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HEADER NERVE GROWTH FACTOR/TRKA COMPLEX 12-MAR-99 1WWW TITLE NGF IN COMPLEX WITH DOMAIN 5 OF THE TRKA RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (NERVE GROWTH FACTOR); COMPND 3 CHAIN: V, W; COMPND 4 SYNONYM: BETA-NGF; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: PROTEIN (TRKA RECEPTOR); COMPND 8 CHAIN: X, Y; COMPND 9 FRAGMENT: DOMAIN 5; COMPND 10 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 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 7 ORGANISM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI KEYWDS COMPLEX, TRKA RECEPTOR, NERVE GROWTH FACTOR, CYSTEINE KNOT, KEYWDS 2 IMMUNOGLOBULIN LIKE DOMAIN EXPDTA X-RAY DIFFRACTION AUTHOR C.WIESMANN,M.H.ULTSCH,A.M.DE VOS REVDAT 2 01-APR-03 1WWW 1 JRNL REVDAT 1 15-SEP-99 1WWW 0 JRNL AUTH C.WIESMANN,M.H.ULTSCH,S.H.BASS,A.M.DE VOS JRNL TITL CRYSTAL STRUCTURE OF NERVE GROWTH FACTOR IN JRNL TITL 2 COMPLEX WITH THE LIGAND-BINDING DOMAIN OF THE TRKA JRNL TITL 3 RECEPTOR. JRNL REF NATURE V. 401 184 1999 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.200 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.2 REMARK 3 NUMBER OF REFLECTIONS : 22780 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.189 REMARK 3 FREE R VALUE : 0.266 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2282 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) : 2.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.10 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2391 REMARK 3 BIN R VALUE (WORKING SET) : 0.2830 REMARK 3 BIN FREE R VALUE : 0.3784 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 259 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 : 3283 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 262 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) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.91 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 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 1WWW 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 RCSB000637. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 160.0 REMARK 200 PH : 5.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23361 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.07100 REMARK 200 FOR THE DATA SET : 7.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.50 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.35500 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: AMORE REMARK 200 STARTING MODEL: 1BET REMARK 200 REMARK 200 REMARK: DATA WERE COLLECTED AT THE ADVANCED LIGHT SOURCE, REMARK 200 BERKELEY REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.0 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 26.86750 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: V, W, X, Y 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 V 1 REMARK 465 PRO V 61 REMARK 465 ASN V 62 REMARK 465 PRO V 63 REMARK 465 VAL V 64 REMARK 465 ASP V 65 REMARK 465 SER V 66 REMARK 465 ALA V 116 REMARK 465 VAL V 117 REMARK 465 ARG V 118 REMARK 465 ARG V 119 REMARK 465 ALA V 120 REMARK 465 SER W 1 REMARK 465 PRO W 61 REMARK 465 ASN W 62 REMARK 465 PRO W 63 REMARK 465 VAL W 64 REMARK 465 ASP W 65 REMARK 465 SER W 66 REMARK 465 VAL W 117 REMARK 465 ARG W 118 REMARK 465 ARG W 119 REMARK 465 ALA W 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 HOH 32 O HOH 70 2.15 REMARK 500 O HOH 72 O HOH 241 2.17 REMARK 500 O HOH 73 O HOH 86 2.17 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 TRP V 76 CB TRP V 76 CG -0.061 REMARK 500 MET X 296 SD MET X 296 CE 0.063 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 V 77 N - CA - C ANGL. DEV. =-11.9 DEGREES REMARK 500 ASN W 77 N - CA - C ANGL. DEV. =-13.9 DEGREES REMARK 500 ALA W 97 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 ILE X 301 N - CA - C ANGL. DEV. =-11.5 DEGREES REMARK 500 SER X 312 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 LEU X 333 N - CA - C ANGL. DEV. =-10.5 DEGREES REMARK 500 LEU X 346 N - CA - C ANGL. DEV. =-21.3 DEGREES REMARK 500 LEU X 348 CA - CB - CG ANGL. DEV. = 11.8 DEGREES REMARK 500 SER Y 287 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 MET Y 296 N - CA - C ANGL. DEV. =-10.7 DEGREES REMARK 500 HIS Y 298 N - CA - C ANGL. DEV. =-10.6 DEGREES REMARK 500 LEU Y 346 N - CA - C ANGL. DEV. =-20.2 DEGREES 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 96 DISTANCE = 5.42 ANGSTROMS REMARK 525 HOH 260 DISTANCE = 6.81 ANGSTROMS DBREF 1WWW V 1 120 UNP P01138 NGF_HUMAN 122 241 DBREF 1WWW W 1 120 UNP P01138 NGF_HUMAN 122 241 DBREF 1WWW X 282 382 UNP P04629 NTRK1_HUMAN 282 382 DBREF 1WWW Y 282 382 UNP P04629 NTRK1_HUMAN 282 382 SEQRES 1 V 120 SER SER SER HIS PRO ILE PHE HIS ARG GLY GLU PHE SER SEQRES 2 V 120 VAL CYS ASP SER VAL SER VAL TRP VAL GLY ASP LYS THR SEQRES 3 V 120 THR ALA THR ASP ILE LYS GLY LYS GLU VAL MET VAL LEU SEQRES 4 V 120 GLY GLU VAL ASN ILE ASN ASN SER VAL PHE LYS GLN TYR SEQRES 5 V 120 PHE PHE GLU THR LYS CYS ARG ASP PRO ASN PRO VAL ASP SEQRES 6 V 120 SER GLY CYS ARG GLY ILE ASP SER LYS HIS TRP ASN SER SEQRES 7 V 120 TYR CYS THR THR THR HIS THR PHE VAL LYS ALA LEU THR SEQRES 8 V 120 MET ASP GLY LYS GLN ALA ALA TRP ARG PHE ILE ARG ILE SEQRES 9 V 120 ASP THR ALA CYS VAL CYS VAL LEU SER ARG LYS ALA VAL SEQRES 10 V 120 ARG ARG ALA SEQRES 1 W 120 SER SER SER HIS PRO ILE PHE HIS ARG GLY GLU PHE SER SEQRES 2 W 120 VAL CYS ASP SER VAL SER VAL TRP VAL GLY ASP LYS THR SEQRES 3 W 120 THR ALA THR ASP ILE LYS GLY LYS GLU VAL MET VAL LEU SEQRES 4 W 120 GLY GLU VAL ASN ILE ASN ASN SER VAL PHE LYS GLN TYR SEQRES 5 W 120 PHE PHE GLU THR LYS CYS ARG ASP PRO ASN PRO VAL ASP SEQRES 6 W 120 SER GLY CYS ARG GLY ILE ASP SER LYS HIS TRP ASN SER SEQRES 7 W 120 TYR CYS THR THR THR HIS THR PHE VAL LYS ALA LEU THR SEQRES 8 W 120 MET ASP GLY LYS GLN ALA ALA TRP ARG PHE ILE ARG ILE SEQRES 9 W 120 ASP THR ALA CYS VAL CYS VAL LEU SER ARG LYS ALA VAL SEQRES 10 W 120 ARG ARG ALA SEQRES 1 X 101 VAL SER PHE PRO ALA SER VAL GLN LEU HIS THR ALA VAL SEQRES 2 X 101 GLU MET HIS HIS TRP CYS ILE PRO PHE SER VAL ASP GLY SEQRES 3 X 101 GLN PRO ALA PRO SER LEU ARG TRP LEU PHE ASN GLY SER SEQRES 4 X 101 VAL LEU ASN GLU THR SER PHE ILE PHE THR GLU PHE LEU SEQRES 5 X 101 GLU PRO ALA ALA ASN GLU THR VAL ARG HIS GLY CYS LEU SEQRES 6 X 101 ARG LEU ASN GLN PRO THR HIS VAL ASN ASN GLY ASN TYR SEQRES 7 X 101 THR LEU LEU ALA ALA ASN PRO PHE GLY GLN ALA SER ALA SEQRES 8 X 101 SER ILE MET ALA ALA PHE MET ASP ASN PRO SEQRES 1 Y 101 VAL SER PHE PRO ALA SER VAL GLN LEU HIS THR ALA VAL SEQRES 2 Y 101 GLU MET HIS HIS TRP CYS ILE PRO PHE SER VAL ASP GLY SEQRES 3 Y 101 GLN PRO ALA PRO SER LEU ARG TRP LEU PHE ASN GLY SER SEQRES 4 Y 101 VAL LEU ASN GLU THR SER PHE ILE PHE THR GLU PHE LEU SEQRES 5 Y 101 GLU PRO ALA ALA ASN GLU THR VAL ARG HIS GLY CYS LEU SEQRES 6 Y 101 ARG LEU ASN GLN PRO THR HIS VAL ASN ASN GLY ASN TYR SEQRES 7 Y 101 THR LEU LEU ALA ALA ASN PRO PHE GLY GLN ALA SER ALA SEQRES 8 Y 101 SER ILE MET ALA ALA PHE MET ASP ASN PRO FORMUL 5 HOH *262(H2 O) HELIX 1 1 PRO V 5 ARG V 9 5 5 HELIX 2 2 PRO W 5 ARG W 9 5 5 HELIX 3 3 HIS X 353 ASN X 355 5 3 HELIX 4 4 HIS Y 353 ASN Y 355 5 3 SHEET 1 A 2 SER V 17 VAL V 22 0 SHEET 2 A 2 PHE V 53 CYS V 58 -1 N LYS V 57 O VAL V 18 SHEET 1 B 2 THR V 27 THR V 29 0 SHEET 2 B 2 GLU V 35 MET V 37 -1 N VAL V 36 O ALA V 28 SHEET 1 C 2 GLU V 41 ASN V 43 0 SHEET 2 C 2 VAL V 48 LYS V 50 -1 N PHE V 49 O VAL V 42 SHEET 1 D 2 TRP V 76 MET V 92 0 SHEET 2 D 2 ALA V 97 ARG V 114 -1 N SER V 113 O ASN V 77 SHEET 1 E 2 SER W 17 VAL W 22 0 SHEET 2 E 2 PHE W 53 CYS W 58 -1 N LYS W 57 O VAL W 18 SHEET 1 F 2 THR W 27 THR W 29 0 SHEET 2 F 2 GLU W 35 MET W 37 -1 N VAL W 36 O ALA W 28 SHEET 1 G 2 GLU W 41 ILE W 44 0 SHEET 2 G 2 SER W 47 LYS W 50 -1 N PHE W 49 O VAL W 42 SHEET 1 H 2 TRP W 76 MET W 92 0 SHEET 2 H 2 ALA W 97 ARG W 114 -1 N SER W 113 O ASN W 77 SHEET 1 I 4 SER X 287 LEU X 290 0 SHEET 2 I 4 TRP X 299 ASP X 306 -1 N ASP X 306 O SER X 287 SHEET 3 I 4 ARG X 342 LEU X 348 -1 N LEU X 348 O TRP X 299 SHEET 4 I 4 ILE X 328 PHE X 332 -1 N GLU X 331 O CYS X 345 SHEET 1 J 3 SER X 312 PHE X 317 0 SHEET 2 J 3 GLY X 357 ASN X 365 -1 N ALA X 364 O SER X 312 SHEET 3 J 3 GLY X 368 ALA X 376 -1 N ALA X 376 O GLY X 357 SHEET 1 K 4 SER Y 287 LEU Y 290 0 SHEET 2 K 4 TRP Y 299 ASP Y 306 -1 N ASP Y 306 O SER Y 287 SHEET 3 K 4 ARG Y 342 LEU Y 348 -1 N LEU Y 348 O TRP Y 299 SHEET 4 K 4 ILE Y 328 PHE Y 332 -1 N GLU Y 331 O CYS Y 345 SHEET 1 L 3 SER Y 312 PHE Y 317 0 SHEET 2 L 3 GLY Y 357 ASN Y 365 -1 N ALA Y 364 O SER Y 312 SHEET 3 L 3 GLY Y 368 ALA Y 376 -1 N ALA Y 376 O GLY Y 357 SSBOND 1 CYS V 15 CYS V 80 SSBOND 2 CYS V 58 CYS V 108 SSBOND 3 CYS V 68 CYS V 110 SSBOND 4 CYS W 15 CYS W 80 SSBOND 5 CYS W 58 CYS W 108 SSBOND 6 CYS W 68 CYS W 110 SSBOND 7 CYS X 300 CYS X 345 SSBOND 8 CYS Y 300 CYS Y 345 CISPEP 1 GLN X 308 PRO X 309 0 -0.36 CISPEP 2 GLN Y 308 PRO Y 309 0 0.49 CRYST1 58.245 53.735 77.101 90.00 107.34 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 0.017169 0.000000 0.005360 0.00000 SCALE2 0.000000 0.018610 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013587 0.00000 MTRIX1 1 0.581280 -0.312710 -0.751210 14.78126 1 MTRIX2 1 -0.290550 -0.942110 0.167300 0.82210 1 MTRIX3 1 -0.760060 0.121000 -0.638490 30.56634 1 MTRIX1 2 0.569520 -0.311990 -0.760470 14.76906 1 MTRIX2 2 -0.329310 -0.934280 0.136670 2.01039 1 MTRIX3 2 -0.753130 0.172590 -0.634830 30.27118 1