HEADER EYE LENS PROTEIN 02-APR-92 4GCR COMPND GAMMA-B CRYSTALLIN (PREVIOUSLY GAMMA-II CRYSTALLIN) SOURCE CALF (BOS TAURUS) EYE LENS AUTHOR C.SLINGSBY,S.NAJMUDIN,V.NALINI,H.P.C.DRIESSEN,T.L.BLUNDELL, AUTHOR 2 D.S.MOSS,P.LINDLEY REVDAT 1 31-OCT-93 4GCR 0 SPRSDE 15-OCT-93 4CGR 1GCR JRNL AUTH S.NAJMUDIN,V.NALINI,H.P.C.DRIESSEN,C.SLINGSBY, JRNL AUTH 2 T.L.BLUNDELL,D.S.MOSS,P.F.LINDLEY JRNL TITL STRUCTURE OF THE BOVINE EYE LENS PROTEIN GAMMA-B JRNL TITL 2 (GAMMA-II)-CRYSTALLIN AT 1.47 ANGSTROMS JRNL REF TO BE PUBLISHED JRNL REFN 353 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.SUMMERS,G.WISTOW,M.NAREBOR,D.MOSS,P.LINDLEY, REMARK 1 AUTH 2 C.SLINGSBY,T.BLUNDELL,H.BARTUNIK,K.BARTELS REMARK 1 TITL X-RAY STUDIES OF THE LENS SPECIFIC PROTEINS, THE REMARK 1 TITL 2 CRYSTALLINS REMARK 1 REF PEPT.PROTEIN REV. V. 3 147 1984 REMARK 1 REFN ASTM PPRVDF US ISSN 0731-1753 882 REMARK 1 REFERENCE 2 REMARK 1 AUTH G.WISTOW,B.TURNELL,L.SUMMERS,C.SLINGSBY,D.MOSS, REMARK 1 AUTH 2 L.MILLER,P.LINDLEY,T.BLUNDELL REMARK 1 TITL GAMMA-II CRYSTALLIN AT 1.9 ANGSTROM RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 170 175 1983 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 3 REMARK 1 AUTH T.BLUNDELL,P.LINDLEY,L.MILLER,D.MOSS,C.SLINGSBY, REMARK 1 AUTH 2 I.TICKLE,B.TURNELL,G.WISTOW REMARK 1 TITL X-RAY ANALYSIS OF GAMMA CRYSTALLIN II REMARK 1 REF NATURE V. 289 771 1981 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 REMARK 2 REMARK 2 RESOLUTION. 1.47 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM RESTRAIN REMARK 3 AUTHORS HANEEF ET AL. REMARK 3 R VALUE 0.181 REMARK 3 RMSD BOND DISTANCES 0.022 ANGSTROMS REMARK 3 RMSD BOND ANGLE DISTANCES 0.038 ANGSTROMS REMARK 4 REMARK 4 THE SIDE CHAINS OF CYS 18 AND CYS 22 WERE REFINED WITH REMARK 4 COUPLED SECOND-SITE OCCUPANCIES. THE MAJOR SITE (60% REMARK 4 OCCUPANCY) FOR THE SULFUR ATOM OF CYS 22 IS IN THE REMARK 4 SULFHYDRYL FORM (I.E. REDUCED). THE MINOR SITE OF CYS 22 REMARK 4 CAN FORM A DISULFIDE BRIDGE WITH EITHER SITES (60% - 40%) REMARK 4 OF CYS 18. THE POSITIONS OF THE MINOR SITES OF THE SIDE REMARK 4 CHAINS OF CYS 18 AND CYS 22 ARE GIVEN AS CONFORMATION B IN REMARK 4 THE ATOM RECORDS. ALTERNATE CONFORMATIONS ARE GIVEN FOR REMARK 4 FOR ALL RESIDUES 15 - 25 BUT THEY ARE VIRTUALLY IDENTICAL REMARK 4 EXCEPT FOR CYS 18 AND CYS 22 WHICH HAVE THEIR SIDE CHAINS REMARK 4 IN THE ALTERNATIVE (MINOR) OCCUPANCY POSITIONS. REMARK 4 REMARK 4 ENTRY RESIDUE 119 IS A THR (AS IN CDNA SEQUENCE, BHAT AND REMARK 4 SPECTOR, DNA V. 3, 287-297 (1984) AND NOT SER AS IN 1GCR, REMARK 4 THE PREVIOUSLY DEPOSITED COORDINATE SET. REMARK 5 REMARK 5 THE QUANTITY GIVEN IN THE TEMPERATURE FACTOR COLUMN OF THE REMARK 5 ATOM AND HETATM RECORDS BELOW IS UISO (U**2), WHICH IS THE REMARK 5 MEAN-SQUARE AMPLITUDE VIBRATION. THE TEMPERATURE FACTOR, REMARK 5 B, CAN BE DERIVED BY THE RELATION: B = 8*(PI)**2*U**2. REMARK 6 REMARK 6 THERE IS A BETA-BRIDGE BETWEEN RESIDUES 119 - 121 AND REMARK 6 162 - 164. SEQRES 1 174 GLY LYS ILE THR PHE TYR GLU ASP ARG GLY PHE GLN GLY SEQRES 2 174 HIS CYS TYR GLU CYS SER SER ASP CYS PRO ASN LEU GLN SEQRES 3 174 PRO TYR PHE SER ARG CYS ASN SER ILE ARG VAL ASP SER SEQRES 4 174 GLY CYS TRP MET LEU TYR GLU ARG PRO ASN TYR GLN GLY SEQRES 5 174 HIS GLN TYR PHE LEU ARG ARG GLY ASP TYR PRO ASP TYR SEQRES 6 174 GLN GLN TRP MET GLY PHE ASN ASP SER ILE ARG SER CYS SEQRES 7 174 ARG LEU ILE PRO GLN HIS THR GLY THR PHE ARG MET ARG SEQRES 8 174 ILE TYR GLU ARG ASP ASP PHE ARG GLY GLN MET SER GLU SEQRES 9 174 ILE THR ASP ASP CYS PRO SER LEU GLN ASP ARG PHE HIS SEQRES 10 174 LEU THR GLU VAL HIS SER LEU ASN VAL LEU GLU GLY SER SEQRES 11 174 TRP VAL LEU TYR GLU MET PRO SER TYR ARG GLY ARG GLN SEQRES 12 174 TYR LEU LEU ARG PRO GLY GLU TYR ARG ARG TYR LEU ASP SEQRES 13 174 TRP GLY ALA MET ASN ALA LYS VAL GLY SER LEU ARG ARG SEQRES 14 174 VAL MET ASP PHE TYR FORMUL 2 HOH *230(H2 O1) HELIX 1 H1 TYR 65 TRP 68 5 HELIX 2 H2 LEU 112 PHE 116 1 HELIX 3 H3 TYR 154 TRP 157 5 SHEET 1 S1 4 HIS 14 CYS 18 0 SHEET 2 S1 4 LYS 2 GLU 7 -1 N ILE 3 O CYS 18 SHEET 3 S1 4 SER 34 SER 39 -1 O SER 39 N LYS 2 SHEET 4 S1 4 GLY 60 TYR 62 -1 N GLY 60 O VAL 37 SHEET 1 S2 4 ASP 21 PRO 23 0 SHEET 2 S2 4 SER 77 ILE 81 -1 N CYS 78 O CYS 22 SHEET 3 S2 4 CYS 41 GLU 46 -1 N MET 43 O ARG 79 SHEET 4 S2 4 HIS 53 LEU 57 -1 N LEU 57 O TRP 42 SHEET 1 S3 4 GLN 101 ILE 105 0 SHEET 2 S3 4 ARG 89 GLU 94 -1 N MET 90 O ILE 105 SHEET 3 S3 4 SER 123 GLU 128 -1 N ASN 125 O ARG 91 SHEET 4 S3 4 GLY 149 TYR 151 -1 N GLY 149 O VAL 126 SHEET 1 S4 4 ASP 108 PRO 110 0 SHEET 2 S4 4 SER 166 VAL 170 -1 N LEU 167 O CYS 109 SHEET 3 S4 4 SER 130 GLU 135 -1 N VAL 132 O ARG 168 SHEET 4 S4 4 ARG 142 LEU 146 -1 N TYR 144 O LEU 133 CRYST1 57.530 57.530 97.950 90.00 90.00 90.00 P 41 21 2 8 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 0.017382 0.000000 0.000000 0.00000 SCALE2 0.000000 0.017382 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010209 0.00000