HEADER NUCLEAR RECEPTOR 19-AUG-97 2LBD TITLE LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR TITLE 2 GAMMA BOUND TO ALL-TRANS RETINOIC ACID COMPND MOL_ID: 1; COMPND 2 MOLECULE: RETINOIC ACID RECEPTOR GAMMA; COMPND 3 CHAIN: NULL; COMPND 4 FRAGMENT: LBD (LIGAND-BINDING DOMAIN), RESIDUES 178 - 423; COMPND 5 SYNONYM: E DOMAIN; COMPND 6 ENGINEERED: YES; COMPND 7 BIOLOGICAL_UNIT: RAR-RXR HETERODIMER SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 CELLULAR_LOCATION: NUCLEUS; SOURCE 5 GENE: HUMAN RAR GAMMA A CDNA (NUCLEOTIDES 946 - 1683); SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-15B; SOURCE 11 EXPRESSION_SYSTEM_GENE: HRARGAMMA; SOURCE 12 OTHER_DETAILS: CDNA CLONING\: KRUST ET AL., SOURCE 13 PROC.NATL.ACAD.SCI.USA,86,5310-5314,1989 KEYWDS NUCLEAR RECEPTOR, RETINOIC ACID RECEPTOR, ALL-TRANS KEYWDS 2 RETINOIC ACID, LIGAND-BINDING DOMAIN, COMPLEX, HOLO FORM, KEYWDS 3 TRANSCRIPTION REGULATION, LIGAND-DEPENDENT, ACTIVE KEYWDS 4 CONFORMATION EXPDTA X-RAY DIFFRACTION AUTHOR J.-P.RENAUD,N.ROCHEL,M.RUFF,D.MORAS REVDAT 1 12-NOV-97 2LBD 0 JRNL AUTH J.P.RENAUD,N.ROCHEL,M.RUFF,V.VIVAT,P.CHAMBON, JRNL AUTH 2 H.GRONEMEYER,D.MORAS JRNL TITL CRYSTAL STRUCTURE OF THE RAR-GAMMA LIGAND-BINDING JRNL TITL 2 DOMAIN BOUND TO ALL-TRANS RETINOIC ACID JRNL REF NATURE V. 378 681 1995 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 0006 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH W.BOURGUET,M.RUFF,P.CHAMBON,H.GRONEMEYER,D.MORAS REMARK 1 TITL CRYSTAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF REMARK 1 TITL 2 THE HUMAN NUCLEAR RECEPTOR RXR-ALPHA REMARK 1 REF NATURE V. 375 377 1995 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 REMARK 2 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86. REMARK 3 NUMBER OF REFLECTIONS : 15632 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM (FREERFLAG, REMARK 3 CCP4) REMARK 3 R VALUE (WORKING SET) : 0.210 REMARK 3 FREE R VALUE : 0.313 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.0 REMARK 3 FREE R VALUE TEST SET COUNT : 1 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1870 REMARK 3 NUCLEIC ACID ATOMS : NULL REMARK 3 HETEROGEN ATOMS : 22 REMARK 3 SOLVENT ATOMS : 119 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.2 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.013 REMARK 3 BOND ANGLES (DEGREES) : 1.67 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.6 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.57 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : PARAM19.SOL REMARK 3 PARAMETER FILE 3 : ATRA.PAR REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : TOPH19.PEP REMARK 3 TOPOLOGY FILE 3 : TOPH19.SOL REMARK 3 TOPOLOGY FILE 4 : ATRA.TOP REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2LBD COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996 REMARK 6 REMARK 6 THE FULL RAR NUCLEAR RECEPTOR CONTAINS SIX DOMAINS NAMED REMARK 6 A - F, C BEING THE DNA-BINDING DOMAIN (DBD) AND E THE REMARK 6 LIGAND-BINDING DOMAIN (LBD). REMARK 7 REMARK 7 THE RAR FRAGMENT CRYSTALLIZED HERE CONTAINS THE LBD REMARK 7 (RESIDUES 178 - 423) PLUS A 21-RESIDUE N-TERMINAL REMARK 7 HISTIDINE TAG ADDED FOR THE PURIFICATION. REMARK 8 REMARK 8 THE PRESENT PDB ENTRY CONTAINS ONLY THE COORDINATES FOR REMARK 8 RESIDUES 182 - 419 BECAUSE THE OTHER RESIDUES WERE NOT REMARK 8 SEEN. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : SEP-1994 REMARK 200 TEMPERATURE (KELVIN) : 268 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 3 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : LURE REMARK 200 BEAMLINE : W32 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.901 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MARXDS REMARK 200 DATA SCALING SOFTWARE : MARSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17193 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.06 REMARK 200 RESOLUTION RANGE LOW (A) : 7.99 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.08 REMARK 200 DATA REDUNDANCY : 3.77 REMARK 200 R MERGE (I) : 0.0974 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.80 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10 REMARK 200 COMPLETENESS FOR SHELL (%) : 57.5 REMARK 200 DATA REDUNDANCY IN SHELL : 1.9 REMARK 200 R MERGE FOR SHELL (I) : 0.3323 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.64 REMARK 200 REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIR REMARK 200 SOFTWARE USED: MLPHARE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 33. REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.364 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION METHOD, HANGING REMARK 280 DROP TECHNIQUE 5UL PROTEIN SOLUTION + 5UL RESERVOIR REMARK 280 AGAINST 500UL RESERVOIR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 1/2-Y,1/2+X,1/4+Z REMARK 290 4555 1/2+Y,1/2-X,3/4+Z REMARK 290 5555 1/2-X,1/2+Y,1/4-Z REMARK 290 6555 1/2+X,1/2-Y,3/4-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,1/2-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.65181 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.29936 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.29936 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 38.82590 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.29936 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.29936 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 116.47771 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.29936 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.29936 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 38.82590 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.29936 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.29936 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 116.47771 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 77.65181 REMARK 290 REMARK 290 REMARK: NULL REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN 185 CG CD OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. SOME OF THESE MAY BE ATOMS REMARK 500 LOCATED ON SPECIAL POSITIONS IN THE CELL. ATOMS WITH REMARK 500 NON-BLANK ALTERNATE LOCATION INDICATORS ARE NOT INCLUDED REMARK 500 IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 2H HOH 542 1HH1 ARG 366 5656 1.58 REMARK 500 2HH1 ARG 296 2H HOH 502 4554 1.58 REMARK 500 2H HOH 529 HG1 THR 191 4554 1.59 REMARK 550 REMARK 550 SEGID REMARK 550 ALT1 AND ALT2 REFER TO THE ALTERNATE POSITIONS OF LYS 236 REMARK 550 AND HOH 581. REMARK 650 REMARK 650 HELIX REMARK 650 HELIX_ID: H3,H2 SKIPPED TO FIT RXR LBD NUMBERING. REMARK 650 HELIX_ID: H7,BEGINS AND ENDS WITH 1 TURN OF 3/10. REMARK 999 REMARK 999 SEQUENCE REMARK 999 2LBD SWS P22932 1 - 170 NOT IN ATOMS LIST REMARK 999 2LBD SWS P22932 409 - 443 NOT IN ATOMS LIST DBREF 2LBD 182 419 SWS P22932 RRG2_HUMAN 171 408 SEQRES 1 267 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 267 LEU VAL PRO ARG GLY SER HIS MET ASP SER TYR GLU LEU SEQRES 3 267 SER PRO GLN LEU GLU GLU LEU ILE THR LYS VAL SER LYS SEQRES 4 267 ALA HIS GLN GLU THR PHE PRO SER LEU CYS GLN LEU GLY SEQRES 5 267 LYS TYR THR THR ASN SER SER ALA ASP HIS ARG VAL GLN SEQRES 6 267 LEU ASP LEU GLY LEU TRP ASP LYS PHE SER GLU LEU ALA SEQRES 7 267 THR LYS CYS ILE ILE LYS ILE VAL GLU PHE ALA LYS ARG SEQRES 8 267 LEU PRO GLY PHE THR GLY LEU SER ILE ALA ASP GLN ILE SEQRES 9 267 THR LEU LEU LYS ALA ALA CYS LEU ASP ILE LEU MET LEU SEQRES 10 267 ARG ILE CYS THR ARG TYR THR PRO GLU GLN ASP THR MET SEQRES 11 267 THR PHE SER ASP GLY LEU THR LEU ASN ARG THR GLN MET SEQRES 12 267 HIS ASN ALA GLY PHE GLY PRO LEU THR ASP LEU VAL PHE SEQRES 13 267 ALA PHE ALA GLY GLN LEU LEU PRO LEU GLU MET ASP ASP SEQRES 14 267 THR GLU THR GLY LEU LEU SER ALA ILE CYS LEU ILE CYS SEQRES 15 267 GLY ASP ARG MET ASP LEU GLU GLU PRO GLU LYS VAL ASP SEQRES 16 267 LYS LEU GLN GLU PRO LEU LEU GLU ALA LEU ARG LEU TYR SEQRES 17 267 ALA ARG ARG ARG ARG PRO SER GLN PRO TYR MET PHE PRO SEQRES 18 267 ARG MET LEU MET LYS ILE THR ASP LEU ARG GLY ILE SER SEQRES 19 267 THR LYS GLY ALA GLU ARG ALA ILE THR LEU LYS MET GLU SEQRES 20 267 ILE PRO GLY PRO MET PRO PRO LEU ILE ARG GLU MET LEU SEQRES 21 267 GLU ASN PRO GLU MET PHE GLU HET REA 500 22 HETNAM REA RETINOIC ACID FORMUL 2 REA C20 H28 O2 FORMUL 3 HOH *120(H2 O1) HELIX 1 H1 SER 183 THR 200 1 18 HELIX 2 H3 LEU 224 ARG 247 1 SEE REMARK 650 24 HELIX 3 H4 ILE 256 ALA 265 1 10 HELIX 4 H5 ALA 266 ARG 278 1 KINK BETWEEN A265 AND A266 13 HELIX 5 H6 ARG 296 ASN 301 1 6 HELIX 6 H7 GLY 305 LEU 321 1 SEE REMARK 650 17 HELIX 7 H8 ASP 325 LEU 336 1 12 HELIX 8 H9 PRO 347 ARG 368 1 22 HELIX 9 H10 MET 375 LYS 392 1 18 HELIX 10 H11 GLY 393 GLU 403 1 KINK BETWEEN K392 AND E403 11 HELIX 11 H12 PRO 410 MET 415 1 6 SHEET 1 A 2 THR 285 THR 287 0 SHEET 2 A 2 THR 293 ASN 295 -1 N LEU 294 O MET 286 CRYST1 60.600 60.600 155.300 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 0.016502 0.000000 0.000000 0.00000 SCALE2 0.000000 0.016502 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006439 0.00000 ATOM 992 N ASP 284 24.755 8.506 78.568 1.00 23.29 N ATOM 993 CA ASP 284 26.157 8.245 78.260 1.00 20.93 C ATOM 994 C ASP 284 26.929 9.561 78.358 1.00 19.57 C ATOM 995 O ASP 284 27.639 9.962 77.422 1.00 17.45 O ATOM 996 CB ASP 284 26.327 7.650 76.869 1.00 21.51 C ATOM 997 CG ASP 284 27.672 6.979 76.688 1.00 20.88 C ATOM 998 OD1 ASP 284 28.087 6.194 77.580 1.00 18.48 O ATOM 999 OD2 ASP 284 28.290 7.212 75.630 1.00 20.71 O ATOM 1000 H ASP 284 24.352 7.979 79.282 1.00 10.73 H ATOM 1001 N THR 285 26.750 10.236 79.492 1.00 19.17 N ATOM 1002 CA THR 285 27.408 11.505 79.759 1.00 18.19 C ATOM 1003 C THR 285 28.125 11.512 81.107 1.00 17.40 C ATOM 1004 O THR 285 27.958 10.599 81.917 1.00 16.90 O ATOM 1005 CB THR 285 26.389 12.681 79.804 1.00 18.36 C ATOM 1006 OG1 THR 285 25.414 12.437 80.830 1.00 17.95 O ATOM 1007 CG2 THR 285 25.716 12.891 78.448 1.00 16.08 C ATOM 1008 H THR 285 26.162 9.871 80.182 1.00 15.55 H ATOM 1009 HG1 THR 285 25.803 12.506 81.713 1.00 13.15 H ATOM 1010 N MET 286 28.926 12.556 81.312 1.00 17.39 N ATOM 1011 CA MET 286 29.655 12.816 82.550 1.00 17.47 C ATOM 1012 C MET 286 29.475 14.316 82.837 1.00 17.11 C ATOM 1013 O MET 286 29.506 15.159 81.924 1.00 16.22 O ATOM 1014 CB MET 286 31.149 12.446 82.443 1.00 16.08 C ATOM 1015 CG MET 286 31.393 10.940 82.406 1.00 15.31 C ATOM 1016 SD MET 286 33.122 10.507 82.292 1.00 21.84 S ATOM 1017 CE MET 286 32.978 8.817 82.523 1.00 13.72 C ATOM 1018 H MET 286 29.052 13.210 80.585 1.00 15.99 H ATOM 1019 N THR 287 29.225 14.631 84.101 1.00 15.98 N ATOM 1020 CA THR 287 28.996 16.000 84.538 1.00 15.63 C ATOM 1021 C THR 287 30.119 16.489 85.459 1.00 15.17 C ATOM 1022 O THR 287 30.560 15.778 86.352 1.00 14.62 O ATOM 1023 CB THR 287 27.633 16.077 85.245 1.00 14.95 C ATOM 1024 OG1 THR 287 26.645 15.597 84.336 1.00 16.07 O ATOM 1025 CG2 THR 287 27.279 17.506 85.659 1.00 14.81 C ATOM 1026 H THR 287 29.197 13.924 84.777 1.00 16.24 H ATOM 1027 HG1 THR 287 26.449 16.309 83.702 1.00 15.36 H ATOM 1028 N PHE 288 30.633 17.675 85.157 1.00 15.64 N ATOM 1029 CA PHE 288 31.700 18.299 85.922 1.00 16.95 C ATOM 1030 C PHE 288 31.040 19.093 87.044 1.00 18.22 C ATOM 1031 O PHE 288 29.814 19.219 87.063 1.00 17.92 O ATOM 1032 CB PHE 288 32.533 19.204 85.005 1.00 16.87 C ATOM 1033 CG PHE 288 33.288 18.451 83.947 1.00 16.91 C ATOM 1034 CD1 PHE 288 32.629 17.932 82.835 1.00 18.03 C ATOM 1035 CD2 PHE 288 34.645 18.205 84.087 1.00 15.86 C ATOM 1036 CE1 PHE 288 33.315 17.178 81.900 1.00 15.63 C ATOM 1037 CE2 PHE 288 35.329 17.456 83.151 1.00 13.84 C ATOM 1038 CZ PHE 288 34.671 16.944 82.066 1.00 13.79 C ATOM 1039 H PHE 288 30.266 18.145 84.380 1.00 14.20 H ATOM 1040 N SER 289 31.836 19.673 87.941 1.00 18.84 N ATOM 1041 CA SER 289 31.314 20.409 89.090 1.00 18.84 C ATOM 1042 C SER 289 30.528 21.682 88.883 1.00 19.48 C ATOM 1043 O SER 289 29.937 22.185 89.828 1.00 21.03 O ATOM 1044 CB SER 289 32.413 20.653 90.086 1.00 18.32 C ATOM 1045 OG SER 289 32.944 19.408 90.460 1.00 20.62 O ATOM 1046 H SER 289 32.775 19.612 87.835 1.00 19.01 H ATOM 1047 HG SER 289 33.624 19.163 89.796 1.00 14.08 H ATOM 1048 N ASP 290 30.544 22.243 87.680 1.00 18.56 N ATOM 1049 CA ASP 290 29.751 23.433 87.443 1.00 16.64 C ATOM 1050 C ASP 290 28.396 23.055 86.781 1.00 16.67 C ATOM 1051 O ASP 290 27.492 23.889 86.648 1.00 16.11 O ATOM 1052 CB ASP 290 30.547 24.465 86.627 1.00 19.14 C ATOM 1053 CG ASP 290 30.679 24.105 85.162 1.00 17.90 C ATOM 1054 OD1 ASP 290 30.715 22.918 84.812 1.00 19.78 O ATOM 1055 OD2 ASP 290 30.765 25.038 84.360 1.00 17.99 O ATOM 1056 H ASP 290 31.098 21.861 86.974 1.00 13.42 H ATOM 1057 N GLY 291 28.238 21.776 86.457 1.00 14.39 N ATOM 1058 CA GLY 291 27.019 21.308 85.824 1.00 14.41 C ATOM 1059 C GLY 291 27.269 20.966 84.370 1.00 15.52 C ATOM 1060 O GLY 291 26.444 20.301 83.757 1.00 16.88 O ATOM 1061 H GLY 291 28.927 21.116 86.668 1.00 13.33 H ATOM 1062 N LEU 292 28.395 21.404 83.807 1.00 13.32 N ATOM 1063 CA LEU 292 28.688 21.088 82.422 1.00 14.58 C ATOM 1064 C LEU 292 28.621 19.576 82.222 1.00 13.88 C ATOM 1065 O LEU 292 29.338 18.846 82.859 1.00 15.24 O ATOM 1066 CB LEU 292 30.068 21.628 81.997 1.00 14.51 C ATOM 1067 CG LEU 292 30.475 21.321 80.540 1.00 14.16 C ATOM 1068 CD1 LEU 292 29.472 21.911 79.585 1.00 12.49 C ATOM 1069 CD2 LEU 292 31.888 21.799 80.233 1.00 10.42 C ATOM 1070 H LEU 292 28.996 21.954 84.328 1.00 10.72 H ATOM 1071 N THR 293 27.707 19.133 81.366 1.00 14.29 N ATOM 1072 CA THR 293 27.479 17.731 81.046 1.00 14.37 C ATOM 1073 C THR 293 27.884 17.475 79.598 1.00 14.38 C ATOM 1074 O THR 293 27.279 18.018 78.688 1.00 14.25 O ATOM 1075 CB THR 293 25.987 17.447 81.193 1.00 16.10 C ATOM 1076 OG1 THR 293 25.593 17.820 82.519 1.00 16.90 O ATOM 1077 CG2 THR 293 25.673 15.984 80.943 1.00 14.68 C ATOM 1078 H THR 293 27.141 19.784 80.904 1.00 12.95 H ATOM 1079 HG1 THR 293 25.829 18.749 82.679 1.00 15.83 H ATOM 1080 N LEU 294 28.914 16.670 79.377 1.00 14.86 N ATOM 1081 CA LEU 294 29.371 16.379 78.022 1.00 15.36 C ATOM 1082 C LEU 294 29.101 14.933 77.666 1.00 16.14 C ATOM 1083 O LEU 294 29.201 14.058 78.514 1.00 17.38 O ATOM 1084 CB LEU 294 30.869 16.623 77.910 1.00 11.39 C ATOM 1085 CG LEU 294 31.373 18.005 78.324 1.00 14.10 C ATOM 1086 CD1 LEU 294 32.895 18.090 78.164 1.00 12.89 C ATOM 1087 CD2 LEU 294 30.717 19.077 77.479 1.00 10.35 C ATOM 1088 H LEU 294 29.370 16.237 80.132 1.00 16.14 H ATOM 1089 N ASN 295 28.715 14.666 76.429 1.00 17.13 N ATOM 1090 CA ASN 295 28.501 13.274 76.032 1.00 17.00 C ATOM 1091 C ASN 295 29.856 12.635 75.750 1.00 15.70 C ATOM 1092 O ASN 295 30.888 13.297 75.871 1.00 16.12 O ATOM 1093 CB ASN 295 27.553 13.151 74.835 1.00 18.00 C ATOM 1094 CG ASN 295 28.085 13.805 73.572 1.00 18.40 C ATOM 1095 OD1 ASN 295 29.276 14.030 73.414 1.00 19.72 O ATOM 1096 ND2 ASN 295 27.184 14.099 72.654 1.00 21.69 N ATOM 1097 H ASN 295 28.612 15.405 75.791 1.00 17.64 H ATOM 1098 1HD2 ASN 295 27.491 14.505 71.817 1.00 16.84 H ATOM 1099 2HD2 ASN 295 26.240 13.898 72.833 1.00 16.48 H CONECT 2290 2291 2295 2305 2306 CONECT 2291 2290 2292 CONECT 2292 2291 2293 CONECT 2293 2292 2294 CONECT 2294 2293 2295 2307 CONECT 2295 2290 2294 2296 CONECT 2296 2295 2297 CONECT 2297 2296 2298 CONECT 2298 2297 2299 2308 CONECT 2299 2298 2300 CONECT 2300 2299 2301 CONECT 2301 2300 2302 CONECT 2302 2301 2303 2309 CONECT 2303 2302 2304 CONECT 2304 2303 2310 2311 CONECT 2305 2290 CONECT 2306 2290 CONECT 2307 2294 CONECT 2308 2298 CONECT 2309 2302 CONECT 2310 2304 CONECT 2311 2304 MASTER 255 0 1 11 2 0 0 6 2670 1 22 21 END .