 265 GUINIER MEAN RADIUS OF GYRATION (NM) : 8.90
REMARK 265 SIGMA MEAN RADIUS OF GYRATION : 0.19
REMARK 265 R(XS-1) MEAN CROSS SECTIONAL RADII (NM) : 2.51
REMARK 265 R(XS-1) SIGMA MEAN CROSS SECTIONAL RADII : 0.06
REMARK 265 R(XS-2) MEAN CROSS SECTIONAL RADII (NM) : 1.79
REMARK 265 R(XS-2) SIGMA MEAN CROSS SECTIONAL RADII : 0.01
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 : 5000
REMARK 265 CONFORMERS, NUMBER SUBMITTED : 8
REMARK 265 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 265 GOODNESS-OF-FIT R-FACTOR AFTER FILTERING ON RG AND RXS-1
REMARK 265
REMARK 265 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 HIS A 332 CA ARG A 387 1.19
REMARK 500 CA ASP A 329 CA ASN A 434 1.80
REMARK 500 CA PHE A 93 CA VAL A 143 1.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2RLP RELATED DB: PDB
REMARK 900 FH SCR DOMAINS 1-2 (NMR STRUCTURE)
REMARK 900 RELATED ID: 2RLQ RELATED DB: PDB
REMARK 900 FH SCR DOMAINS 2-3 (NMR STRUCTURE)
REMARK 900 RELATED ID: 2UWN RELATED DB: PDB
REMARK 900 FH SCR DOMAINS 6-8 (CRYSTAL STRUCTURE)
REMARK 900 RELATED ID: 1HFH RELATED DB: PDB
REMARK 900 FH SCR DOMAINS 15-16 (NMR STRUCTURE)
REMARK 900 RELATED ID: 2G7I RELATED DB: PDB
REMARK 900 FH SCR DOMAINS 19-20 (CRYSTAL STRUCTURE)
REMARK 900 RELATED ID: 1HAQ RELATED DB: PDB
REMARK 900 FH SCR 1-20 SOLUTION STRUCTURE FROM 2001
REMARK 900 RELATED ID: 2IC4 RELATED DB: PDB
REMARK 900 FH SCR 6-8 SOLUTION STRUCTURE FROM 2007
REMARK 900 RELATED ID: 2QFG RELATED DB: PDB
REMARK 900 FH SCR 1-5 SOLUTION STRUCTURE FROM 2008
REMARK 900 RELATED ID: 2QFH RELATED DB: PDB
REMARK 900 FH SCR 16-20 SOLUTION STRUCTURE FROM 2008
REMARK 900 RELATED ID: 3GAU RELATED DB: PDB
REMARK 900 RELATED ID: 3GAW RELATED DB: PDB
DBREF 3GAV A 19 1231 UNP P08603 CFAH_HUMAN 19 1231
SEQADV 3GAV HIS A 402 UNP P08603 TYR 402 VARIANT
SEQRES 1 A 1213 GLU ASP CYS ASN GLU LEU PRO PRO ARG ARG ASN THR GLU
SEQRES 2 A 1213 ILE LEU THR GLY SER TRP SER ASP GLN THR TYR PRO GLU
SEQRES 3 A 1213 GLY THR GLN ALA ILE TYR LYS CYS ARG PRO GLY TYR ARG
SEQRES 4 A 1213 SER LEU GLY ASN VAL ILE MET VAL CYS ARG LYS GLY GLU
SEQRES 5 A 1213 TRP VAL ALA LEU ASN PRO LEU ARG LYS CYS GLN LYS ARG
SEQRES 6 A 1213 PRO CYS GLY HIS PRO GLY ASP THR PRO PHE GLY THR PHE
SEQRES 7 A 1213 THR LEU THR GLY GLY ASN VAL PHE GLU TYR GLY VAL LYS
SEQRES 8 A 1213 ALA VAL TYR THR CYS ASN GLU GLY TYR GLN LEU LEU GLY
SEQRES 9 A 1213 GLU ILE ASN TYR ARG GLU CYS ASP THR ASP GLY TRP THR
SEQRES 10 A 1213 ASN ASP ILE PRO ILE CYS GLU VAL VAL LYS CYS LEU PRO
SEQRES 11 A 1213 VAL THR ALA PRO GLU ASN GLY LYS ILE VAL SER SER ALA
SEQRES 12 A 1213 MET GLU PRO ASP ARG GLU TYR HIS PHE GLY GLN ALA VAL
SEQRES 13 A 1213 ARG PHE VAL CYS ASN SER GLY TYR LYS ILE GLU GLY ASP
SEQRES 14 A 1213 GLU GLU MET HIS CYS SER ASP ASP GLY PHE TRP SER LYS
SEQRES 15 A 1213 GLU LYS PRO LYS CYS VAL GLU ILE SER CYS LYS SER PRO
SEQRES 16 A 1213 ASP VAL ILE ASN GLY SER PRO ILE SER GLN LYS ILE ILE
SEQRES 17 A 1213 TYR LYS GLU ASN GLU ARG PHE GLN TYR LYS CYS ASN MET
SEQRES 18 A 1213 GLY TYR GLU TYR SER GLU ARG GLY ASP ALA VAL CYS THR
SEQRES 19 A 1213 GLU SER GLY TRP ARG PRO LEU PRO SER CYS GLU GLU LYS
SEQRES 20 A 1213 SER CYS ASP ASN PRO TYR ILE PRO ASN GLY ASP TYR SER
SEQRES 21 A 1213 PRO LEU ARG ILE LYS HIS ARG THR GLY ASP GLU ILE THR
SEQRES 22 A 1213 TYR GLN CYS ARG ASN GLY PHE TYR PRO ALA THR ARG GLY
SEQRES 23 A 1213 ASN THR ALA LYS CYS THR SER THR GLY TRP ILE PRO ALA
SEQRES 24 A 1213 PRO ARG CYS THR LEU LYS PRO CYS ASP TYR PRO ASP ILE
SEQRES 25 A 1213 LYS HIS GLY GLY LEU TYR HIS GLU ASN MET ARG ARG PRO
SEQRES 26 A 1213 TYR PHE PRO VAL ALA VAL GLY LYS TYR TYR SER TYR TYR
SEQRES 27 A 1213 CYS ASP GLU HIS PHE GLU THR PRO SER GLY SER TYR TRP
SEQRES 28 A 1213 ASP HIS ILE HIS CYS THR GLN ASP GLY TRP SER PRO ALA
SEQRES 29 A 1213 VAL PRO CYS LEU ARG LYS CYS TYR PHE PRO TYR LEU GLU
SEQRES 30 A 1213 ASN GLY TYR ASN GLN ASN HIS GLY ARG LYS PHE VAL GLN
SEQRES 31 A 1213 GLY LYS SER ILE ASP VAL ALA CYS HIS PRO GLY TYR ALA
SEQRES 32 A 1213 LEU PRO LYS ALA GLN THR THR VAL THR CYS MET GLU ASN
SEQRES 33 A 1213 GLY TRP SER PRO THR PRO ARG CYS ILE ARG VAL LYS THR
SEQRES 34 A 1213 CYS SER LYS SER SER ILE ASP ILE GLU ASN GLY PHE ILE
SEQRES 35 A 1213 SER GLU SER GLN TYR THR TYR ALA LEU LYS GLU LYS ALA
SEQRES 36 A 1213 LYS TYR GLN CYS LYS LEU GLY TYR VAL THR ALA ASP GLY
SEQRES 37 A 1213 GLU THR SER GLY SER ILE THR CYS GLY LYS ASP GLY TRP
SEQRES 38 A 1213 SER ALA GLN PRO THR CYS ILE LYS SER CYS ASP ILE PRO
SEQRES 39 A 1213 VAL PHE MET ASN ALA ARG THR LYS ASN ASP PHE THR TRP
SEQRES 40 A 1213 PHE LYS LEU ASN ASP THR LEU ASP TYR GLU CYS HIS ASP
SEQRES 41 A 1213 GLY TYR GLU SER ASN THR GLY SER THR THR GLY SER ILE
SEQRES 42 A 1213 VAL CYS GLY TYR ASN GLY TRP SER ASP LEU PRO ILE CYS
SEQRES 43 A 1213 TYR GLU ARG GLU CYS GLU LEU PRO LYS ILE ASP VAL HIS
SEQRES 44 A 1213 LEU VAL PRO ASP ARG LYS LYS ASP GLN TYR LYS VAL GLY
SEQRES 45 A 1213 GLU VAL LEU LYS PHE SER CYS LYS PRO GLY PHE THR ILE
SEQRES 46 A 1213 VAL GLY PRO ASN SER VAL GLN CYS TYR HIS PHE GLY LEU
SEQRES 47 A 1213 SER PRO ASP LEU PRO ILE CYS LYS GLU GLN VAL GLN SER
SEQRES 48 A 1213 CYS GLY PRO PRO PRO GLU LEU LEU ASN GLY ASN VAL LYS
SEQRES 49 A 1213 GLU LYS THR LYS GLU GLU TYR GLY HIS SER GLU VAL VAL
SEQRES 50 A 1213 GLU TYR TYR CYS ASN PRO ARG PHE LEU MET LYS GLY PRO
SEQRES 51 A 1213 ASN LYS ILE GLN CYS VAL ASP GLY GLU TRP THR THR LEU
SEQRES 52 A 1213 PRO VAL CYS ILE VAL GLU GLU SER THR CYS GLY ASP ILE
SEQRES 53 A 1213 PRO GLU LEU GLU HIS GLY TRP ALA GLN LEU SER SER PRO
SEQRES 54 A 1213 PRO TYR TYR TYR GLY ASP SER VAL GLU PHE ASN CYS SER
SEQRES 55 A 1213 GLU SER PHE THR MET ILE GLY HIS ARG SER ILE THR CYS
SEQRES 56 A 1213 ILE HIS GLY VAL TRP THR GLN LEU PRO GLN CYS VAL ALA
SEQRES 57 A 1213 ILE ASP LYS LEU LYS LYS CYS LYS SER SER ASN LEU ILE
SEQRES 58 A 1213 ILE LEU GLU GLU HIS LEU LYS ASN LYS LYS GLU PHE ASP
SEQRES 59 A 1213 HIS ASN SER ASN ILE ARG TYR ARG CYS ARG GLY LYS GLU
SEQRES 60 A 1213 GLY TRP ILE HIS THR VAL CYS ILE ASN GLY ARG TRP ASP
SEQRES 61 A 1213 PRO GLU VAL ASN CYS SER MET ALA GLN ILE GLN LEU CYS
SEQRES 62 A 1213 PRO PRO PRO PRO GLN ILE PRO ASN SER HIS ASN MET THR
SEQRES 63 A 1213 THR THR LEU ASN TYR ARG ASP GLY GLU LYS VAL SER VAL
SEQRES 64 A 1213 LEU CYS GLN GLU ASN TYR LEU ILE GLN GLU GLY GLU GLU
SEQRES 65 A 1213 ILE THR CYS LYS ASP GLY ARG TRP GLN SER ILE PRO LEU
SEQRES 66 A 1213 CYS VAL GLU LYS ILE PRO CYS SER GLN PRO PRO GLN ILE
SEQRES 67 A 1213 GLU HIS GLY THR ILE ASN SER SER ARG SER SER GLN GLU
SEQRES 68 A 1213 SER TYR ALA HIS GLY THR LYS LEU SER TYR THR CYS GLU
SEQRES 69 A 1213 GLY GLY PHE ARG ILE SER GLU GLU ASN GLU THR THR CYS
SEQRES 70 A 1213 TYR MET GLY LYS TRP SER SER PRO PRO GLN CYS GLU GLY
SEQRES 71 A 1213 LEU PRO CYS LYS SER PRO PRO GLU ILE SER HIS GLY VAL
SEQRES 72 A 1213 VAL ALA HIS MET SER ASP SER TYR GLN TYR GLY GLU GLU
SEQRES 73 A 1213 VAL THR TYR LYS CYS PHE GLU GLY PHE GLY ILE ASP GLY
SEQRES 74 A 1213 PRO ALA ILE ALA LYS CYS LEU GLY GLU LYS TRP SER HIS
SEQRES 75 A 1213 PRO PRO SER CYS ILE LYS THR ASP CYS LEU SER LEU PRO
SEQRES 76 A 1213 SER PHE GLU ASN ALA ILE PRO MET GLY GLU LYS LYS ASP
SEQRES 77 A 1213 VAL TYR LYS ALA GLY GLU GLN VAL THR TYR THR CYS ALA
SEQRES 78 A 1213 THR TYR TYR LYS MET ASP GLY ALA SER ASN VAL THR CYS
SEQRES 79 A 1213 ILE ASN SER ARG TRP THR GLY ARG PRO THR CYS ARG ASP
SEQRES 80 A 1213 THR SER CYS VAL ASN PRO PRO THR VAL GLN ASN ALA TYR
SEQRES 81 A 1213 ILE VAL SER ARG GLN MET SER LYS TYR PRO SER GLY GLU
SEQRES 82 A 1213 ARG VAL ARG TYR GLN CYS ARG SER PRO TYR GLU MET PHE
SEQRES 83 A 1213 GLY ASP GLU GLU VAL MET CYS LEU ASN GLY ASN TRP THR
SEQRES 84 A 1213 GLU PRO PRO GLN CYS LYS ASP SER THR GLY LYS CYS GLY
SEQRES 85 A 1213 PRO PRO PRO PRO ILE ASP ASN GLY ASP ILE THR SER PHE
SEQRES 86 A 1213 PRO LEU SER VAL TYR ALA PRO ALA SER SER VAL GLU TYR
SEQRES 87 A 1213 GLN CYS GLN ASN LEU TYR GLN LEU GLU GLY ASN LYS ARG
SEQRES 88 A 1213 ILE THR CYS ARG ASN GLY GLN TRP SER GLU PRO PRO LYS
SEQRES 89 A 1213 CYS LEU HIS PRO CYS VAL ILE SER ARG GLU ILE MET GLU
SEQRES 90 A 1213 ASN TYR ASN ILE ALA LEU ARG TRP THR ALA LYS GLN LYS
SEQRES 91 A 1213 LEU TYR SER ARG THR GLY GLU SER VAL GLU PHE VAL CYS
SEQRES 92 A 1213 LYS ARG GLY TYR ARG LEU SER SER ARG SER HIS THR LEU
SEQRES 93 A 1213 ARG THR THR CYS TRP ASP GLY LYS LEU GLU TYR PRO THR
SEQRES 94 A 1213 CYS ALA LYS ARG
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
