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HEADER TRANSFERASE 20-NOV-00 1HE7 TITLE HUMAN NERVE GROWTH FACTOR RECEPTOR TRKA COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIGH AFFINITY NERVE GROWTH FACTOR RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN, SPANS RESIDUES 285-380; COMPND 5 SYNONYM: TRK1 TRANSFORMING TYROSINE KINASE PROTEIN, P140- COMPND 6 TRKA, TRK-A; COMPND 7 EC: 2.7.1.112; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 6 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B KEYWDS TRANSFERASE, TRK-RECEPTOR, STRAND-SWAPPING, NERVE GROWTH KEYWDS 2 FACTOR EXPDTA X-RAY DIFFRACTION AUTHOR M.J.BANFIELD,A.ROBERTSON,S.J.ALLEN,J.A.DANDO,S.J.TYLER, AUTHOR 2 G.S.BENNETT,S.D.BRAIN,G.MASON,P.H.HOLDEN,A.R.CLARKE, AUTHOR 3 R.L.NAYLOR,G.K.WILCOCK,R.L.BRADY REVDAT 2 01-APR-03 1HE7 1 JRNL REVDAT 1 02-APR-01 1HE7 0 JRNL AUTH A.G.ROBERTSON,M.J.BANFIELD,S.J.ALLEN,J.A.DANDO, JRNL AUTH 2 G.G.MASON,S.J.TYLER,G.S.BENNETT,S.D.BRAIN, JRNL AUTH 3 A.R.CLARKE,R.L.NAYLOR,G.K.WILCOCK,R.L.BRADY, JRNL AUTH 4 D.DAWBARN JRNL TITL IDENTIFICATION AND STRUCTURE OF THE NERVE GROWTH JRNL TITL 2 FACTOR BINDING SITE ON TRKA. JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 282 131 2001 JRNL REFN ASTM BBRCA9 US ISSN 0006-291X REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.H.ULTSCH,C.WIESMANN,L.C.SIMMONS,J.HENRICH,M.YANG, REMARK 1 AUTH 2 D.REILLY,S.H.BASS,A.M.DE VOS REMARK 1 TITL CRYSTAL STRUCTURE OF THE NEUROTROPHIN-BINDING REMARK 1 TITL 2 DOMAIN OF TRKA, TRKB AND TRKC REMARK 1 REF J.MOL.BIOL. V. 290 149 1999 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REFERENCE 2 REMARK 1 AUTH C.WIESMANN,M.H.ULTSCH,S.H.BASS,A.M.DE VOS REMARK 1 TITL CRYSTAL STRUCTURE OF NERVE GROWTH FACTOR IN REMARK 1 TITL 2 COMPLEX WITH THE LIGAND-BINDING DOMAIN OF THE TRKA REMARK 1 TITL 3 RECEPTOR REMARK 1 REF NATURE V. 401 184 1999 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00 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) (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 10145 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.237 REMARK 3 FREE R VALUE : 0.276 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 992 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 : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1109 REMARK 3 BIN R VALUE (WORKING SET) : 0.2540 REMARK 3 BIN FREE R VALUE : 0.2910 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 123 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 : 900 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 6 REMARK 3 SOLVENT ATOMS : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 23.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.30 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -8.98700 REMARK 3 B22 (A**2) : -8.98700 REMARK 3 B33 (A**2) : 17.97400 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28 REMARK 3 ESD FROM SIGMAA (A) : 0.18 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.35 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.016 REMARK 3 BOND ANGLES (DEGREES) : 1.74 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.50 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.03 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.650 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.756 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.238 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.152 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : 0.35 REMARK 3 BSOL : 46.80 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 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : GOL.PAR REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE FOLLOWING ATOMS WERE SET TO ZERO REMARK 3 OCCUPANCY AS THEY WERE NOT OBSERVED IN ELECTRON DENSI REMARK 4 REMARK 4 1HE7 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 3.101 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-5569 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-FEB-1999 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 4.70 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG REMARK 200 BEAMLINE : X11 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.91 REMARK 200 MONOCHROMATOR : MIRRORS REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11819 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.200 REMARK 200 R MERGE (I) : 0.04100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 43.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7 REMARK 200 DATA REDUNDANCY IN SHELL : 5.70 REMARK 200 R MERGE FOR SHELL (I) : 0.23300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1WWA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 32.40 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.7 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 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 -Y,X,3/4+Z REMARK 290 4555 Y,-X,1/4+Z REMARK 290 5555 -X,Y,-Z REMARK 290 6555 X,-Y,1/2-Z REMARK 290 7555 Y,X,1/4-Z REMARK 290 8555 -Y,-X,3/4-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 53.90400 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 80.85600 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.95200 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 53.90400 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 26.95200 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 80.85600 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 1 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 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 50.85400 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 53.90400 REMARK 350 APPLY THE FOLLOWING TO CHAINS: Z 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH Z 7 LIES ON A SPECIAL POSITION. 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 ASP A 389 REMARK 465 PRO A 390 REMARK 465 ILE A 391 REMARK 465 PRO A 392 REMARK 465 ASP A 393 REMARK 465 THR A 394 REMARK 465 ASN A 395 REMARK 465 SER A 396 REMARK 465 THR A 397 REMARK 465 SER A 398 REMARK 465 GLY A 399 REMARK 465 ASP A 400 REMARK 465 PRO A 401 REMARK 465 VAL A 402 REMARK 465 GLU A 403 REMARK 465 LYS A 404 REMARK 465 LYS A 405 REMARK 465 ASP A 406 REMARK 465 GLU A 407 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET A 296 SD MET A 296 CE 0.223 REMARK 500 MET A 375 SD MET A 375 CE -0.110 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 ILE A 301 N - CA - C ANGL. DEV. =-12.8 DEGREES REMARK 500 LEU A 346 N - CA - C ANGL. DEV. =-17.7 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 ASN A 338 -31.14 70.23 DBREF 1HE7 A 282 407 UNP P04629 NTRK1_HUMAN 282 407 SEQADV 1HE7 SER A 282 UNP P04629 VAL 282 CLONING ARTIFACT SEQADV 1HE7 HIS A 283 UNP P04629 SER 283 CLONING ARTIFACT SEQADV 1HE7 MET A 284 UNP P04629 PHE 284 CLONING ARTIFACT SEQADV 1HE7 A UNP P04629 VAL 393 DELETION SEQADV 1HE7 A UNP P04629 SER 394 DELETION SEQADV 1HE7 A UNP P04629 PHE 395 DELETION SEQADV 1HE7 A UNP P04629 SER 396 DELETION SEQADV 1HE7 A UNP P04629 PRO 397 DELETION SEQADV 1HE7 A UNP P04629 VAL 398 DELETION SEQRES 1 A 126 SER HIS MET PRO ALA SER VAL GLN LEU HIS THR ALA VAL SEQRES 2 A 126 GLU MET HIS HIS TRP CYS ILE PRO PHE SER VAL ASP GLY SEQRES 3 A 126 GLN PRO ALA PRO SER LEU ARG TRP LEU PHE ASN GLY SER SEQRES 4 A 126 VAL LEU ASN GLU THR SER PHE ILE PHE THR GLU PHE LEU SEQRES 5 A 126 GLU PRO ALA ALA ASN GLU THR VAL ARG HIS GLY CYS LEU SEQRES 6 A 126 ARG LEU ASN GLN PRO THR HIS VAL ASN ASN GLY ASN TYR SEQRES 7 A 126 THR LEU LEU ALA ALA ASN PRO PHE GLY GLN ALA SER ALA SEQRES 8 A 126 SER ILE MET ALA ALA PHE MET ASP ASN PRO PHE GLU PHE SEQRES 9 A 126 ASN PRO GLU ASP PRO ILE PRO ASP THR ASN SER THR SER SEQRES 10 A 126 GLY ASP PRO VAL GLU LYS LYS ASP GLU HET GOL A1389 6 HETNAM GOL GLYCEROL FORMUL 2 GOL C3 H8 O3 FORMUL 3 HOH *32(H2 O) HELIX 1 1 THR A 352 ASN A 356 5 5 SHEET 1 AA 3 HIS A 298 VAL A 305 0 SHEET 2 AA 3 ARG A 342 ASN A 349 -1 O ARG A 342 N VAL A 305 SHEET 3 AA 3 ILE A 328 LEU A 333 -1 O PHE A 329 N ARG A 347 SHEET 1 AB 4 SER A 320 VAL A 321 0 SHEET 2 AB 4 SER A 312 PHE A 317 -1 O PHE A 317 N SER A 320 SHEET 3 AB 4 GLY A 357 ASN A 365 -1 O THR A 360 N LEU A 316 SHEET 4 AB 4 GLY A 368 ALA A 376 -1 O GLY A 368 N ASN A 365 SSBOND 1 CYS A 300 CYS A 345 CISPEP 1 GLN A 308 PRO A 309 0 0.29 CRYST1 50.854 50.854 107.808 90.00 90.00 90.00 P 43 2 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 0.019664 0.000000 0.000000 0.00000 SCALE2 0.000000 0.019664 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009276 0.00000