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HEADER SIGNALING PROTEIN 09-APR-03 1OZN TITLE 1.5A CRYSTAL STRUCTURE OF THE NOGO RECEPTOR LIGAND BINDING TITLE 2 DOMAIN REVEALS A CONVERGENT RECOGNITION SCAFFOLD MEDIATING TITLE 3 INHIBITION OF MYELINATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: RETICULON 4 RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN; COMPND 5 SYNONYM: NOGO RECEPTOR, NGR, NOGO-66 RECEPTOR; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 GENE: RTN4R OR NOGOR; SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: FUNGI; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HI5; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PACGP67A KEYWDS NOGO RECEPTOR, CRYSTAL STRUCTURE, MAD, MYELINATION KEYWDS 2 INHIBITION, OMGP, MAG, NOGO-66, P75, SIGNAL TRANSDUCTION, KEYWDS 3 NEURONAL REGENERATION, LIGAND BINDING EXPDTA X-RAY DIFFRACTION AUTHOR X.HE,J.F.BAZAN,J.B.PARK,G.MCDERMOTT,Z.HE,K.C.GARCIA REVDAT 1 20-MAY-03 1OZN 0 JRNL AUTH X.L.HE,J.F.BAZAN,G.MCDERMOTT,J.B.PARK,K.WANG, JRNL AUTH 2 M.TESSIER-LAVIGNE,Z.HE,K.C.GARCIA JRNL TITL STRUCTURE OF THE NOGO RECEPTOR ECTODOMAIN. A JRNL TITL 2 RECOGNITION MODULE IMPLICATED IN MYELIN INHIBITION. JRNL REF NEURON V. 38 177 2003 JRNL REFN ASTM NERNET US ISSN 0896-6273 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.52 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) : 1.52 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) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 32883 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) : 0.167 REMARK 3 FREE R VALUE : 0.198 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1634 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) : 1.52 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2140 REMARK 3 BIN FREE R VALUE : 0.2760 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 262 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2219 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 89 REMARK 3 SOLVENT ATOMS : 366 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 16.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.50 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.90000 REMARK 3 B22 (A**2) : 1.51000 REMARK 3 B33 (A**2) : -2.42000 REMARK 3 B12 (A**2) : -3.31000 REMARK 3 B13 (A**2) : -1.55000 REMARK 3 B23 (A**2) : 1.90000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.15 REMARK 3 ESD FROM SIGMAA (A) : 0.09 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) : 0.19 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14 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) : 26.50 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.99 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 1OZN 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 RCSB018843. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-DEC-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.00 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) : 1.0064, 1.0096, 0.9950 REMARK 200 MONOCHROMATOR : N/A 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 : 33484 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.520 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 (%) : 96.6 REMARK 200 DATA REDUNDANCY : 14.400 REMARK 200 R MERGE (I) : 0.05300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 34.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4 REMARK 200 DATA REDUNDANCY IN SHELL : 13.80 REMARK 200 R MERGE FOR SHELL (I) : 0.21400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 7.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 34.21 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, SODIUM CHLORIDE, SODIUM REMARK 280 ACETATE, PH 6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,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 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, Y, 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 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 ALA A 310 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 229 SD MET A 229 CE -0.109 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 VAL A 32 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 ASN A 115 N - CA - C ANGL. DEV. =-11.7 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 ARG A 119 -40.75 63.49 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 246 DISTANCE = 5.33 ANGSTROMS REMARK 525 HOH 301 DISTANCE = 5.53 ANGSTROMS REMARK 525 HOH 344 DISTANCE = 5.31 ANGSTROMS DBREF 1OZN A 26 310 UNP Q9BZR6 RT4R_HUMAN 26 310 SEQRES 1 A 285 PRO CYS PRO GLY ALA CYS VAL CYS TYR ASN GLU PRO LYS SEQRES 2 A 285 VAL THR THR SER CYS PRO GLN GLN GLY LEU GLN ALA VAL SEQRES 3 A 285 PRO VAL GLY ILE PRO ALA ALA SER GLN ARG ILE PHE LEU SEQRES 4 A 285 HIS GLY ASN ARG ILE SER HIS VAL PRO ALA ALA SER PHE SEQRES 5 A 285 ARG ALA CYS ARG ASN LEU THR ILE LEU TRP LEU HIS SER SEQRES 6 A 285 ASN VAL LEU ALA ARG ILE ASP ALA ALA ALA PHE THR GLY SEQRES 7 A 285 LEU ALA LEU LEU GLU GLN LEU ASP LEU SER ASP ASN ALA SEQRES 8 A 285 GLN LEU ARG SER VAL ASP PRO ALA THR PHE HIS GLY LEU SEQRES 9 A 285 GLY ARG LEU HIS THR LEU HIS LEU ASP ARG CYS GLY LEU SEQRES 10 A 285 GLN GLU LEU GLY PRO GLY LEU PHE ARG GLY LEU ALA ALA SEQRES 11 A 285 LEU GLN TYR LEU TYR LEU GLN ASP ASN ALA LEU GLN ALA SEQRES 12 A 285 LEU PRO ASP ASP THR PHE ARG ASP LEU GLY ASN LEU THR SEQRES 13 A 285 HIS LEU PHE LEU HIS GLY ASN ARG ILE SER SER VAL PRO SEQRES 14 A 285 GLU ARG ALA PHE ARG GLY LEU HIS SER LEU ASP ARG LEU SEQRES 15 A 285 LEU LEU HIS GLN ASN ARG VAL ALA HIS VAL HIS PRO HIS SEQRES 16 A 285 ALA PHE ARG ASP LEU GLY ARG LEU MET THR LEU TYR LEU SEQRES 17 A 285 PHE ALA ASN ASN LEU SER ALA LEU PRO THR GLU ALA LEU SEQRES 18 A 285 ALA PRO LEU ARG ALA LEU GLN TYR LEU ARG LEU ASN ASP SEQRES 19 A 285 ASN PRO TRP VAL CYS ASP CYS ARG ALA ARG PRO LEU TRP SEQRES 20 A 285 ALA TRP LEU GLN LYS PHE ARG GLY SER SER SER GLU VAL SEQRES 21 A 285 PRO CYS SER LEU PRO GLN ARG LEU ALA GLY ARG ASP LEU SEQRES 22 A 285 LYS ARG LEU ALA ALA ASN ASP LEU GLN GLY CYS ALA MODRES 1OZN ASN A 82 ASN GLYCOSYLATION SITE MODRES 1OZN ASN A 179 ASN GLYCOSYLATION SITE HET NDG Y 401 14 HET NDG Y 402 14 HET MAN Y 403 11 HET MAN Y 404 11 HET NAG Z 405 14 HET NDG Z 406 14 HET BMA Z 407 11 HET ACY 1 4 HET ACY 2 4 HET ACY 3 4 HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM ACY ACETIC ACID HETSYN NAG NAG FORMUL 2 NDG 3(C8 H15 N O6) FORMUL 2 MAN 2(C6 H12 O6) FORMUL 3 NAG C8 H15 N O6 FORMUL 3 BMA C6 H12 O6 FORMUL 4 ACY 3(C2 H4 O2) FORMUL 7 HOH *354(H2 O) HELIX 1 1 PRO A 242 ALA A 247 1 6 HELIX 2 2 ASP A 265 ARG A 267 5 3 HELIX 3 3 ALA A 268 PHE A 278 1 11 HELIX 4 4 PRO A 290 ALA A 294 5 5 HELIX 5 5 ASP A 297 LEU A 301 5 5 HELIX 6 6 ALA A 302 LEU A 306 5 5 SHEET 1 A12 VAL A 32 TYR A 34 0 SHEET 2 A12 THR A 40 SER A 42 -1 O SER A 42 N VAL A 32 SHEET 3 A12 ARG A 61 PHE A 63 1 O ARG A 61 N THR A 41 SHEET 4 A12 ILE A 85 TRP A 87 1 O TRP A 87 N ILE A 62 SHEET 5 A12 GLN A 109 ASP A 111 1 O GLN A 109 N LEU A 86 SHEET 6 A12 THR A 134 HIS A 136 1 O HIS A 136 N LEU A 110 SHEET 7 A12 TYR A 158 TYR A 160 1 O TYR A 160 N LEU A 135 SHEET 8 A12 HIS A 182 PHE A 184 1 O HIS A 182 N LEU A 159 SHEET 9 A12 ARG A 206 LEU A 208 1 O ARG A 206 N LEU A 183 SHEET 10 A12 THR A 230 TYR A 232 1 O THR A 230 N LEU A 207 SHEET 11 A12 TYR A 254 ARG A 256 1 O TYR A 254 N LEU A 231 SHEET 12 A12 SER A 281 SER A 282 1 O SER A 281 N LEU A 255 SHEET 1 B 2 HIS A 71 VAL A 72 0 SHEET 2 B 2 ARG A 95 ILE A 96 1 O ARG A 95 N VAL A 72 SHEET 1 C 2 SER A 192 VAL A 193 0 SHEET 2 C 2 HIS A 216 VAL A 217 1 O HIS A 216 N VAL A 193 SHEET 1 D 2 TRP A 262 VAL A 263 0 SHEET 2 D 2 CYS A 287 LEU A 289 1 O SER A 288 N TRP A 262 SSBOND 1 CYS A 27 CYS A 33 SSBOND 2 CYS A 31 CYS A 43 SSBOND 3 CYS A 264 CYS A 287 SSBOND 4 CYS A 266 CYS A 309 LINK ND2 ASN A 82 C1 NDG Y 401 LINK ND2 ASN A 179 C1 NAG Z 405 LINK O4 NDG Y 401 C1 NDG Y 402 LINK O4 NDG Y 402 C1 MAN Y 403 LINK O6 MAN Y 403 C1 MAN Y 404 LINK O4 NAG Z 405 C1 NDG Z 406 LINK O4 NDG Z 406 C1 BMA Z 407 CISPEP 1 GLU A 36 PRO A 37 0 0.24 CISPEP 2 LEU A 289 PRO A 290 0 -0.57 CRYST1 32.206 33.915 60.221 85.02 75.91 67.96 P 1 1 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 0.031050 -0.012570 -0.007857 0.00000 SCALE2 0.000000 0.031810 0.000161 0.00000 SCALE3 0.000000 0.000000 0.017121 0.00000