HEADER IMMUNE SYSTEM 20-AUG-24 9J8A TITLE STRUCTURE OF ANTIBODY BA8 IN COMPLEX WITH SULFATED PEPTIDE FROM CCR5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN OF BA8 FAB; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LIGHT CHAIN OF FAB BA8; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SULFATED PEPTIDE FROM CCR5; COMPND 11 CHAIN: P; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 3 ORGANISM_TAXID: 9986; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 9 ORGANISM_TAXID: 9986; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 13 MOL_ID: 3; SOURCE 14 SYNTHETIC: YES; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606 KEYWDS FAB, SULFATED PEPTIDE, CCR5, POST-TRANSLATIONAL MODIFICATION, RABBIT KEYWDS 2 IMMUNIZATION, PHAGE DISPLAY, HIV-1, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.M.M.CAAVEIRO,K.UJIIE,K.TSUMOTO REVDAT 1 02-JUL-25 9J8A 0 JRNL AUTH K.UJIIE,M.NAKAKIDO,S.KINOSHITA,J.M.M.CAAVEIRO, JRNL AUTH 2 C.K.ENTZMINGER,S.C.J.OKUMURA,T.MARUYAMA,K.MIYAUCHI,T.MATANO, JRNL AUTH 3 K.TSUMOTO JRNL TITL SPECIFIC RECOGNITION MECHANISM OF AN ANTIBODY TO SULFATED JRNL TITL 2 TYROSINE AND ITS POTENTIAL USE IN BIOLOGICAL RESEARCH. JRNL REF J.BIOL.CHEM. V. 301 08176 2025 JRNL REFN ESSN 1083-351X JRNL PMID 39798874 JRNL DOI 10.1016/J.JBC.2025.108176 REMARK 2 REMARK 2 RESOLUTION. 1.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0425 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.68 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 3 NUMBER OF REFLECTIONS : 40803 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 + TEST SET) : 0.167 REMARK 3 R VALUE (WORKING SET) : 0.165 REMARK 3 FREE R VALUE : 0.206 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1286 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2976 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.52 REMARK 3 BIN R VALUE (WORKING SET) : 0.2580 REMARK 3 BIN FREE R VALUE SET COUNT : 94 REMARK 3 BIN FREE R VALUE : 0.2890 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3323 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 433 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.63 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.78000 REMARK 3 B22 (A**2) : 1.64000 REMARK 3 B33 (A**2) : -0.84000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.06000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.113 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.111 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.600 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3447 ; 0.007 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 3091 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4741 ; 1.580 ; 1.784 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7161 ; 0.569 ; 1.716 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 454 ; 7.120 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 13 ;34.287 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 493 ;11.360 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 561 ; 0.079 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4041 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 751 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1804 ; 1.617 ; 1.753 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1804 ; 1.616 ; 1.753 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2253 ; 2.560 ; 3.139 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2254 ; 2.559 ; 3.139 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1643 ; 2.351 ; 1.940 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1642 ; 2.351 ; 1.940 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2486 ; 3.650 ; 3.464 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3774 ; 5.026 ;22.700 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3652 ; 4.904 ;21.670 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 9J8A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1300050605. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-DEC-21 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 : PHOTON FACTORY REMARK 200 BEAMLINE : BL-5A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20210323 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42109 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 REMARK 200 RESOLUTION RANGE LOW (A) : 40.680 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : 0.12800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.97600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.8.3 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.47 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 1000, 10% PEG 8,000, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K 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 35.47150 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 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: 4550 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20520 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, P 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 H 134 REMARK 465 SER H 135 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS H 216 CG CD CE NZ 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 ARG H 65 NE - CZ - NH2 ANGL. DEV. = -5.0 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 THR H 14 -17.60 85.29 REMARK 500 ASN H 42 -164.28 -117.33 REMARK 500 ARG H 65 17.23 -140.73 REMARK 500 PHE H 101 40.47 -105.46 REMARK 500 SER H 188 68.04 -111.67 REMARK 500 ASN H 202 55.06 36.24 REMARK 500 THR L 7 127.31 -38.78 REMARK 500 SER L 31 19.99 50.76 REMARK 500 LYS L 32 -18.17 77.77 REMARK 500 ALA L 53 -38.05 73.77 REMARK 500 ALA L 86 171.07 178.22 REMARK 500 TYR L 94 -168.62 -124.65 REMARK 500 ASP L 96 21.66 -141.63 REMARK 500 LYS L 140 71.61 52.13 REMARK 500 LYS L 191 -64.76 -104.17 REMARK 500 ASP P 4 51.91 -94.46 REMARK 500 REMARK 500 REMARK: NULL DBREF 9J8A H 1 226 PDB 9J8A 9J8A 1 226 DBREF 9J8A L 1 213 PDB 9J8A 9J8A 1 213 DBREF 9J8A P 1 11 PDB 9J8A 9J8A 1 11 SEQRES 1 H 226 GLN SER LEU GLU GLU SER GLY GLY GLY LEU PHE LYS PRO SEQRES 2 H 226 THR ASP THR LEU THR LEU THR CYS THR VAL SER GLY PHE SEQRES 3 H 226 SER LEU SER SER TYR SER ILE ARG TRP VAL ARG GLN ALA SEQRES 4 H 226 PRO GLY ASN GLY LEU GLU TRP ILE GLY ALA ILE GLY SER SEQRES 5 H 226 GLY GLY ASN ALA TYR TYR THR SER TRP ALA LYS SER ARG SEQRES 6 H 226 SER THR ILE THR ARG ASN THR ASN GLU ASN THR VAL THR SEQRES 7 H 226 LEU LYS MET THR SER LEU THR VAL ALA ASP THR ALA THR SEQRES 8 H 226 TYR PHE CYS ALA ARG GLY GLY ILE ASN PHE GLY ILE TRP SEQRES 9 H 226 GLY PRO GLY THR LEU VAL THR VAL SER SER GLY GLN PRO SEQRES 10 H 226 LYS ALA PRO SER VAL PHE PRO LEU ALA PRO CYS CYS GLY SEQRES 11 H 226 ASP THR PRO SER SER THR VAL THR LEU GLY CYS LEU VAL SEQRES 12 H 226 LYS GLY TYR LEU PRO GLU PRO VAL THR VAL THR TRP ASN SEQRES 13 H 226 SER GLY THR LEU THR ASN GLY VAL ARG THR PHE PRO SER SEQRES 14 H 226 VAL ARG GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 H 226 VAL SER VAL THR SER SER SER GLN PRO VAL THR CYS ASN SEQRES 16 H 226 VAL ALA HIS PRO ALA THR ASN THR LYS VAL ASP LYS THR SEQRES 17 H 226 VAL ALA PRO SER THR CYS SER LYS PRO GLY GLY SER HIS SEQRES 18 H 226 HIS HIS HIS HIS HIS SEQRES 1 L 213 ALA ALA VAL LEU THR GLN THR PRO SER PRO VAL SER ALA SEQRES 2 L 213 ALA VAL GLY SER THR VAL THR ILE ASN CYS GLN SER SER SEQRES 3 L 213 GLN SER VAL TYR SER LYS ASN TRP LEU SER TRP PHE GLN SEQRES 4 L 213 GLN LYS PRO GLY GLN PRO PRO LYS GLN LEU ILE TYR SER SEQRES 5 L 213 ALA SER THR LEU ASP SER GLY VAL PRO SER ARG PHE SER SEQRES 6 L 213 GLY SER GLY SER GLY THR GLN PHE THR LEU THR ILE SER SEQRES 7 L 213 GLY VAL GLN CYS ASP ASP ALA ALA THR TYR TYR CYS GLN SEQRES 8 L 213 GLY THR TYR GLY ASP ALA SER ALA PHE GLY GLY GLY THR SEQRES 9 L 213 GLU VAL VAL VAL LYS GLY ASP PRO VAL ALA PRO THR VAL SEQRES 10 L 213 LEU ILE PHE PRO PRO SER ALA ASP LEU VAL ALA THR GLY SEQRES 11 L 213 THR VAL THR ILE VAL CYS VAL ALA ASN LYS TYR PHE PRO SEQRES 12 L 213 ASP VAL THR VAL THR TRP GLU VAL ASP GLY THR THR GLN SEQRES 13 L 213 THR THR GLY ILE GLU ASN SER LYS THR PRO GLN ASN SER SEQRES 14 L 213 ALA ASP CYS THR TYR ASN LEU SER SER THR LEU THR LEU SEQRES 15 L 213 THR SER THR GLN TYR ASN SER HIS LYS GLU TYR THR CYS SEQRES 16 L 213 LYS VAL THR GLN GLY THR THR SER VAL VAL GLN SER PHE SEQRES 17 L 213 ASN ARG GLY ASP CYS SEQRES 1 P 11 PRO ILE TYS ASP ILE ASN TYS TYS THR SER GLU HET TYS P 3 16 HET TYS P 7 16 HET TYS P 8 16 HETNAM TYS O-SULFO-L-TYROSINE FORMUL 3 TYS 3(C9 H11 N O6 S) FORMUL 4 HOH *433(H2 O) HELIX 1 AA1 SER H 27 TYR H 31 5 5 HELIX 2 AA2 THR H 85 THR H 89 5 5 HELIX 3 AA3 SER H 157 THR H 159 5 3 HELIX 4 AA4 PRO H 199 ASN H 202 5 4 HELIX 5 AA5 VAL L 29 ASN L 33 5 5 HELIX 6 AA6 GLN L 81 ALA L 85 5 5 HELIX 7 AA7 SER L 123 ALA L 128 1 6 HELIX 8 AA8 SER L 184 ASN L 188 1 5 HELIX 9 AA9 GLY L 211 CYS L 213 5 3 HELIX 10 AB1 ASP P 4 TYS P 8 5 5 SHEET 1 AA1 4 SER H 2 SER H 6 0 SHEET 2 AA1 4 LEU H 17 SER H 24 -1 O THR H 22 N GLU H 4 SHEET 3 AA1 4 THR H 76 MET H 81 -1 O VAL H 77 N CYS H 21 SHEET 4 AA1 4 SER H 66 ASN H 71 -1 N THR H 69 O THR H 78 SHEET 1 AA2 6 GLY H 9 PHE H 11 0 SHEET 2 AA2 6 THR H 108 VAL H 112 1 O THR H 111 N GLY H 9 SHEET 3 AA2 6 ALA H 90 ARG H 96 -1 N ALA H 90 O VAL H 110 SHEET 4 AA2 6 ILE H 33 GLN H 38 -1 N VAL H 36 O PHE H 93 SHEET 5 AA2 6 LEU H 44 ILE H 50 -1 O GLY H 48 N TRP H 35 SHEET 6 AA2 6 ALA H 56 TYR H 58 -1 O TYR H 57 N ALA H 49 SHEET 1 AA3 4 SER H 121 LEU H 125 0 SHEET 2 AA3 4 VAL H 137 TYR H 146 -1 O LEU H 142 N PHE H 123 SHEET 3 AA3 4 TYR H 177 VAL H 185 -1 O LEU H 179 N VAL H 143 SHEET 4 AA3 4 ARG H 165 THR H 166 -1 N ARG H 165 O VAL H 182 SHEET 1 AA4 4 SER H 121 LEU H 125 0 SHEET 2 AA4 4 VAL H 137 TYR H 146 -1 O LEU H 142 N PHE H 123 SHEET 3 AA4 4 TYR H 177 VAL H 185 -1 O LEU H 179 N VAL H 143 SHEET 4 AA4 4 VAL H 170 ARG H 171 -1 N VAL H 170 O SER H 178 SHEET 1 AA5 3 THR H 152 TRP H 155 0 SHEET 2 AA5 3 VAL H 192 HIS H 198 -1 O ASN H 195 N THR H 154 SHEET 3 AA5 3 THR H 203 VAL H 209 -1 O VAL H 205 N VAL H 196 SHEET 1 AA6 4 LEU L 4 GLN L 6 0 SHEET 2 AA6 4 VAL L 19 SER L 25 -1 O GLN L 24 N THR L 5 SHEET 3 AA6 4 GLN L 72 ILE L 77 -1 O LEU L 75 N ILE L 21 SHEET 4 AA6 4 PHE L 64 SER L 69 -1 N SER L 65 O THR L 76 SHEET 1 AA7 6 VAL L 11 ALA L 14 0 SHEET 2 AA7 6 THR L 104 LYS L 109 1 O VAL L 107 N VAL L 11 SHEET 3 AA7 6 ALA L 86 THR L 93 -1 N ALA L 86 O VAL L 106 SHEET 4 AA7 6 LEU L 35 GLN L 40 -1 N PHE L 38 O TYR L 89 SHEET 5 AA7 6 LYS L 47 TYR L 51 -1 O LEU L 49 N TRP L 37 SHEET 6 AA7 6 THR L 55 LEU L 56 -1 O THR L 55 N TYR L 51 SHEET 1 AA8 4 VAL L 11 ALA L 14 0 SHEET 2 AA8 4 THR L 104 LYS L 109 1 O VAL L 107 N VAL L 11 SHEET 3 AA8 4 ALA L 86 THR L 93 -1 N ALA L 86 O VAL L 106 SHEET 4 AA8 4 SER L 98 PHE L 100 -1 O ALA L 99 N GLY L 92 SHEET 1 AA9 4 THR L 116 PHE L 120 0 SHEET 2 AA9 4 THR L 131 TYR L 141 -1 O VAL L 135 N PHE L 120 SHEET 3 AA9 4 TYR L 174 THR L 183 -1 O SER L 178 N CYS L 136 SHEET 4 AA9 4 ILE L 160 LYS L 164 -1 N SER L 163 O SER L 177 SHEET 1 AB1 4 THR L 154 THR L 155 0 SHEET 2 AB1 4 THR L 146 VAL L 151 -1 N VAL L 151 O THR L 154 SHEET 3 AB1 4 GLU L 192 GLN L 199 -1 O THR L 198 N THR L 146 SHEET 4 AB1 4 THR L 202 ASN L 209 -1 O PHE L 208 N TYR L 193 SSBOND 1 CYS H 21 CYS H 94 1555 1555 2.06 SSBOND 2 CYS H 128 CYS L 213 1555 1555 2.09 SSBOND 3 CYS H 129 CYS H 214 1555 1555 2.06 SSBOND 4 CYS H 141 CYS H 194 1555 1555 2.05 SSBOND 5 CYS L 23 CYS L 90 1555 1555 2.10 SSBOND 6 CYS L 82 CYS L 172 1555 1555 2.04 SSBOND 7 CYS L 136 CYS L 195 1555 1555 2.00 LINK C ILE P 2 N TYS P 3 1555 1555 1.34 LINK C TYS P 3 N ASP P 4 1555 1555 1.34 LINK C ASN P 6 N TYS P 7 1555 1555 1.34 LINK C TYS P 7 N TYS P 8 1555 1555 1.35 LINK C TYS P 8 N THR P 9 1555 1555 1.35 CISPEP 1 LEU H 147 PRO H 148 0 -4.63 CISPEP 2 GLU H 149 PRO H 150 0 -6.06 CISPEP 3 SER L 9 PRO L 10 0 -5.55 CISPEP 4 PHE L 142 PRO L 143 0 1.30 CRYST1 50.129 70.943 60.984 90.00 97.93 90.00 P 1 21 1 2 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 0.019949 0.000000 0.002780 0.00000 SCALE2 0.000000 0.014096 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016556 0.00000