HEADER VIRAL PROTEIN/IMMUNE SYSTEM 23-DEC-24 9MNS TITLE STRUCTURE OF HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 CORE FROM TITLE 2 GENOTYPE 6A BOUND TO BROADLY NEUTRALIZING ANTIBODY RM1-36 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RM1-36 FAB HEAVY CHAIN; COMPND 3 CHAIN: H, h; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RM1-36 FAB LIGHT CHAIN; COMPND 7 CHAIN: L, l; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN E2; COMPND 11 CHAIN: E, B; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 4 ORGANISM_TAXID: 9544; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 10 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 11 ORGANISM_TAXID: 9544; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: RECOMBINANT HEPATITIS C VIRUS HK6A/JFH-1; SOURCE 17 ORGANISM_TAXID: 595609; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR T.K.Y.NGUYEN,R.L.STANFIELD,I.A.WILSON REVDAT 1 14-JAN-26 9MNS 0 JRNL AUTH T.K.Y.NGUYEN JRNL TITL STRUCTURE OF HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 CORE JRNL TITL 2 FROM GENOTYPE 6A BOUND TO BROADLY NEUTRALIZING ANTIBODY JRNL TITL 3 RM1-36 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.89 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.87 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1 REMARK 3 NUMBER OF REFLECTIONS : 41933 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.233 REMARK 3 R VALUE (WORKING SET) : 0.232 REMARK 3 FREE R VALUE : 0.250 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880 REMARK 3 FREE R VALUE TEST SET COUNT : 2047 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 44.8700 - 7.1200 1.00 2747 140 0.1929 0.2004 REMARK 3 2 7.1200 - 5.6600 1.00 2718 131 0.2196 0.2258 REMARK 3 3 5.6600 - 4.9400 1.00 2687 151 0.1777 0.1871 REMARK 3 4 4.9400 - 4.4900 1.00 2764 114 0.1710 0.1614 REMARK 3 5 4.4900 - 4.1700 1.00 2692 164 0.1948 0.2212 REMARK 3 6 4.1700 - 3.9200 1.00 2668 164 0.2318 0.2617 REMARK 3 7 3.9200 - 3.7300 0.98 2624 141 0.2851 0.3460 REMARK 3 8 3.7300 - 3.5600 0.99 2673 163 0.3089 0.3145 REMARK 3 9 3.5600 - 3.4300 0.99 2703 128 0.3284 0.3606 REMARK 3 10 3.4300 - 3.3100 1.00 2672 116 0.2856 0.3321 REMARK 3 11 3.3100 - 3.2100 1.00 2722 137 0.2845 0.3013 REMARK 3 12 3.2100 - 3.1100 1.00 2714 108 0.2949 0.3530 REMARK 3 13 3.1100 - 3.0300 0.99 2668 140 0.3253 0.3475 REMARK 3 14 3.0300 - 2.9600 0.98 2632 134 0.3634 0.4434 REMARK 3 15 2.9600 - 2.8900 0.81 2202 116 0.4273 0.4369 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.509 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.176 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 88.63 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 92.78 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 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.005 9371 REMARK 3 ANGLE : 1.163 12768 REMARK 3 CHIRALITY : 0.073 1449 REMARK 3 PLANARITY : 0.007 1617 REMARK 3 DIHEDRAL : 12.804 3331 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9MNS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291418. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-SEP-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42383 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 6.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.7400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.99 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M TRI-SODIUM CITRATE, 20% W/V REMARK 280 PEG3350, EVAPORATION, TEMPERATURE 293K 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,Y+1/2,-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 111.77250 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5840 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27840 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, E 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27860 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: l, h, B 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 PRO E 452A REMARK 465 GLU E 452B REMARK 465 ARG E 452C REMARK 465 MET E 452D REMARK 465 ALA E 452E REMARK 465 ALA E 452F REMARK 465 CYS E 452G REMARK 465 LYS E 452H REMARK 465 PRO E 452I REMARK 465 LEU E 452J REMARK 465 ALA E 452K REMARK 465 ASP E 452L REMARK 465 PHE E 452M REMARK 465 ARG E 452N REMARK 465 GLN E 452O REMARK 465 GLY E 452P REMARK 465 TRP E 452Q REMARK 465 GLY E 452R REMARK 465 GLN E 452S REMARK 465 ILE E 452T REMARK 465 THR E 452U REMARK 465 TYR E 452V REMARK 465 LYS E 452W REMARK 465 VAL E 452X REMARK 465 ASN E 452Y REMARK 465 ILE E 452Z REMARK 465 SER E 453A REMARK 465 GLY E 453B REMARK 465 PRO E 453C REMARK 465 SER E 453D REMARK 465 ASP E 453E REMARK 465 ASP E 453F REMARK 465 ARG E 453G REMARK 465 PRO E 453H REMARK 465 TYR E 453I REMARK 465 CYS E 453J REMARK 465 TRP E 453K REMARK 465 HIS E 453L REMARK 465 TYR E 453M REMARK 465 ALA E 453N REMARK 465 PRO E 453O REMARK 465 CYS E 568A REMARK 465 GLN E 568B REMARK 465 ILE E 568C REMARK 465 VAL E 568D REMARK 465 PRO E 568E REMARK 465 GLY E 568F REMARK 465 ASP E 568G REMARK 465 TYR E 568H REMARK 465 ASN E 568I REMARK 465 SER E 568J REMARK 465 SER E 568K REMARK 465 ALA E 568L REMARK 465 ASN E 568M REMARK 465 GLU E 568N REMARK 465 LEU E 568O REMARK 465 LEU E 568P REMARK 465 CYS E 568Q REMARK 465 PRO E 568R REMARK 465 THR E 568S REMARK 465 ASP E 568T REMARK 465 CYS E 568U REMARK 465 PHE E 568V REMARK 465 ARG E 568W REMARK 465 LYS E 568X REMARK 465 HIS E 568Y REMARK 465 PRO E 568Z REMARK 465 GLU E 569A REMARK 465 ALA E 569B REMARK 465 THR E 569C REMARK 465 PRO E 569D REMARK 465 HIS B 421 REMARK 465 PRO B 452A REMARK 465 GLU B 452B REMARK 465 ARG B 452C REMARK 465 MET B 452D REMARK 465 ALA B 452E REMARK 465 ALA B 452F REMARK 465 CYS B 452G REMARK 465 LYS B 452H REMARK 465 PRO B 452I REMARK 465 LEU B 452J REMARK 465 ALA B 452K REMARK 465 ASP B 452L REMARK 465 PHE B 452M REMARK 465 ARG B 452N REMARK 465 GLN B 452O REMARK 465 GLY B 452P REMARK 465 TRP B 452Q REMARK 465 GLY B 452R REMARK 465 GLN B 452S REMARK 465 ILE B 452T REMARK 465 THR B 452U REMARK 465 TYR B 452V REMARK 465 LYS B 452W REMARK 465 VAL B 452X REMARK 465 ASN B 452Y REMARK 465 ILE B 452Z REMARK 465 SER B 453A REMARK 465 GLY B 453B REMARK 465 PRO B 453C REMARK 465 SER B 453D REMARK 465 ASP B 453E REMARK 465 ASP B 453F REMARK 465 ARG B 453G REMARK 465 PRO B 453H REMARK 465 TYR B 453I REMARK 465 CYS B 453J REMARK 465 TRP B 453K REMARK 465 HIS B 453L REMARK 465 TYR B 453M REMARK 465 ALA B 453N REMARK 465 PRO B 453O REMARK 465 PRO B 567A REMARK 465 CYS B 567B REMARK 465 GLN B 567C REMARK 465 ILE B 567D REMARK 465 VAL B 567E REMARK 465 PRO B 567F REMARK 465 GLY B 567G REMARK 465 ASP B 567H REMARK 465 TYR B 567I REMARK 465 ASN B 567J REMARK 465 SER B 567K REMARK 465 SER B 567L REMARK 465 ALA B 567M REMARK 465 ASN B 567N REMARK 465 GLU B 567O REMARK 465 LEU B 567P REMARK 465 LEU B 567Q REMARK 465 CYS B 567R REMARK 465 PRO B 567S REMARK 465 THR B 567T REMARK 465 ASP B 567U REMARK 465 CYS B 567V REMARK 465 PHE B 567W REMARK 465 ARG B 567X REMARK 465 LYS B 567Y REMARK 465 HIS B 567Z REMARK 465 PRO B 568A REMARK 465 GLU B 568B REMARK 465 ALA B 568C REMARK 465 THR B 568D 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 PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS H 140 CA - CB - SG ANGL. DEV. = 8.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER H 7 -156.91 -74.30 REMARK 500 ALA H 16 -164.36 -101.31 REMARK 500 SER H 30 -128.29 54.08 REMARK 500 MET H 48 -77.31 -92.72 REMARK 500 THR H 76 58.72 36.69 REMARK 500 SER H 113 31.85 -94.01 REMARK 500 THR H 131 -63.76 39.96 REMARK 500 ASP H 144 78.46 62.90 REMARK 500 GLN L 27 -164.62 -107.45 REMARK 500 SER L 30 -111.11 54.13 REMARK 500 TYR L 32 38.60 -76.30 REMARK 500 SER L 52 -28.10 -161.79 REMARK 500 ALA L 84 -163.30 -163.50 REMARK 500 ASN L 138 78.35 58.43 REMARK 500 GLN l 27 -163.68 -108.43 REMARK 500 SER l 30 -111.31 54.31 REMARK 500 TYR l 32 38.59 -77.22 REMARK 500 ALA l 51 15.02 55.08 REMARK 500 SER l 52 -31.51 -160.79 REMARK 500 ALA l 84 -163.66 -163.45 REMARK 500 ASN l 138 78.50 57.87 REMARK 500 SER h 7 -156.55 -74.29 REMARK 500 ALA h 16 -164.32 -101.60 REMARK 500 SER h 30 -127.67 53.50 REMARK 500 MET h 48 -77.55 -92.97 REMARK 500 THR h 76 59.22 36.94 REMARK 500 SER h 113 32.39 -93.97 REMARK 500 THR h 131 -137.37 41.00 REMARK 500 ASP h 144 77.94 62.78 REMARK 500 ASN E 446 -148.47 -103.84 REMARK 500 ASP E 495 -101.40 -122.85 REMARK 500 THR E 519 -157.06 -129.08 REMARK 500 GLU E 540 -69.40 -23.05 REMARK 500 SER E 541 -60.57 -24.50 REMARK 500 ARG E 543 108.32 -37.92 REMARK 500 SER E 599 -74.10 -80.85 REMARK 500 LYS B 445 -158.89 -78.06 REMARK 500 ASN B 446 -145.08 -103.36 REMARK 500 ASP B 495 -100.36 -125.55 REMARK 500 THR B 519 -156.48 -129.39 REMARK 500 GLU B 540 -69.42 -22.87 REMARK 500 SER B 541 -59.25 -23.93 REMARK 500 ARG B 543 108.77 -36.07 REMARK 500 SER B 599 -73.86 -80.17 REMARK 500 REMARK 500 REMARK: NULL DBREF 9MNS H 2 214 PDB 9MNS 9MNS 2 214 DBREF 9MNS L 1 211 PDB 9MNS 9MNS 1 211 DBREF 9MNS l 1 211 PDB 9MNS 9MNS 1 211 DBREF 9MNS h 2 214 PDB 9MNS 9MNS 2 214 DBREF 9MNS E 421 645 UNP B9V0E2 B9V0E2_9HEPC 421 651 DBREF 9MNS B 421 645 UNP B9V0E2 B9V0E2_9HEPC 421 651 SEQADV 9MNS ASP E 448 UNP B9V0E2 ASN 448 CONFLICT SEQADV 9MNS PRO E 569D UNP B9V0E2 TYR 600 CONFLICT SEQADV 9MNS THR E 583 UNP B9V0E2 GLN 601 CONFLICT SEQADV 9MNS ASP E 584 UNP B9V0E2 ARG 602 CONFLICT SEQADV 9MNS GLY E 591 UNP B9V0E2 CYS 603 CONFLICT SEQADV 9MNS ASP B 448 UNP B9V0E2 ASN 448 CONFLICT SEQADV 9MNS PRO B 582 UNP B9V0E2 TYR 600 CONFLICT SEQADV 9MNS THR B 583 UNP B9V0E2 GLN 601 CONFLICT SEQADV 9MNS ASP B 584 UNP B9V0E2 ARG 602 CONFLICT SEQADV 9MNS GLY B 591 UNP B9V0E2 CYS 603 CONFLICT SEQRES 1 H 222 VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS PRO SEQRES 2 H 222 GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY PHE SEQRES 3 H 222 THR PHE SER ILE TYR ALA ILE CYS TRP VAL ARG GLN ALA SEQRES 4 H 222 PRO GLY GLN GLY LEU GLU TRP MET GLY GLU ILE ILE PRO SEQRES 5 H 222 ARG VAL GLY LEU THR THR TYR ALA GLN LYS PHE GLN GLY SEQRES 6 H 222 ARG VAL THR ILE THR ALA ASP THR SER THR THR THR VAL SEQRES 7 H 222 TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR ALA SEQRES 8 H 222 VAL TYR TYR CYS VAL ARG GLY PRO ARG TYR SER GLU TYR SEQRES 9 H 222 SER TYR ARG ALA SER TRP PHE ASP VAL TRP GLY PRO GLY SEQRES 10 H 222 VAL LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 222 SER VAL PHE PRO LEU ALA PRO SER THR SER GLY GLY THR SEQRES 12 H 222 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 222 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 222 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 222 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 222 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 222 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 H 222 LYS SEQRES 1 L 211 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 211 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 211 GLN GLY ILE SER SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 211 PRO GLY LYS ALA PRO LYS PRO LEU ILE TYR TYR ALA SER SEQRES 5 L 211 ASN LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 211 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 211 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 211 ASN SER ASP PRO TYR SER PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 211 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 211 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 211 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 211 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 211 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 211 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 211 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 211 VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE ASN SEQRES 17 L 211 ARG GLY GLU SEQRES 1 l 211 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 l 211 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 l 211 GLN GLY ILE SER SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 l 211 PRO GLY LYS ALA PRO LYS PRO LEU ILE TYR TYR ALA SER SEQRES 5 l 211 ASN LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 l 211 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 l 211 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 l 211 ASN SER ASP PRO TYR SER PHE GLY GLN GLY THR LYS VAL SEQRES 9 l 211 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 l 211 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 l 211 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 l 211 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 l 211 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 l 211 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 l 211 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 l 211 VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE ASN SEQRES 17 l 211 ARG GLY GLU SEQRES 1 h 222 VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS PRO SEQRES 2 h 222 GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY PHE SEQRES 3 h 222 THR PHE SER ILE TYR ALA ILE CYS TRP VAL ARG GLN ALA SEQRES 4 h 222 PRO GLY GLN GLY LEU GLU TRP MET GLY GLU ILE ILE PRO SEQRES 5 h 222 ARG VAL GLY LEU THR THR TYR ALA GLN LYS PHE GLN GLY SEQRES 6 h 222 ARG VAL THR ILE THR ALA ASP THR SER THR THR THR VAL SEQRES 7 h 222 TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR ALA SEQRES 8 h 222 VAL TYR TYR CYS VAL ARG GLY PRO ARG TYR SER GLU TYR SEQRES 9 h 222 SER TYR ARG ALA SER TRP PHE ASP VAL TRP GLY PRO GLY SEQRES 10 h 222 VAL LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 h 222 SER VAL PHE PRO LEU ALA PRO SER THR SER GLY GLY THR SEQRES 12 h 222 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 h 222 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 h 222 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 h 222 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 h 222 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 h 222 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 h 222 LYS SEQRES 1 E 231 HIS ILE ASN ARG THR ALA LEU ASN CYS ASN ASP SER LEU SEQRES 2 E 231 GLN THR GLY PHE ILE THR SER LEU PHE TYR ALA LYS ASN SEQRES 3 E 231 VAL ASP SER SER GLY CYS PRO GLU ARG MET ALA ALA CYS SEQRES 4 E 231 LYS PRO LEU ALA ASP PHE ARG GLN GLY TRP GLY GLN ILE SEQRES 5 E 231 THR TYR LYS VAL ASN ILE SER GLY PRO SER ASP ASP ARG SEQRES 6 E 231 PRO TYR CYS TRP HIS TYR ALA PRO ARG PRO CYS ASP VAL SEQRES 7 E 231 VAL SER ALA ARG THR VAL CYS GLY PRO VAL TYR CYS PHE SEQRES 8 E 231 THR PRO SER PRO VAL VAL VAL GLY THR THR ASP LYS LEU SEQRES 9 E 231 GLY ILE PRO THR TYR ASN TRP GLY GLU ASN GLU THR ASP SEQRES 10 E 231 VAL PHE MET LEU GLU SER LEU ARG PRO PRO THR GLY GLY SEQRES 11 E 231 TRP PHE GLY CYS THR TRP MET ASN SER THR GLY PHE THR SEQRES 12 E 231 LYS THR CYS GLY ALA PRO PRO CYS GLN ILE VAL PRO GLY SEQRES 13 E 231 ASP TYR ASN SER SER ALA ASN GLU LEU LEU CYS PRO THR SEQRES 14 E 231 ASP CYS PHE ARG LYS HIS PRO GLU ALA THR PRO THR ASP SEQRES 15 E 231 GLY GLY SER GLY PRO TRP ILE THR PRO ARG CYS LEU VAL SEQRES 16 E 231 ASP TYR PRO TYR ARG LEU TRP HIS TYR PRO CYS THR VAL SEQRES 17 E 231 ASN PHE THR LEU HIS LYS VAL ARG MET PHE VAL GLY GLY SEQRES 18 E 231 ILE GLU HIS ARG PHE ASP ALA ALA CYS ASN SEQRES 1 B 231 HIS ILE ASN ARG THR ALA LEU ASN CYS ASN ASP SER LEU SEQRES 2 B 231 GLN THR GLY PHE ILE THR SER LEU PHE TYR ALA LYS ASN SEQRES 3 B 231 VAL ASP SER SER GLY CYS PRO GLU ARG MET ALA ALA CYS SEQRES 4 B 231 LYS PRO LEU ALA ASP PHE ARG GLN GLY TRP GLY GLN ILE SEQRES 5 B 231 THR TYR LYS VAL ASN ILE SER GLY PRO SER ASP ASP ARG SEQRES 6 B 231 PRO TYR CYS TRP HIS TYR ALA PRO ARG PRO CYS ASP VAL SEQRES 7 B 231 VAL SER ALA ARG THR VAL CYS GLY PRO VAL TYR CYS PHE SEQRES 8 B 231 THR PRO SER PRO VAL VAL VAL GLY THR THR ASP LYS LEU SEQRES 9 B 231 GLY ILE PRO THR TYR ASN TRP GLY GLU ASN GLU THR ASP SEQRES 10 B 231 VAL PHE MET LEU GLU SER LEU ARG PRO PRO THR GLY GLY SEQRES 11 B 231 TRP PHE GLY CYS THR TRP MET ASN SER THR GLY PHE THR SEQRES 12 B 231 LYS THR CYS GLY ALA PRO PRO CYS GLN ILE VAL PRO GLY SEQRES 13 B 231 ASP TYR ASN SER SER ALA ASN GLU LEU LEU CYS PRO THR SEQRES 14 B 231 ASP CYS PHE ARG LYS HIS PRO GLU ALA THR PRO THR ASP SEQRES 15 B 231 GLY GLY SER GLY PRO TRP ILE THR PRO ARG CYS LEU VAL SEQRES 16 B 231 ASP TYR PRO TYR ARG LEU TRP HIS TYR PRO CYS THR VAL SEQRES 17 B 231 ASN PHE THR LEU HIS LYS VAL ARG MET PHE VAL GLY GLY SEQRES 18 B 231 ILE GLU HIS ARG PHE ASP ALA ALA CYS ASN HET NAG E 701 14 HET NAG E 702 14 HET NAG E 703 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 7 NAG 6(C8 H15 N O6) HELIX 1 AA1 GLN H 61 GLN H 64 5 4 HELIX 2 AA2 ARG H 83 THR H 87 5 5 HELIX 3 AA3 TYR H 98 SER H 100B 5 5 HELIX 4 AA4 SER H 156 ALA H 158 5 3 HELIX 5 AA5 SER H 187 LEU H 189 5 3 HELIX 6 AA6 LYS H 201 ASN H 204 5 4 HELIX 7 AA7 GLN L 79 PHE L 83 5 5 HELIX 8 AA8 SER L 121 LYS L 126 1 6 HELIX 9 AA9 LYS L 183 LYS L 188 1 6 HELIX 10 AB1 GLN l 79 PHE l 83 5 5 HELIX 11 AB2 SER l 121 LYS l 126 1 6 HELIX 12 AB3 LYS l 183 LYS l 188 1 6 HELIX 13 AB4 GLN h 61 GLN h 64 5 4 HELIX 14 AB5 ARG h 83 THR h 87 5 5 HELIX 15 AB6 SER h 156 ALA h 158 5 3 HELIX 16 AB7 SER h 187 LEU h 189 5 3 HELIX 17 AB8 LYS h 201 ASN h 204 5 4 HELIX 18 AB9 HIS E 421 THR E 425 5 5 HELIX 19 AC1 ILE E 438 TYR E 443 1 6 HELIX 20 AC2 LEU E 539 ARG E 543 1 5 HELIX 21 AC3 TYR E 613 TYR E 618 1 6 HELIX 22 AC4 PRO E 619 PHE E 624 5 6 HELIX 23 AC5 ILE B 438 TYR B 443 1 6 HELIX 24 AC6 LEU B 539 ARG B 543 1 5 HELIX 25 AC7 TYR B 613 TYR B 618 1 6 HELIX 26 AC8 PRO B 619 PHE B 624 5 6 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 SER H 17 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 SER H 82A-1 O MET H 80 N LEU H 20 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA2 6 GLU H 10 LYS H 12 0 SHEET 2 AA2 6 VAL H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA2 6 ALA H 88 PRO H 96 -1 N TYR H 90 O VAL H 107 SHEET 4 AA2 6 TYR H 32 GLN H 39 -1 N ALA H 33 O GLY H 95 SHEET 5 AA2 6 LEU H 45 ILE H 52 -1 O MET H 48 N TRP H 36 SHEET 6 AA2 6 LEU H 56 TYR H 59 -1 O THR H 58 N GLU H 50 SHEET 1 AA3 4 SER H 120 LEU H 124 0 SHEET 2 AA3 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA3 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AA3 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AA4 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA5 3 THR H 151 TRP H 154 0 SHEET 2 AA5 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA5 3 THR H 205 LYS H 210 -1 O THR H 205 N HIS H 200 SHEET 1 AA6 4 MET L 4 SER L 7 0 SHEET 2 AA6 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA6 4 GLU L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA6 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AA7 6 SER L 10 SER L 12 0 SHEET 2 AA7 6 THR L 102 GLU L 105 1 O GLU L 105 N LEU L 11 SHEET 3 AA7 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA7 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AA7 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA7 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AA8 4 SER L 114 PHE L 118 0 SHEET 2 AA8 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AA8 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AA8 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AA9 3 LYS L 145 VAL L 150 0 SHEET 2 AA9 3 VAL L 191 THR L 197 -1 O THR L 197 N LYS L 145 SHEET 3 AA9 3 SER L 202 ASN L 208 -1 O VAL L 203 N VAL L 196 SHEET 1 AB1 4 MET l 4 SER l 7 0 SHEET 2 AB1 4 VAL l 19 ALA l 25 -1 O ARG l 24 N THR l 5 SHEET 3 AB1 4 GLU l 70 ILE l 75 -1 O LEU l 73 N ILE l 21 SHEET 4 AB1 4 PHE l 62 SER l 67 -1 N SER l 63 O THR l 74 SHEET 1 AB2 6 SER l 10 SER l 12 0 SHEET 2 AB2 6 THR l 102 GLU l 105 1 O GLU l 105 N LEU l 11 SHEET 3 AB2 6 THR l 85 GLN l 90 -1 N TYR l 86 O THR l 102 SHEET 4 AB2 6 LEU l 33 GLN l 38 -1 N ALA l 34 O GLN l 89 SHEET 5 AB2 6 LYS l 45 TYR l 49 -1 O LYS l 45 N GLN l 37 SHEET 6 AB2 6 ASN l 53 LEU l 54 -1 O ASN l 53 N TYR l 49 SHEET 1 AB3 4 SER l 114 PHE l 118 0 SHEET 2 AB3 4 THR l 129 PHE l 139 -1 O LEU l 135 N PHE l 116 SHEET 3 AB3 4 TYR l 173 SER l 182 -1 O LEU l 181 N ALA l 130 SHEET 4 AB3 4 SER l 159 VAL l 163 -1 N GLN l 160 O THR l 178 SHEET 1 AB4 3 LYS l 145 VAL l 150 0 SHEET 2 AB4 3 VAL l 191 GLN l 198 -1 O THR l 197 N LYS l 145 SHEET 3 AB4 3 THR l 201 ASN l 208 -1 O LYS l 205 N CYS l 194 SHEET 1 AB5 4 GLN h 3 GLN h 6 0 SHEET 2 AB5 4 SER h 17 SER h 25 -1 O LYS h 23 N VAL h 5 SHEET 3 AB5 4 THR h 77 SER h 82A-1 O MET h 80 N LEU h 20 SHEET 4 AB5 4 VAL h 67 ASP h 72 -1 N ASP h 72 O THR h 77 SHEET 1 AB6 6 GLU h 10 LYS h 12 0 SHEET 2 AB6 6 VAL h 107 VAL h 111 1 O THR h 110 N LYS h 12 SHEET 3 AB6 6 ALA h 88 PRO h 96 -1 N TYR h 90 O VAL h 107 SHEET 4 AB6 6 TYR h 32 GLN h 39 -1 N ALA h 33 O GLY h 95 SHEET 5 AB6 6 LEU h 45 ILE h 52 -1 O ILE h 51 N ILE h 34 SHEET 6 AB6 6 LEU h 56 TYR h 59 -1 O THR h 58 N GLU h 50 SHEET 1 AB7 4 SER h 120 LEU h 124 0 SHEET 2 AB7 4 THR h 135 TYR h 145 -1 O LEU h 141 N PHE h 122 SHEET 3 AB7 4 TYR h 176 PRO h 185 -1 O VAL h 184 N ALA h 136 SHEET 4 AB7 4 VAL h 163 THR h 165 -1 N HIS h 164 O VAL h 181 SHEET 1 AB8 4 SER h 120 LEU h 124 0 SHEET 2 AB8 4 THR h 135 TYR h 145 -1 O LEU h 141 N PHE h 122 SHEET 3 AB8 4 TYR h 176 PRO h 185 -1 O VAL h 184 N ALA h 136 SHEET 4 AB8 4 VAL h 169 LEU h 170 -1 N VAL h 169 O SER h 177 SHEET 1 AB9 3 THR h 151 TRP h 154 0 SHEET 2 AB9 3 TYR h 194 HIS h 200 -1 O ASN h 197 N SER h 153 SHEET 3 AB9 3 THR h 205 VAL h 211 -1 O THR h 205 N HIS h 200 SHEET 1 AC1 2 ALA E 426 LEU E 427 0 SHEET 2 AC1 2 CYS E 503 GLY E 504 -1 O GLY E 504 N ALA E 426 SHEET 1 AC2 2 VAL E 496 SER E 498 0 SHEET 2 AC2 2 VAL E 536 MET E 538 -1 O PHE E 537 N VAL E 497 SHEET 1 AC3 4 PRO E 513 VAL E 516 0 SHEET 2 AC3 4 VAL E 506 PHE E 509 -1 N CYS E 508 O VAL E 514 SHEET 3 AC3 4 GLY E 551 MET E 555 -1 O THR E 553 N TYR E 507 SHEET 4 AC3 4 THR E 561 GLY E 565 -1 O LYS E 562 N TRP E 554 SHEET 1 AC4 3 LEU E 608 VAL E 609 0 SHEET 2 AC4 3 GLU E 637 CYS E 644 -1 O ALA E 643 N LEU E 608 SHEET 3 AC4 3 THR E 625 PHE E 632 -1 N THR E 625 O CYS E 644 SHEET 1 AC5 2 ALA B 426 LEU B 427 0 SHEET 2 AC5 2 CYS B 503 GLY B 504 -1 O GLY B 504 N ALA B 426 SHEET 1 AC6 2 VAL B 496 SER B 498 0 SHEET 2 AC6 2 VAL B 536 MET B 538 -1 O PHE B 537 N VAL B 497 SHEET 1 AC7 4 PRO B 513 VAL B 516 0 SHEET 2 AC7 4 VAL B 506 PHE B 509 -1 N CYS B 508 O VAL B 514 SHEET 3 AC7 4 GLY B 551 MET B 555 -1 O THR B 553 N TYR B 507 SHEET 4 AC7 4 THR B 561 GLY B 565 -1 O LYS B 562 N TRP B 554 SHEET 1 AC8 3 LEU B 608 VAL B 609 0 SHEET 2 AC8 3 GLU B 637 CYS B 644 -1 O ALA B 643 N LEU B 608 SHEET 3 AC8 3 THR B 625 PHE B 632 -1 N MET B 631 O HIS B 638 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.05 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 5 CYS l 23 CYS l 88 1555 1555 2.04 SSBOND 6 CYS l 134 CYS l 194 1555 1555 2.03 SSBOND 7 CYS h 22 CYS h 92 1555 1555 2.03 SSBOND 8 CYS h 140 CYS h 196 1555 1555 2.04 SSBOND 9 CYS E 429 CYS E 503 1555 1555 2.03 SSBOND 10 CYS E 452 CYS E 620 1555 1555 2.04 SSBOND 11 CYS E 494 CYS E 564 1555 1555 2.03 SSBOND 12 CYS E 508 CYS E 552 1555 1555 2.03 SSBOND 13 CYS E 607 CYS E 644 1555 1555 2.03 SSBOND 14 CYS B 429 CYS B 503 1555 1555 2.03 SSBOND 15 CYS B 452 CYS B 620 1555 1555 2.04 SSBOND 16 CYS B 494 CYS B 564 1555 1555 2.03 SSBOND 17 CYS B 508 CYS B 552 1555 1555 2.03 SSBOND 18 CYS B 607 CYS B 644 1555 1555 2.04 LINK ND2 ASN E 532 C1 NAG E 703 1555 1555 1.45 LINK ND2 ASN E 556 C1 NAG E 701 1555 1555 1.46 LINK ND2 ASN E 623 C1 NAG E 702 1555 1555 1.44 LINK ND2 ASN B 532 C1 NAG B 702 1555 1555 1.44 LINK ND2 ASN B 556 C1 NAG B 701 1555 1555 1.45 LINK ND2 ASN B 623 C1 NAG B 703 1555 1555 1.44 CISPEP 1 PHE H 146 PRO H 147 0 -5.21 CISPEP 2 GLU H 148 PRO H 149 0 0.15 CISPEP 3 SER L 7 PRO L 8 0 -3.73 CISPEP 4 ASP L 94 PRO L 95 0 0.40 CISPEP 5 TYR L 140 PRO L 141 0 2.42 CISPEP 6 SER l 7 PRO l 8 0 -3.71 CISPEP 7 ASP l 94 PRO l 95 0 -0.27 CISPEP 8 TYR l 140 PRO l 141 0 2.83 CISPEP 9 PHE h 146 PRO h 147 0 -4.93 CISPEP 10 GLU h 148 PRO h 149 0 0.24 CISPEP 11 THR E 510 PRO E 511 0 -7.50 CISPEP 12 THR B 510 PRO B 511 0 -7.24 CRYST1 59.751 223.545 73.296 90.00 93.58 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 0.016736 0.000000 0.001047 0.00000 SCALE2 0.000000 0.004473 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013670 0.00000