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HEADER HORMONE/GROWTH FACTOR/MEMBRANE PROTEIN 22-FEB-04 1SG1 TITLE CRYSTAL STRUCTURE OF THE RECEPTOR-LIGAND COMPLEX BETWEEN TITLE 2 NERVE GROWTH FACTOR AND THE COMMON NEUROTROPHIN RECEPTOR TITLE 3 P75 COMPND MOL_ID: 1; COMPND 2 MOLECULE: BETA-NERVE GROWTH FACTOR; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: BETA-NGF; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY COMPND 8 MEMBER 16; COMPND 9 CHAIN: X; COMPND 10 SYNONYM: LOW- AFFINITY NERVE GROWTH FACTOR RECEPTOR, NGF COMPND 11 RECEPTOR, GP80-LNGFR, P75 ICD, LOW AFFINITY NEUROTROPHIN COMPND 12 RECEPTOR P75NTR; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: NGFB; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 10 ORGANISM_COMMON: RAT; SOURCE 11 GENE: P75; SOURCE 12 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS; SOURCE 13 EXPRESSION_SYSTEM_STRAIN: TN5; SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PACGP67A KEYWDS NERVE GROWTH FACTOR, NGF, P75, NEUROTROPHIN, COMMON KEYWDS 2 NEUROTROPHIN RECEPTOR, CRYSTAL STRUCTURE, GROWTH FACTOR KEYWDS 3 RECEPTOR, RECEPTOR/LIGAND COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR X.L.HE,K.C.GARCIA REVDAT 2 12-APR-05 1SG1 1 JRNL REVDAT 1 01-JUN-04 1SG1 0 JRNL AUTH X.L.HE,K.C.GARCIA JRNL TITL STRUCTURE OF NERVE GROWTH FACTOR COMPLEXED WITH JRNL TITL 2 THE SHARED NEUROTROPHIN RECEPTOR P75 JRNL REF SCIENCE V. 304 870 2004 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 16891 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 REMARK 3 R VALUE (WORKING SET) : 0.243 REMARK 3 FREE R VALUE : 0.269 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 803 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) : 2.40 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.30 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.4000 REMARK 3 BIN FREE R VALUE : 0.4110 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 85 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 : 2763 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 1 REMARK 3 SOLVENT ATOMS : 375 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 45.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.40 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) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.50 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.70 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.80 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : 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 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1SG1 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB021679. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-OCT-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.30 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0597 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16891 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 4.800 REMARK 200 R MERGE (I) : 0.08300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3 REMARK 200 DATA REDUNDANCY IN SHELL : 4.70 REMARK 200 R MERGE FOR SHELL (I) : 0.34900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR REMARK 200 SOFTWARE USED: SOLVE REMARK 200 STARTING MODEL: PART OF THE STRUCTURE STARTS FROM PDB ENTRY 1WWW REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1000, ISOPROPONAL, SODIUM REMARK 280 CHLORIDE, CITRATE, PH 6.3, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-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 24.84600 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.00500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.89800 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.00500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.84600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.89800 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: A, B, X 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 1 REMARK 465 SER A 2 REMARK 465 SER A 3 REMARK 465 HIS A 4 REMARK 465 PRO A 5 REMARK 465 ILE A 6 REMARK 465 PHE A 7 REMARK 465 HIS A 8 REMARK 465 ARG A 9 REMARK 465 GLY A 10 REMARK 465 PRO A 61 REMARK 465 ASN A 62 REMARK 465 PRO A 63 REMARK 465 VAL A 64 REMARK 465 ASP A 65 REMARK 465 SER A 66 REMARK 465 ALA A 116 REMARK 465 VAL A 117 REMARK 465 ARG A 118 REMARK 465 ARG A 119 REMARK 465 ALA A 120 REMARK 465 SER B 1 REMARK 465 SER B 2 REMARK 465 SER B 3 REMARK 465 HIS B 4 REMARK 465 PRO B 5 REMARK 465 ILE B 6 REMARK 465 PHE B 7 REMARK 465 HIS B 8 REMARK 465 PRO B 61 REMARK 465 ASN B 62 REMARK 465 PRO B 63 REMARK 465 VAL B 64 REMARK 465 ASP B 65 REMARK 465 SER B 66 REMARK 465 VAL B 117 REMARK 465 ARG B 118 REMARK 465 ARG B 119 REMARK 465 ALA B 120 REMARK 465 LYS X 1 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASN A 77 N - CA - C ANGL. DEV. =-12.3 DEGREES REMARK 500 GLY B 94 N - CA - C ANGL. DEV. =-10.4 DEGREES REMARK 500 GLN X 33 N - CA - C ANGL. DEV. = 9.4 DEGREES REMARK 500 GLU X 89 N - CA - C ANGL. DEV. = 9.8 DEGREES REMARK 500 GLY X 105 N - CA - C ANGL. DEV. = 10.0 DEGREES REMARK 500 GLU X 120 N - CA - C ANGL. DEV. =-13.3 DEGREES REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP X 112 -102.08 34.33 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 26 DISTANCE = 5.51 ANGSTROMS REMARK 525 HOH 33 DISTANCE = 6.86 ANGSTROMS REMARK 525 HOH 54 DISTANCE = 5.44 ANGSTROMS REMARK 525 HOH 57 DISTANCE = 5.43 ANGSTROMS REMARK 525 HOH 88 DISTANCE = 5.02 ANGSTROMS REMARK 525 HOH 94 DISTANCE = 5.15 ANGSTROMS REMARK 525 HOH 121 DISTANCE = 6.43 ANGSTROMS REMARK 525 HOH 129 DISTANCE = 6.98 ANGSTROMS REMARK 525 HOH 133 DISTANCE = 7.23 ANGSTROMS REMARK 525 HOH 150 DISTANCE = 5.13 ANGSTROMS REMARK 525 HOH 163 DISTANCE = 5.65 ANGSTROMS REMARK 525 HOH 171 DISTANCE = 5.93 ANGSTROMS REMARK 525 HOH 183 DISTANCE = 7.91 ANGSTROMS REMARK 525 HOH 190 DISTANCE = 5.47 ANGSTROMS REMARK 525 HOH 197 DISTANCE = 6.86 ANGSTROMS REMARK 525 HOH 198 DISTANCE = 11.42 ANGSTROMS REMARK 525 HOH 201 DISTANCE = 5.22 ANGSTROMS REMARK 525 HOH 203 DISTANCE = 6.00 ANGSTROMS REMARK 525 HOH 207 DISTANCE = 6.64 ANGSTROMS REMARK 525 HOH 209 DISTANCE = 8.25 ANGSTROMS REMARK 525 HOH 210 DISTANCE = 5.36 ANGSTROMS REMARK 525 HOH 211 DISTANCE = 8.59 ANGSTROMS REMARK 525 HOH 212 DISTANCE = 12.04 ANGSTROMS REMARK 525 HOH 213 DISTANCE = 7.39 ANGSTROMS REMARK 525 HOH 215 DISTANCE = 9.07 ANGSTROMS REMARK 525 HOH 218 DISTANCE = 7.17 ANGSTROMS REMARK 525 HOH 220 DISTANCE = 7.01 ANGSTROMS REMARK 525 HOH 221 DISTANCE = 8.22 ANGSTROMS REMARK 525 HOH 222 DISTANCE = 8.04 ANGSTROMS REMARK 525 HOH 223 DISTANCE = 6.06 ANGSTROMS REMARK 525 HOH 225 DISTANCE = 9.30 ANGSTROMS REMARK 525 HOH 227 DISTANCE = 7.89 ANGSTROMS REMARK 525 HOH 229 DISTANCE = 7.59 ANGSTROMS REMARK 525 HOH 230 DISTANCE = 7.05 ANGSTROMS REMARK 525 HOH 231 DISTANCE = 9.30 ANGSTROMS REMARK 525 HOH 232 DISTANCE = 9.24 ANGSTROMS REMARK 525 HOH 238 DISTANCE = 5.90 ANGSTROMS REMARK 525 HOH 240 DISTANCE = 6.59 ANGSTROMS REMARK 525 HOH 245 DISTANCE = 7.98 ANGSTROMS REMARK 525 HOH 253 DISTANCE = 5.35 ANGSTROMS REMARK 525 HOH 255 DISTANCE = 9.55 ANGSTROMS REMARK 525 HOH 256 DISTANCE = 9.21 ANGSTROMS REMARK 525 HOH 264 DISTANCE = 13.65 ANGSTROMS REMARK 525 HOH 270 DISTANCE = 9.35 ANGSTROMS REMARK 525 HOH 274 DISTANCE = 6.22 ANGSTROMS REMARK 525 HOH 293 DISTANCE = 6.29 ANGSTROMS REMARK 525 HOH 302 DISTANCE = 9.89 ANGSTROMS REMARK 525 HOH 305 DISTANCE = 8.82 ANGSTROMS REMARK 525 HOH 306 DISTANCE = 9.20 ANGSTROMS REMARK 525 HOH 307 DISTANCE = 7.96 ANGSTROMS REMARK 525 HOH 311 DISTANCE = 5.36 ANGSTROMS REMARK 525 HOH 313 DISTANCE = 5.42 ANGSTROMS REMARK 525 HOH 315 DISTANCE = 5.04 ANGSTROMS REMARK 525 HOH 330 DISTANCE = 5.54 ANGSTROMS REMARK 525 HOH 331 DISTANCE = 8.26 ANGSTROMS REMARK 525 HOH 337 DISTANCE = 8.90 ANGSTROMS REMARK 525 HOH 342 DISTANCE = 10.25 ANGSTROMS REMARK 525 HOH 346 DISTANCE = 6.02 ANGSTROMS REMARK 525 HOH 347 DISTANCE = 7.26 ANGSTROMS REMARK 525 HOH 363 DISTANCE = 7.60 ANGSTROMS REMARK 525 HOH 367 DISTANCE = 5.92 ANGSTROMS REMARK 525 HOH 370 DISTANCE = 5.63 ANGSTROMS REMARK 525 HOH 373 DISTANCE = 8.27 ANGSTROMS REMARK 525 HOH 374 DISTANCE = 8.54 ANGSTROMS REMARK 525 HOH 376 DISTANCE = 7.67 ANGSTROMS REMARK 525 HOH 377 DISTANCE = 7.31 ANGSTROMS DBREF 1SG1 A 1 120 UNP P01138 NGF_HUMAN 122 241 DBREF 1SG1 B 1 120 UNP P01138 NGF_HUMAN 122 241 DBREF 1SG1 X 1 161 UNP P07174 TNR16_RAT 30 190 SEQRES 1 A 120 SER SER SER HIS PRO ILE PHE HIS ARG GLY GLU PHE SER SEQRES 2 A 120 VAL CYS ASP SER VAL SER VAL TRP VAL GLY ASP LYS THR SEQRES 3 A 120 THR ALA THR ASP ILE LYS GLY LYS GLU VAL MET VAL LEU SEQRES 4 A 120 GLY GLU VAL ASN ILE ASN ASN SER VAL PHE LYS GLN TYR SEQRES 5 A 120 PHE PHE GLU THR LYS CYS ARG ASP PRO ASN PRO VAL ASP SEQRES 6 A 120 SER GLY CYS ARG GLY ILE ASP SER LYS HIS TRP ASN SER SEQRES 7 A 120 TYR CYS THR THR THR HIS THR PHE VAL LYS ALA LEU THR SEQRES 8 A 120 MET ASP GLY LYS GLN ALA ALA TRP ARG PHE ILE ARG ILE SEQRES 9 A 120 ASP THR ALA CYS VAL CYS VAL LEU SER ARG LYS ALA VAL SEQRES 10 A 120 ARG ARG ALA SEQRES 1 B 120 SER SER SER HIS PRO ILE PHE HIS ARG GLY GLU PHE SER SEQRES 2 B 120 VAL CYS ASP SER VAL SER VAL TRP VAL GLY ASP LYS THR SEQRES 3 B 120 THR ALA THR ASP ILE LYS GLY LYS GLU VAL MET VAL LEU SEQRES 4 B 120 GLY GLU VAL ASN ILE ASN ASN SER VAL PHE LYS GLN TYR SEQRES 5 B 120 PHE PHE GLU THR LYS CYS ARG ASP PRO ASN PRO VAL ASP SEQRES 6 B 120 SER GLY CYS ARG GLY ILE ASP SER LYS HIS TRP ASN SER SEQRES 7 B 120 TYR CYS THR THR THR HIS THR PHE VAL LYS ALA LEU THR SEQRES 8 B 120 MET ASP GLY LYS GLN ALA ALA TRP ARG PHE ILE ARG ILE SEQRES 9 B 120 ASP THR ALA CYS VAL CYS VAL LEU SER ARG LYS ALA VAL SEQRES 10 B 120 ARG ARG ALA SEQRES 1 X 161 LYS GLU THR CYS SER THR GLY LEU TYR THR HIS SER GLY SEQRES 2 X 161 GLU CYS CYS LYS ALA CYS ASN LEU GLY GLU GLY VAL ALA SEQRES 3 X 161 GLN PRO CYS GLY ALA ASN GLN THR VAL CYS GLU PRO CYS SEQRES 4 X 161 LEU ASP ASN VAL THR PHE SER ASP VAL VAL SER ALA THR SEQRES 5 X 161 GLU PRO CYS LYS PRO CYS THR GLU CYS LEU GLY LEU GLN SEQRES 6 X 161 SER MET SER ALA PRO CYS VAL GLU ALA ASP ASP ALA VAL SEQRES 7 X 161 CYS ARG CYS ALA TYR GLY TYR TYR GLN ASP GLU GLU THR SEQRES 8 X 161 GLY HIS CYS GLU ALA CYS SER VAL CYS GLU VAL GLY SER SEQRES 9 X 161 GLY LEU VAL PHE SER CYS GLN ASP LYS GLN ASN THR VAL SEQRES 10 X 161 CYS GLU GLU CYS PRO GLU GLY THR TYR SER ASP GLU ALA SEQRES 11 X 161 ASN HIS VAL ASP PRO CYS LEU PRO CYS THR VAL CYS GLU SEQRES 12 X 161 ASP THR GLU ARG GLN LEU ARG GLU CYS THR PRO TRP ALA SEQRES 13 X 161 ASP ALA GLU CYS GLU HET CL 551 1 HETNAM CL CHLORIDE ION FORMUL 4 CL CL 1- FORMUL 5 HOH *375(H2 O) SHEET 1 A 5 PHE A 12 SER A 13 0 SHEET 2 A 5 ALA B 97 ARG B 114 -1 O LEU B 112 N PHE A 12 SHEET 3 A 5 TRP B 76 MET B 92 -1 N ASN B 77 O SER B 113 SHEET 4 A 5 GLU B 35 VAL B 38 -1 N MET B 37 O MET B 92 SHEET 5 A 5 THR B 27 THR B 29 -1 N ALA B 28 O VAL B 36 SHEET 1 B 2 SER A 17 VAL A 22 0 SHEET 2 B 2 PHE A 53 CYS A 58 -1 O GLU A 55 N VAL A 20 SHEET 1 C 2 THR A 27 THR A 29 0 SHEET 2 C 2 GLU A 35 MET A 37 -1 O VAL A 36 N ALA A 28 SHEET 1 D 2 GLU A 41 ASN A 43 0 SHEET 2 D 2 VAL A 48 LYS A 50 -1 O PHE A 49 N VAL A 42 SHEET 1 E 3 TRP A 76 THR A 91 0 SHEET 2 E 3 ALA A 98 ARG A 114 -1 O ALA A 98 N THR A 91 SHEET 3 E 3 PHE B 12 SER B 13 -1 O PHE B 12 N LEU A 112 SHEET 1 F 2 VAL B 18 VAL B 22 0 SHEET 2 F 2 PHE B 53 LYS B 57 -1 O PHE B 53 N VAL B 22 SHEET 1 G 2 VAL B 42 ASN B 43 0 SHEET 2 G 2 VAL B 48 PHE B 49 -1 O PHE B 49 N VAL B 42 SHEET 1 H 2 GLU X 23 GLN X 27 0 SHEET 2 H 2 VAL X 35 PRO X 38 -1 O VAL X 35 N ALA X 26 SHEET 1 I 2 THR X 44 PHE X 45 0 SHEET 2 I 2 LYS X 56 PRO X 57 -1 O LYS X 56 N PHE X 45 SHEET 1 J 2 GLN X 65 ALA X 69 0 SHEET 2 J 2 VAL X 78 CYS X 81 -1 O ARG X 80 N SER X 66 SHEET 1 K 2 TYR X 85 GLN X 87 0 SHEET 2 K 2 CYS X 94 ALA X 96 -1 O GLU X 95 N TYR X 86 SHEET 1 L 2 SER X 104 PHE X 108 0 SHEET 2 L 2 VAL X 117 GLU X 120 -1 O GLU X 119 N GLY X 105 SHEET 1 M 2 THR X 125 TYR X 126 0 SHEET 2 M 2 LEU X 137 PRO X 138 -1 O LEU X 137 N TYR X 126 SSBOND 1 CYS A 15 CYS A 80 SSBOND 2 CYS A 58 CYS A 108 SSBOND 3 CYS A 68 CYS A 110 SSBOND 4 CYS B 15 CYS B 80 SSBOND 5 CYS B 58 CYS B 108 SSBOND 6 CYS B 68 CYS B 110 SSBOND 7 CYS X 4 CYS X 15 SSBOND 8 CYS X 16 CYS X 29 SSBOND 9 CYS X 19 CYS X 36 SSBOND 10 CYS X 39 CYS X 55 SSBOND 11 CYS X 58 CYS X 71 SSBOND 12 CYS X 61 CYS X 79 SSBOND 13 CYS X 81 CYS X 94 SSBOND 14 CYS X 97 CYS X 110 SSBOND 15 CYS X 100 CYS X 118 SSBOND 16 CYS X 121 CYS X 136 SSBOND 17 CYS X 139 CYS X 152 SSBOND 18 CYS X 142 CYS X 160 CRYST1 49.692 91.796 92.010 90.00 90.00 90.00 P 21 21 21 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 0.020124 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010894 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010868 0.00000