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HEADER TRANSFERASE 20-SEP-06 2IFG TITLE STRUCTURE OF THE EXTRACELLULAR SEGMENT OF HUMAN TRKA IN TITLE 2 COMPLEX WITH NERVE GROWTH FACTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIGH AFFINITY NERVE GROWTH FACTOR RECEPTOR; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: NEUROTROPHIC TYROSINE KINASE RECEPTOR TYPE 1, COMPND 5 TRK1 TRANSFORMING TYROSINE KINASE PROTEIN, P140-TRKA, TRK- COMPND 6 A; COMPND 7 EC: 2.7.10.1; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: BETA-NERVE GROWTH FACTOR; COMPND 11 CHAIN: E, F; COMPND 12 SYNONYM: BETA-NGF; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: NTRK1, TRK; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TN5; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PACGP67A; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 GENE: NGFB; SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM KEYWDS TRK, TRKA, NGF, NERVE GROWTH FACTOR, RECEPTOR/LIGAND COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR X.HE,K.C.GARCIA REVDAT 1 13-FEB-07 2IFG 0 JRNL AUTH T.WEHRMAN,X.HE,B.RAAB,A.DUKIPATTI,H.BLAU,K.C.GARCIA JRNL TITL STRUCTURAL AND MECHANISTIC INSIGHTS INTO NERVE JRNL TITL 2 GROWTH FACTOR INTERACTIONS WITH THE TRKA AND P75 JRNL TITL 3 RECEPTORS. JRNL REF NEURON V. 53 25 2007 JRNL REFN ASTM NERNET US ISSN 0896-6273 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.40 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) : 3.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00 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) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 26668 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) : 0.297 REMARK 3 FREE R VALUE : 0.331 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL 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) : 3.40 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.50 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3700 REMARK 3 BIN FREE R VALUE : 0.3910 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 : 7037 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 446 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.60 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL 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 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 2IFG 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 (2007-03-18) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB039513. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-APR-2004 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 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 : 26668 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400 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 : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.50 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 1WWW REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 75.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.91 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, GLYCINE, PH 7.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 7.50 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 40.84050 REMARK 290 SMTRY3 2 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 4 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, E, F, U, V, W, X, Y, REMARK 350 Z, H, I, J, K, L, M 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 E 1 REMARK 465 PRO E 61 REMARK 465 ASN E 62 REMARK 465 PRO E 63 REMARK 465 VAL E 64 REMARK 465 ASP E 65 REMARK 465 SER E 66 REMARK 465 ALA E 116 REMARK 465 VAL E 117 REMARK 465 ARG E 118 REMARK 465 ARG E 119 REMARK 465 ALA E 120 REMARK 465 SER F 1 REMARK 465 PRO F 61 REMARK 465 ASN F 62 REMARK 465 PRO F 63 REMARK 465 VAL F 64 REMARK 465 ASP F 65 REMARK 465 SER F 66 REMARK 465 VAL F 117 REMARK 465 ARG F 118 REMARK 465 ARG F 119 REMARK 465 ALA F 120 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 O PRO B 149 CB HIS B 178 2.04 REMARK 500 O HIS A 178 N GLN A 180 2.06 REMARK 500 O SER A 118 N GLN A 141 2.12 REMARK 500 O SER B 118 N GLN B 141 2.12 REMARK 500 O HIS B 178 N GLN B 180 2.19 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 GLU A 70 C LEU A 71 N -0.050 REMARK 500 THR A 114 C PRO A 115 N 0.101 REMARK 500 PRO A 182 CB PRO A 182 CG -0.073 REMARK 500 PRO A 182 CA PRO A 182 C -0.055 REMARK 500 SER A 204 CA SER A 204 C -0.052 REMARK 500 THR B 114 C PRO B 115 N -0.094 REMARK 500 PRO B 149 C LEU B 150 N 0.069 REMARK 500 SER B 283 CA SER B 283 C -0.061 REMARK 500 PRO E 5 CB PRO E 5 CG 0.056 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 CYS A 41 N - CA - C ANGL. DEV. = 11.8 DEGREES REMARK 500 GLU A 74 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 GLY A 147 N - CA - C ANGL. DEV. =-11.8 DEGREES REMARK 500 GLY A 179 N - CA - C ANGL. DEV. =-13.6 DEGREES REMARK 500 GLY A 181 N - CA - C ANGL. DEV. =-21.5 DEGREES REMARK 500 PRO A 182 N - CA - C ANGL. DEV. = 19.2 DEGREES REMARK 500 PRO A 182 C - N - CA ANGL. DEV. = 19.8 DEGREES REMARK 500 PRO A 182 C - N - CD ANGL. DEV. =-20.9 DEGREES REMARK 500 LEU A 183 N - CA - C ANGL. DEV. = 12.7 DEGREES REMARK 500 LEU A 183 C - N - CA ANGL. DEV. =-11.7 DEGREES REMARK 500 HIS A 185 N - CA - C ANGL. DEV. =-23.3 DEGREES REMARK 500 PRO A 187 N - CA - C ANGL. DEV. =-11.6 DEGREES REMARK 500 LEU A 196 N - CA - C ANGL. DEV. = 12.6 DEGREES REMARK 500 MET A 296 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 LEU A 346 N - CA - C ANGL. DEV. =-20.3 DEGREES REMARK 500 GLY B 147 N - CA - C ANGL. DEV. =-17.9 DEGREES REMARK 500 PRO B 149 CA - C - N ANGL. DEV. =-15.2 DEGREES REMARK 500 PRO B 149 O - C - N ANGL. DEV. = 18.7 DEGREES REMARK 500 GLY B 179 N - CA - C ANGL. DEV. =-12.6 DEGREES REMARK 500 GLY B 181 N - CA - C ANGL. DEV. =-25.4 DEGREES REMARK 500 PRO B 182 N - CA - C ANGL. DEV. = 17.9 DEGREES REMARK 500 PRO B 182 C - N - CA ANGL. DEV. = 13.4 DEGREES REMARK 500 PRO B 182 C - N - CD ANGL. DEV. =-14.7 DEGREES REMARK 500 LEU B 183 N - CA - C ANGL. DEV. = 13.0 DEGREES REMARK 500 HIS B 185 N - CA - C ANGL. DEV. =-24.0 DEGREES REMARK 500 PRO B 187 N - CA - C ANGL. DEV. =-12.4 DEGREES REMARK 500 PRO B 285 N - CA - C ANGL. DEV. = 10.8 DEGREES REMARK 500 ILE B 301 N - CA - C ANGL. DEV. =-11.5 DEGREES REMARK 500 LEU B 346 N - CA - C ANGL. DEV. =-21.4 DEGREES REMARK 500 ASN E 77 N - CA - C ANGL. DEV. =-12.0 DEGREES REMARK 500 ASN F 77 N - CA - C ANGL. DEV. =-13.9 DEGREES REMARK 500 ALA F 97 N - CA - C ANGL. DEV. =-10.8 DEGREES DBREF 2IFG A 36 382 UNP P04629 NTRK1_HUMAN 36 382 DBREF 2IFG B 36 382 UNP P04629 NTRK1_HUMAN 36 382 DBREF 2IFG E 1 120 UNP P01138 NGF_HUMAN 122 241 DBREF 2IFG F 1 120 UNP P01138 NGF_HUMAN 122 241 SEQRES 1 A 347 CYS PRO ASP ALA CYS CYS PRO HIS GLY SER SER GLY LEU SEQRES 2 A 347 ARG CYS THR ARG ASP GLY ALA LEU ASP SER LEU HIS HIS SEQRES 3 A 347 LEU PRO GLY ALA GLU ASN LEU THR GLU LEU TYR ILE GLU SEQRES 4 A 347 ASN GLN GLN HIS LEU GLN HIS LEU GLU LEU ARG ASP LEU SEQRES 5 A 347 ARG GLY LEU GLY GLU LEU ARG ASN LEU THR ILE VAL LYS SEQRES 6 A 347 SER GLY LEU ARG PHE VAL ALA PRO ASP ALA PHE HIS PHE SEQRES 7 A 347 THR PRO ARG LEU SER ARG LEU ASN LEU SER PHE ASN ALA SEQRES 8 A 347 LEU GLU SER LEU SER TRP LYS THR VAL GLN GLY LEU SER SEQRES 9 A 347 LEU GLN GLU LEU VAL LEU SER GLY ASN PRO LEU HIS CYS SEQRES 10 A 347 SER CYS ALA LEU ARG TRP LEU GLN ARG TRP GLU GLU GLU SEQRES 11 A 347 GLY LEU GLY GLY VAL PRO GLU GLN LYS LEU GLN CYS HIS SEQRES 12 A 347 GLY GLN GLY PRO LEU ALA HIS MET PRO ASN ALA SER CYS SEQRES 13 A 347 GLY VAL PRO THR LEU LYS VAL GLN VAL PRO ASN ALA SER SEQRES 14 A 347 VAL ASP VAL GLY ASP ASP VAL LEU LEU ARG CYS GLN VAL SEQRES 15 A 347 GLU GLY ARG GLY LEU GLU GLN ALA GLY TRP ILE LEU THR SEQRES 16 A 347 GLU LEU GLU GLN SER ALA THR VAL MET LYS SER GLY GLY SEQRES 17 A 347 LEU PRO SER LEU GLY LEU THR LEU ALA ASN VAL THR SER SEQRES 18 A 347 ASP LEU ASN ARG LYS ASN VAL THR CYS TRP ALA GLU ASN SEQRES 19 A 347 ASP VAL GLY ARG ALA GLU VAL SER VAL GLN VAL ASN VAL SEQRES 20 A 347 SER PHE PRO ALA SER VAL GLN LEU HIS THR ALA VAL GLU SEQRES 21 A 347 MET HIS HIS TRP CYS ILE PRO PHE SER VAL ASP GLY GLN SEQRES 22 A 347 PRO ALA PRO SER LEU ARG TRP LEU PHE ASN GLY SER VAL SEQRES 23 A 347 LEU ASN GLU THR SER PHE ILE PHE THR GLU PHE LEU GLU SEQRES 24 A 347 PRO ALA ALA ASN GLU THR VAL ARG HIS GLY CYS LEU ARG SEQRES 25 A 347 LEU ASN GLN PRO THR HIS VAL ASN ASN GLY ASN TYR THR SEQRES 26 A 347 LEU LEU ALA ALA ASN PRO PHE GLY GLN ALA SER ALA SER SEQRES 27 A 347 ILE MET ALA ALA PHE MET ASP ASN PRO SEQRES 1 B 347 CYS PRO ASP ALA CYS CYS PRO HIS GLY SER SER GLY LEU SEQRES 2 B 347 ARG CYS THR ARG ASP GLY ALA LEU ASP SER LEU HIS HIS SEQRES 3 B 347 LEU PRO GLY ALA GLU ASN LEU THR GLU LEU TYR ILE GLU SEQRES 4 B 347 ASN GLN GLN HIS LEU GLN HIS LEU GLU LEU ARG ASP LEU SEQRES 5 B 347 ARG GLY LEU GLY GLU LEU ARG ASN LEU THR ILE VAL LYS SEQRES 6 B 347 SER GLY LEU ARG PHE VAL ALA PRO ASP ALA PHE HIS PHE SEQRES 7 B 347 THR PRO ARG LEU SER ARG LEU ASN LEU SER PHE ASN ALA SEQRES 8 B 347 LEU GLU SER LEU SER TRP LYS THR VAL GLN GLY LEU SER SEQRES 9 B 347 LEU GLN GLU LEU VAL LEU SER GLY ASN PRO LEU HIS CYS SEQRES 10 B 347 SER CYS ALA LEU ARG TRP LEU GLN ARG TRP GLU GLU GLU SEQRES 11 B 347 GLY LEU GLY GLY VAL PRO GLU GLN LYS LEU GLN CYS HIS SEQRES 12 B 347 GLY GLN GLY PRO LEU ALA HIS MET PRO ASN ALA SER CYS SEQRES 13 B 347 GLY VAL PRO THR LEU LYS VAL GLN VAL PRO ASN ALA SER SEQRES 14 B 347 VAL ASP VAL GLY ASP ASP VAL LEU LEU ARG CYS GLN VAL SEQRES 15 B 347 GLU GLY ARG GLY LEU GLU GLN ALA GLY TRP ILE LEU THR SEQRES 16 B 347 GLU LEU GLU GLN SER ALA THR VAL MET LYS SER GLY GLY SEQRES 17 B 347 LEU PRO SER LEU GLY LEU THR LEU ALA ASN VAL THR SER SEQRES 18 B 347 ASP LEU ASN ARG LYS ASN VAL THR CYS TRP ALA GLU ASN SEQRES 19 B 347 ASP VAL GLY ARG ALA GLU VAL SER VAL GLN VAL ASN VAL SEQRES 20 B 347 SER PHE PRO ALA SER VAL GLN LEU HIS THR ALA VAL GLU SEQRES 21 B 347 MET HIS HIS TRP CYS ILE PRO PHE SER VAL ASP GLY GLN SEQRES 22 B 347 PRO ALA PRO SER LEU ARG TRP LEU PHE ASN GLY SER VAL SEQRES 23 B 347 LEU ASN GLU THR SER PHE ILE PHE THR GLU PHE LEU GLU SEQRES 24 B 347 PRO ALA ALA ASN GLU THR VAL ARG HIS GLY CYS LEU ARG SEQRES 25 B 347 LEU ASN GLN PRO THR HIS VAL ASN ASN GLY ASN TYR THR SEQRES 26 B 347 LEU LEU ALA ALA ASN PRO PHE GLY GLN ALA SER ALA SER SEQRES 27 B 347 ILE MET ALA ALA PHE MET ASP ASN PRO SEQRES 1 E 120 SER SER SER HIS PRO ILE PHE HIS ARG GLY GLU PHE SER SEQRES 2 E 120 VAL CYS ASP SER VAL SER VAL TRP VAL GLY ASP LYS THR SEQRES 3 E 120 THR ALA THR ASP ILE LYS GLY LYS GLU VAL MET VAL LEU SEQRES 4 E 120 GLY GLU VAL ASN ILE ASN ASN SER VAL PHE LYS GLN TYR SEQRES 5 E 120 PHE PHE GLU THR LYS CYS ARG ASP PRO ASN PRO VAL ASP SEQRES 6 E 120 SER GLY CYS ARG GLY ILE ASP SER LYS HIS TRP ASN SER SEQRES 7 E 120 TYR CYS THR THR THR HIS THR PHE VAL LYS ALA LEU THR SEQRES 8 E 120 MET ASP GLY LYS GLN ALA ALA TRP ARG PHE ILE ARG ILE SEQRES 9 E 120 ASP THR ALA CYS VAL CYS VAL LEU SER ARG LYS ALA VAL SEQRES 10 E 120 ARG ARG ALA SEQRES 1 F 120 SER SER SER HIS PRO ILE PHE HIS ARG GLY GLU PHE SER SEQRES 2 F 120 VAL CYS ASP SER VAL SER VAL TRP VAL GLY ASP LYS THR SEQRES 3 F 120 THR ALA THR ASP ILE LYS GLY LYS GLU VAL MET VAL LEU SEQRES 4 F 120 GLY GLU VAL ASN ILE ASN ASN SER VAL PHE LYS GLN TYR SEQRES 5 F 120 PHE PHE GLU THR LYS CYS ARG ASP PRO ASN PRO VAL ASP SEQRES 6 F 120 SER GLY CYS ARG GLY ILE ASP SER LYS HIS TRP ASN SER SEQRES 7 F 120 TYR CYS THR THR THR HIS THR PHE VAL LYS ALA LEU THR SEQRES 8 F 120 MET ASP GLY LYS GLN ALA ALA TRP ARG PHE ILE ARG ILE SEQRES 9 F 120 ASP THR ALA CYS VAL CYS VAL LEU SER ARG LYS ALA VAL SEQRES 10 F 120 ARG ARG ALA MODRES 1YK2 ASN A 95 ASN GLYCOSYLATION SITE MODRES 1YK2 ASN A 121 ASN GLYCOSYLATION SITE MODRES 1YK2 ASN A 188 ASN GLYCOSYLATION SITE MODRES 1YK2 ASN A 262 ASN GLYCOSYLATION SITE MODRES 1YK2 ASN A 281 ASN GLYCOSYLATION SITE MODRES 1YK2 ASN A 358 ASN GLYCOSYLATION SITE MODRES 1YK2 ASN B 95 ASN GLYCOSYLATION SITE MODRES 1YK2 ASN B 121 ASN GLYCOSYLATION SITE MODRES 1YK2 ASN B 188 ASN GLYCOSYLATION SITE MODRES 1YK2 ASN B 262 ASN GLYCOSYLATION SITE MODRES 1YK2 ASN B 281 ASN GLYCOSYLATION SITE MODRES 1YK2 ASN B 358 ASN GLYCOSYLATION SITE MODRES 2IFG ASN A 95 ASN GLYCOSYLATION SITE MODRES 2IFG ASN A 121 ASN GLYCOSYLATION SITE MODRES 2IFG ASN A 188 ASN GLYCOSYLATION SITE MODRES 2IFG ASN A 262 ASN GLYCOSYLATION SITE MODRES 2IFG ASN A 281 ASN GLYCOSYLATION SITE MODRES 2IFG ASN A 358 ASN GLYCOSYLATION SITE MODRES 2IFG ASN B 95 ASN GLYCOSYLATION SITE MODRES 2IFG ASN B 121 ASN GLYCOSYLATION SITE MODRES 2IFG ASN B 188 ASN GLYCOSYLATION SITE MODRES 2IFG ASN B 262 ASN GLYCOSYLATION SITE MODRES 2IFG ASN B 281 ASN GLYCOSYLATION SITE MODRES 2IFG ASN B 358 ASN GLYCOSYLATION SITE HET NAG U 1 14 HET NDG U 2 14 HET NAG V 1 14 HET NDG V 2 14 HET MAN V 3 11 HET NAG W 1 14 HET NDG W 2 14 HET BMA W 3 11 HET NDG X 1 14 HET NDG X 2 14 HET BMA X 3 11 HET NDG Y 1 14 HET NDG Y 2 14 HET MAN Y 3 11 HET NDG Z 1 14 HET NDG Z 2 14 HET BMA Z 3 11 HET NAG H 1 14 HET NDG H 2 14 HET NAG I 1 14 HET NDG I 2 14 HET MAN I 3 11 HET NAG J 1 14 HET NDG J 2 14 HET BMA J 3 11 HET NAG K 1 14 HET NDG K 2 14 HET BMA K 3 11 HET NDG L 1 14 HET NDG L 2 14 HET MAN L 3 11 HET NDG M 1 14 HET NDG M 2 14 HET BMA M 3 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM BMA BETA-D-MANNOSE HETSYN NAG NAG FORMUL 5 NAG 7(C8 H15 N O6) FORMUL 5 NDG 17(C8 H15 N O6) FORMUL 6 MAN 4(C6 H12 O6) FORMUL 7 BMA 6(C6 H12 O6) HELIX 1 1 GLU A 83 LEU A 87 5 5 HELIX 2 2 ASP A 109 PHE A 113 5 5 HELIX 3 3 SER A 153 ALA A 155 5 3 HELIX 4 4 LEU A 156 GLU A 165 1 10 HELIX 5 5 VAL A 170 LYS A 174 5 5 HELIX 6 6 THR A 352 ASN A 356 5 5 HELIX 7 7 GLU B 83 ARG B 88 5 6 HELIX 8 8 ASP B 109 PHE B 113 5 5 HELIX 9 9 SER B 131 VAL B 135 5 5 HELIX 10 10 SER B 153 ALA B 155 5 3 HELIX 11 11 LEU B 156 GLU B 165 1 10 HELIX 12 12 VAL B 170 LYS B 174 5 5 HELIX 13 13 THR B 255 ASN B 259 5 5 HELIX 14 14 THR B 352 ASN B 356 5 5 HELIX 15 15 PRO E 5 GLY E 10 1 6 HELIX 16 16 PRO F 5 GLY F 10 1 6 SHEET 1 A 5 LEU A 48 ARG A 49 0 SHEET 2 A 5 GLU A 70 TYR A 72 1 O GLU A 70 N LEU A 48 SHEET 3 A 5 ASN A 95 THR A 97 1 O THR A 97 N LEU A 71 SHEET 4 A 5 ARG A 119 ASN A 121 1 O ASN A 121 N LEU A 96 SHEET 5 A 5 GLU A 142 VAL A 144 1 O GLU A 142 N LEU A 120 SHEET 1 B 2 HIS A 81 LEU A 82 0 SHEET 2 B 2 PHE A 105 VAL A 106 1 O PHE A 105 N LEU A 82 SHEET 1 C 4 THR A 195 GLN A 199 0 SHEET 2 C 4 VAL A 211 GLU A 218 -1 O GLU A 218 N THR A 195 SHEET 3 C 4 SER A 246 ALA A 252 -1 O LEU A 249 N LEU A 213 SHEET 4 C 4 ALA A 236 VAL A 238 -1 N ALA A 236 O ALA A 252 SHEET 1 D 3 TRP A 227 LEU A 229 0 SHEET 2 D 3 VAL A 263 CYS A 265 -1 O THR A 264 N ILE A 228 SHEET 3 D 3 VAL A 276 VAL A 278 -1 O VAL A 276 N CYS A 265 SHEET 1 E 2 GLU A 268 ASN A 269 0 SHEET 2 E 2 GLY A 272 ARG A 273 -1 O GLY A 272 N ASN A 269 SHEET 1 F 3 PHE A 284 LEU A 290 0 SHEET 2 F 3 TRP A 299 GLN A 308 -1 O ASP A 306 N SER A 287 SHEET 3 F 3 VAL A 294 GLU A 295 -1 N VAL A 294 O CYS A 300 SHEET 1 G 4 PHE A 284 LEU A 290 0 SHEET 2 G 4 TRP A 299 GLN A 308 -1 O ASP A 306 N SER A 287 SHEET 3 G 4 ARG A 342 LEU A 348 -1 O LEU A 348 N TRP A 299 SHEET 4 G 4 ILE A 328 PHE A 332 -1 N PHE A 329 O ARG A 347 SHEET 1 H 4 SER A 320 VAL A 321 0 SHEET 2 H 4 SER A 312 PHE A 317 -1 N PHE A 317 O SER A 320 SHEET 3 H 4 GLY A 357 ASN A 365 -1 O LEU A 362 N ARG A 314 SHEET 4 H 4 GLY A 368 ALA A 376 -1 O ILE A 374 N TYR A 359 SHEET 1 I 5 GLY B 47 ARG B 49 0 SHEET 2 I 5 GLU B 70 TYR B 72 1 O GLU B 70 N LEU B 48 SHEET 3 I 5 ASN B 95 THR B 97 1 O THR B 97 N LEU B 71 SHEET 4 I 5 ARG B 119 ASN B 121 1 O ASN B 121 N LEU B 96 SHEET 5 I 5 GLU B 142 VAL B 144 1 O GLU B 142 N LEU B 120 SHEET 1 J 2 HIS B 81 LEU B 82 0 SHEET 2 J 2 PHE B 105 VAL B 106 1 O PHE B 105 N LEU B 82 SHEET 1 K 4 THR B 195 GLN B 199 0 SHEET 2 K 4 VAL B 211 GLU B 218 -1 O GLN B 216 N LYS B 197 SHEET 3 K 4 SER B 246 ALA B 252 -1 O LEU B 251 N VAL B 211 SHEET 4 K 4 ALA B 236 VAL B 238 -1 N VAL B 238 O THR B 250 SHEET 1 L 3 TRP B 227 LEU B 229 0 SHEET 2 L 3 VAL B 263 CYS B 265 -1 O THR B 264 N ILE B 228 SHEET 3 L 3 VAL B 276 VAL B 278 -1 O VAL B 278 N VAL B 263 SHEET 1 M 3 PHE B 284 LEU B 290 0 SHEET 2 M 3 TRP B 299 GLN B 308 -1 O GLN B 308 N PHE B 284 SHEET 3 M 3 VAL B 294 GLU B 295 -1 N VAL B 294 O CYS B 300 SHEET 1 N 4 PHE B 284 LEU B 290 0 SHEET 2 N 4 TRP B 299 GLN B 308 -1 O GLN B 308 N PHE B 284 SHEET 3 N 4 ARG B 342 LEU B 348 -1 O ARG B 342 N VAL B 305 SHEET 4 N 4 ILE B 328 PHE B 332 -1 N PHE B 329 O ARG B 347 SHEET 1 O 4 SER B 320 VAL B 321 0 SHEET 2 O 4 SER B 312 PHE B 317 -1 N PHE B 317 O SER B 320 SHEET 3 O 4 GLY B 357 ASN B 365 -1 O LEU B 362 N ARG B 314 SHEET 4 O 4 GLY B 368 ALA B 376 -1 O ILE B 374 N TYR B 359 SHEET 1 P 5 GLU E 11 SER E 13 0 SHEET 2 P 5 GLN F 96 ARG F 114 -1 O LEU F 112 N PHE E 12 SHEET 3 P 5 TRP F 76 ASP F 93 -1 N ASN F 77 O SER F 113 SHEET 4 P 5 GLU F 35 VAL F 38 -1 N MET F 37 O MET F 92 SHEET 5 P 5 THR F 27 THR F 29 -1 N ALA F 28 O VAL F 36 SHEET 1 Q 2 SER E 17 VAL E 22 0 SHEET 2 Q 2 PHE E 53 CYS E 58 -1 O PHE E 53 N VAL E 22 SHEET 1 R 5 THR E 27 THR E 29 0 SHEET 2 R 5 GLU E 35 VAL E 38 -1 O VAL E 36 N ALA E 28 SHEET 3 R 5 TRP E 76 MET E 92 -1 O MET E 92 N MET E 37 SHEET 4 R 5 ALA E 97 ARG E 114 -1 O SER E 113 N ASN E 77 SHEET 5 R 5 GLU F 11 SER F 13 -1 O PHE F 12 N LEU E 112 SHEET 1 S 2 GLU E 41 ASN E 43 0 SHEET 2 S 2 VAL E 48 LYS E 50 -1 O PHE E 49 N VAL E 42 SHEET 1 T 2 SER F 17 VAL F 22 0 SHEET 2 T 2 PHE F 53 CYS F 58 -1 O PHE F 53 N VAL F 22 SHEET 1 U 2 GLU F 41 ILE F 44 0 SHEET 2 U 2 SER F 47 LYS F 50 -1 O PHE F 49 N VAL F 42 SSBOND 1 CYS A 36 CYS A 41 SSBOND 2 CYS A 40 CYS A 50 SSBOND 3 CYS A 152 CYS A 177 SSBOND 4 CYS A 154 CYS A 191 SSBOND 5 CYS A 215 CYS A 265 SSBOND 6 CYS A 300 CYS A 345 SSBOND 7 CYS B 36 CYS B 41 SSBOND 8 CYS B 40 CYS B 50 SSBOND 9 CYS B 152 CYS B 177 SSBOND 10 CYS B 154 CYS B 191 SSBOND 11 CYS B 215 CYS B 265 SSBOND 12 CYS B 300 CYS B 345 SSBOND 13 CYS E 15 CYS E 80 SSBOND 14 CYS E 58 CYS E 108 SSBOND 15 CYS E 68 CYS E 110 SSBOND 16 CYS F 15 CYS F 80 SSBOND 17 CYS F 58 CYS F 108 SSBOND 18 CYS F 68 CYS F 110 LINK ND2 ASN A 95 C1 NDG Y 1 LINK ND2 ASN A 121 C1 NDG Z 1 LINK ND2 ASN A 188 C1 NAG U 1 LINK ND2 ASN A 262 C1 NAG V 1 LINK ND2 ASN A 281 C1 NAG W 1 LINK ND2 ASN A 358 C1 NDG X 1 LINK ND2 ASN B 95 C1 NDG L 1 LINK ND2 ASN B 121 C1 NDG M 1 LINK ND2 ASN B 188 C1 NAG H 1 LINK ND2 ASN B 262 C1 NAG I 1 LINK ND2 ASN B 281 C1 NAG J 1 LINK ND2 ASN B 358 C1 NAG K 1 LINK O4 NAG U 1 C1 NDG U 2 LINK O4 NAG V 1 C1 NDG V 2 LINK O4 NDG V 2 C1 MAN V 3 LINK O4 NAG W 1 C1 NDG W 2 LINK O4 NDG W 2 C1 BMA W 3 LINK O4 NDG X 1 C1 NDG X 2 LINK O4 NDG X 2 C1 BMA X 3 LINK O4 NDG Y 1 C1 NDG Y 2 LINK O4 NDG Y 2 C1 MAN Y 3 LINK O4 NDG Z 1 C1 NDG Z 2 LINK O4 NDG Z 2 C1 BMA Z 3 LINK O4 NAG H 1 C1 NDG H 2 LINK O4 NAG I 1 C1 NDG I 2 LINK O4 NDG I 2 C1 MAN I 3 LINK O4 NAG J 1 C1 NDG J 2 LINK O4 NDG J 2 C1 BMA J 3 LINK O4 NAG K 1 C1 NDG K 2 LINK O4 NDG K 2 C1 BMA K 3 LINK O4 NDG L 1 C1 NDG L 2 LINK O4 NDG L 2 C1 MAN L 3 LINK O4 NDG M 1 C1 NDG M 2 LINK O4 NDG M 2 C1 BMA M 3 CISPEP 1 CYS A 36 PRO A 37 0 -0.32 CISPEP 2 GLN A 308 PRO A 309 0 0.51 CISPEP 3 CYS B 36 PRO B 37 0 -0.20 CISPEP 4 GLN B 308 PRO B 309 0 -0.31 CRYST1 110.215 81.681 115.748 90.00 104.15 90.00 P 1 21 1 4 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 0.009073 0.000000 0.002287 0.00000 SCALE2 0.000000 0.012243 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008910 0.00000