HEADER IMMUNE SYSTEM 19-JUL-24 9G6R TITLE FAB-IP8 IN COMPLEX WITH ROCURONIUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB-IP8 HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB-IP8 LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK 293-F CELLS; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HEK 293-F CELLS KEYWDS IMMUNOTHERAPY, ANAPHYLAXIS, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.HAOUZ,F.A.SAUL,P.BRUHNS REVDAT 1 12-FEB-25 9G6R 0 JRNL AUTH A.DEJOUX,Q.ZHU,A.WOOLFE,O.GODON,S.ELLOUZE,G.MOTTET, JRNL AUTH 2 C.CASTRILLON,C.GILLIS,C.PECALVEL,C.GANNEAU,B.IANNASCOLI, JRNL AUTH 3 F.LEMOINE,F.SAUL,P.ENGLAND,L.L.REBER,A.GOUEL-CHERON, JRNL AUTH 4 L.DE CHAISEMARTIN,A.HAOUZ,G.A.MILLOT,S.BAY,A.GERARD, JRNL AUTH 5 F.JONSSON,S.CHOLLET-MARTIN,P.BRUHNS JRNL TITL ANTIBODY-SECRETING CELL REPERTOIRES HOLD HIGH-AFFINITY JRNL TITL 2 ANTI-ROCURONIUM SPECIFICITIES THAT CAN INDUCE ANAPHYLAXIS IN JRNL TITL 3 VIVO. JRNL REF J.ALLERGY CLIN.IMMUNOL. 2025 JRNL REFN ESSN 1097-6825 JRNL PMID 39892658 JRNL DOI 10.1016/J.JACI.2025.01.025 REMARK 2 REMARK 2 RESOLUTION. 1.72 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) : 1.72 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.47 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 47138 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) : 0.163 REMARK 3 R VALUE (WORKING SET) : 0.162 REMARK 3 FREE R VALUE : 0.203 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1489 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 40 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.72 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1701 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.93 REMARK 3 BIN R VALUE (WORKING SET) : 0.3020 REMARK 3 BIN FREE R VALUE SET COUNT : 53 REMARK 3 BIN FREE R VALUE : 0.3020 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3381 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 38 REMARK 3 SOLVENT ATOMS : 354 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.16 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.57000 REMARK 3 B22 (A**2) : -1.71000 REMARK 3 B33 (A**2) : 1.96000 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): 0.097 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.859 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3505 ; 0.008 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 3199 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4770 ; 1.592 ; 1.824 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7430 ; 0.568 ; 1.759 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 439 ; 7.356 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 12 ; 7.922 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 561 ;11.958 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 535 ; 0.080 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4036 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 780 ; 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): 1762 ; 3.688 ; 4.639 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1762 ; 3.672 ; 4.639 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2199 ; 4.641 ; 8.324 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2200 ; 4.640 ; 8.325 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1743 ; 4.641 ; 4.979 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1744 ; 4.640 ; 4.978 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2572 ; 6.706 ; 8.935 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3826 ; 8.203 ;46.020 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3760 ; 8.149 ;45.250 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 : BABINET MODEL WITH 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 9G6R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1292139340. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-FEB-19 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 : SOLEIL REMARK 200 BEAMLINE : PROXIMA 1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9785657 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48808 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720 REMARK 200 RESOLUTION RANGE LOW (A) : 44.300 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 8.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.99 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 60 % (W/V) MPD 0.01 M CACL2 0.1 M NA REMARK 280 ACETATE PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K 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 27.58500 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3920 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19750 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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 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 DISTANCE REMARK 500 OD2 ASP H 208 O HOH H 401 2.18 REMARK 500 REMARK 500 REMARK: NULL 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 40 NE - CZ - NH1 ANGL. DEV. = -3.6 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 132 116.09 -164.96 REMARK 500 MET L 51 -33.68 71.49 REMARK 500 SER L 67 -150.65 -89.87 REMARK 500 ASN L 138 66.65 62.88 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH H 619 DISTANCE = 6.55 ANGSTROMS REMARK 525 HOH H 620 DISTANCE = 8.34 ANGSTROMS DBREF 9G6R H 1 213 PDB 9G6R 9G6R 1 213 DBREF 9G6R L 1 213 PDB 9G6R 9G6R 1 213 SEQRES 1 H 223 PCA VAL GLN LEU GLN GLN SER GLY ALA GLU LEU ALA LYS SEQRES 2 H 223 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 H 223 TYR THR PHE THR SER ASN TRP MET HIS TRP VAL LYS GLN SEQRES 4 H 223 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR ILE ASN SEQRES 5 H 223 PRO SER SER GLY TYR SER LYS TYR ASN GLN LYS PHE LYS SEQRES 6 H 223 ASP LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 H 223 ALA TYR MET GLN LEU SER SER LEU THR TYR GLU ASP SER SEQRES 8 H 223 ALA VAL TYR PHE CYS ALA ARG LEU SER TYR TYR ASP TYR SEQRES 9 H 223 ASP GLY GLY TYR PHE PHE ASP PHE TRP GLY GLN GLY THR SEQRES 10 H 223 THR LEU THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 223 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 223 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 223 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 223 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 223 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 223 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 223 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 H 223 GLU PRO SEQRES 1 L 218 ASP ILE VAL ILE THR GLN ASP GLU LEU SER SER PRO VAL SEQRES 2 L 218 THR SER GLY GLU SER VAL SER ILE SER CYS ARG SER SER SEQRES 3 L 218 LYS SER LEU LEU TYR LYS ASP GLY LYS THR TYR LEU ASN SEQRES 4 L 218 TRP PHE LEU GLN ARG PRO GLY GLN SER PRO GLN ILE LEU SEQRES 5 L 218 ILE TYR LEU MET SER THR ARG ALA SER GLY VAL SER ASP SEQRES 6 L 218 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 218 GLU ILE SER ARG VAL LYS ALA GLU ASP VAL GLY VAL TYR SEQRES 8 L 218 TYR CYS GLN GLN VAL VAL GLU TYR PRO TYR THR PHE GLY SEQRES 9 L 218 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 L 218 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 218 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 218 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 218 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 218 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 218 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 218 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 218 PRO VAL THR LYS SER PHE ASN ARG GLY GLU HET PCA H 1 8 HET RBR H 301 38 HETNAM PCA PYROGLUTAMIC ACID HETNAM RBR ROCURONIUM FORMUL 1 PCA C5 H7 N O3 FORMUL 3 RBR C32 H53 N2 O4 1+ FORMUL 4 HOH *354(H2 O) HELIX 1 AA1 THR H 28 ASN H 32 5 5 HELIX 2 AA2 GLN H 61 LYS H 64 5 4 HELIX 3 AA3 THR H 83 SER H 87 5 5 HELIX 4 AA4 SER H 127 LYS H 129 5 3 HELIX 5 AA5 SER H 156 ALA H 158 5 3 HELIX 6 AA6 SER H 187 THR H 191 5 5 HELIX 7 AA7 LYS H 201 ASN H 204 5 4 HELIX 8 AA8 LYS L 79 VAL L 83 5 5 HELIX 9 AA9 SER L 121 SER L 127 1 7 HELIX 10 AB1 LYS L 183 LYS L 188 1 6 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 77 LEU H 82 -1 O MET H 80 N LEU H 20 SHEET 4 AA1 4 ALA H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA2 6 GLU H 10 ALA H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N ALA H 12 SHEET 3 AA2 6 ALA H 88 TYR H 97 -1 N ALA H 88 O LEU H 109 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N HIS H 35 O ALA H 93 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AA2 6 SER H 57 TYR H 59 -1 O LYS H 58 N TYR H 50 SHEET 1 AA3 4 GLU H 10 ALA H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N ALA H 12 SHEET 3 AA3 4 ALA H 88 TYR H 97 -1 N ALA H 88 O LEU H 109 SHEET 4 AA3 4 TYR H 100D TRP H 103 -1 O PHE H 100E N SER H 96 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA4 4 HIS H 164 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 ARG H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 ILE L 4 GLN L 6 0 SHEET 2 AA7 4 VAL L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA7 4 PHE L 62 GLY L 66 -1 N SER L 63 O GLU L 74 SHEET 1 AA8 2 VAL L 13 THR L 14 0 SHEET 2 AA8 2 ILE L 106 LYS L 107 1 O LYS L 107 N VAL L 13 SHEET 1 AA9 5 THR L 53 ARG L 54 0 SHEET 2 AA9 5 GLN L 45 TYR L 49 -1 N TYR L 49 O THR L 53 SHEET 3 AA9 5 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 AA9 5 GLY L 84 GLN L 90 -1 O VAL L 85 N GLN L 38 SHEET 5 AA9 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 5 THR L 53 ARG L 54 0 SHEET 2 AB1 5 GLN L 45 TYR L 49 -1 N TYR L 49 O THR L 53 SHEET 3 AB1 5 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 AB1 5 GLY L 84 GLN L 90 -1 O VAL L 85 N GLN L 38 SHEET 5 AB1 5 THR L 102 LEU L 104 -1 O LEU L 104 N GLY L 84 SHEET 1 AB2 4 SER L 114 PHE L 118 0 SHEET 2 AB2 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114 SHEET 3 AB2 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AB2 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB3 4 ALA L 153 LEU L 154 0 SHEET 2 AB3 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB3 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB3 4 VAL L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.11 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.13 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.34 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.13 LINK C PCA H 1 N VAL H 2 1555 1555 1.32 CISPEP 1 PHE H 146 PRO H 147 0 -11.17 CISPEP 2 GLU H 148 PRO H 149 0 -10.42 CISPEP 3 TYR L 94 PRO L 95 0 -1.36 CISPEP 4 TYR L 140 PRO L 141 0 -3.99 CRYST1 56.496 55.170 76.892 90.00 104.87 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 0.017700 0.000000 0.004700 0.00000 SCALE2 0.000000 0.018126 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013456 0.00000