HEADER HORMONE 22-SEP-93 1HUW 1HUW 2 COMPND HUMAN GROWTH HORMONE MUTANT WITH PHE 10 REPLACED BY ALA, 1HUW 3 COMPND 2 MET 14 REPLACED BY TRP, HIS 18 REPLACED BY ASP, HIS 21 1HUW 4 COMPND 3 REPLACED BY ASN, LYS 41 REPLACED BY ILE, TYR 42 REPLACED BY 1HUW 5 COMPND 4 HIS, LEU 45 REPLACED BY TRP, GLN 46 REPLACED BY TRP, PHE 54 1HUW 6 COMPND 5 REPLACED BY PRO, ARG 64 REPLACED BY LYS, ARG 167 REPLACED 1HUW 7 COMPND 6 ASN, ASP 171 REPLACED BY SER, GLU 174 REPLACED BY SER, 1HUW 8 COMPND 7 PHE 176 REPLACED BY TYR, ILE 179 REPLACED BY THR (F10A, 1HUW 9 COMPND 8 M14W,H18D,H21N,K41I,Y42H,L45W,Q46W,F54P,R64K,R167N,D171S, 1HUW 10 COMPND 9 E174S,F176Y,I179T) 1HUW 11 SOURCE HUMAN (HOMO SAPIENS) RECOMBINANT FORM EXPRESSED IN 1HUW 12 SOURCE 2 (ESCHERICHIA COLI) 1HUW 13 AUTHOR M.H.ULTSCH,W.S.SOMERS,A.A.KOSSIAKOFF,A.M.DE VOS 1HUW 14 REVDAT 1 31-JAN-94 1HUW 0 1HUW 15 JRNL AUTH M.H.ULTSCH,W.S.SOMERS,A.A.KOSSIAKOFF,A.M.DE VOS 1HUW 16 JRNL TITL THE CRYSTAL STRUCTURE OF AFFINITY-MATURED HUMAN 1HUW 17 JRNL TITL 2 GROWTH HORMONE AT 2 ANGSTROMS RESOLUTION 1HUW 18 JRNL REF TO BE PUBLISHED 1HUW 19 JRNL REFN 353 1HUW 20 REMARK 1 1HUW 21 REMARK 1 REFERENCE 1 1HUW 22 REMARK 1 AUTH H.B.LOWMAN,J.A.WELLS 1HUW 23 REMARK 1 TITL AFFINITY MATURATION OF HUMAN GROWTH HORMONE BY 1HUW 24 REMARK 1 TITL 2 MONOVALENT PHAGE DISPLAY 1HUW 25 REMARK 1 REF TO BE PUBLISHED 1HUW 26 REMARK 1 REFN 353 1HUW 27 REMARK 2 1HUW 28 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 1HUW 29 REMARK 3 1HUW 30 REMARK 3 REFINEMENT. 1HUW 31 REMARK 3 PROGRAM X-PLOR 1HUW 32 REMARK 3 AUTHORS BRUNGER 1HUW 33 REMARK 3 R VALUE 0.185 1HUW 34 REMARK 3 RMSD BOND DISTANCES 0.012 ANGSTROMS 1HUW 35 REMARK 3 RMSD BOND ANGLES 2.63 DEGREES 1HUW 36 REMARK 3 1HUW 37 REMARK 3 RESOLUTION RANGE 8.0 - 2.0 ANGSTROMS 1HUW 38 REMARK 3 DATA CUTOFF 2.0 SIGMA(F) 1HUW 39 REMARK 3 1HUW 40 REMARK 3 NUMBER OF PROTEIN ATOMS 1361 1HUW 41 REMARK 3 NUMBER OF SOLVENT ATOMS 77 1HUW 42 REMARK 4 1HUW 43 REMARK 4 RESIDUES 130 - 154 ARE DISORDERED AND NOT INCLUDED IN THE 1HUW 44 REMARK 4 MODEL. 1HUW 45 REMARK 5 1HUW 46 REMARK 5 THE SIDE CHAINS OF GLN 29, GLU 39, AND ASP 116 ARE MODELLED 1HUW 47 REMARK 5 IN TWO CONFORMATIONS. 1HUW 48 SEQRES 1 166 PHE PRO THR ILE PRO LEU SER ARG LEU ALA ASP ASN ALA 1HUW 49 SEQRES 2 166 TRP LEU ARG ALA ASP ARG LEU ASN GLN LEU ALA PHE ASP 1HUW 50 SEQRES 3 166 THR TYR GLN GLU PHE GLU GLU ALA TYR ILE PRO LYS GLU 1HUW 51 SEQRES 4 166 GLN ILE HIS SER PHE TRP TRP ASN PRO GLN THR SER LEU 1HUW 52 SEQRES 5 166 CYS PRO SER GLU SER ILE PRO THR PRO SER ASN LYS GLU 1HUW 53 SEQRES 6 166 GLU THR GLN GLN LYS SER ASN LEU GLU LEU LEU ARG ILE 1HUW 54 SEQRES 7 166 SER LEU LEU LEU ILE GLN SER TRP LEU GLU PRO VAL GLN 1HUW 55 SEQRES 8 166 PHE LEU ARG SER VAL PHE ALA ASN SER LEU VAL TYR GLY 1HUW 56 SEQRES 9 166 ALA SER ASP SER ASN VAL TYR ASP LEU LEU LYS ASP LEU 1HUW 57 SEQRES 10 166 GLU GLU GLY ILE GLN THR LEU MET GLY ARG LEU GLU ALA 1HUW 58 SEQRES 11 166 LEU LEU LYS ASN TYR GLY LEU LEU TYR CYS PHE ASN LYS 1HUW 59 SEQRES 12 166 ASP MET SER LYS VAL SER THR TYR LEU ARG THR VAL GLN 1HUW 60 SEQRES 13 166 CYS ARG SER VAL GLU GLY SER CYS GLY PHE 1HUW 61 FORMUL 2 HOH *77(H2 O1) 1HUW 62 HELIX 1 A LEU 6 TYR 35 1 1HUW 63 HELIX 2 B LYS 38 TRP 46 1 1HUW 64 HELIX 3 C LYS 64 GLN 69 1 1HUW 65 HELIX 4 D ASN 72 PHE 92 1 1HUW 66 HELIX 5 E ARG 94 SER 100 1 1HUW 67 HELIX 6 F TYR 111 LEU 128 1 1HUW 68 HELIX 7 G ALA 155 SER 184 1 1HUW 69 SSBOND 1 CYS 53 CYS 165 1HUW 70 SSBOND 2 CYS 182 CYS 189 1HUW 71 CRYST1 80.450 59.340 50.870 90.00 128.20 90.00 C 2 4 1HUW 72 ORIGX1 1.000000 0.000000 0.000000 0.00000 1HUW 73 ORIGX2 0.000000 1.000000 0.000000 0.00000 1HUW 74 ORIGX3 0.000000 0.000000 1.000000 0.00000 1HUW 75 SCALE1 0.012430 0.000000 0.009782 0.00000 1HUW 76 SCALE2 0.000000 0.016852 0.000000 0.00000 1HUW 77 SCALE3 0.000000 0.000000 0.025015 0.00000 1HUW 78