HEADER IMMUNE SYSTEM 19-JUL-24 9G6S TITLE FAB-IP2 IN COMPLEX WITH ROCURONIUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB-IP2 H CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB-IP2 L 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 FAB, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.HAOUZ,F.A.SAUL,P.BRUHNS REVDAT 1 12-FEB-25 9G6S 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. 2.37 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.4 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.37 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.01 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 42.0 REMARK 3 NUMBER OF REFLECTIONS : 16325 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) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.208 REMARK 3 FREE R VALUE : 0.253 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 785 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 (ANGSTROMS) : 2.37 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.69 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 3.50 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2887 REMARK 3 BIN FREE R VALUE : 0.3599 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 29 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 : 3178 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 38 REMARK 3 SOLVENT ATOMS : 122 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.73 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.93970 REMARK 3 B22 (A**2) : -0.93970 REMARK 3 B33 (A**2) : 1.87940 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.370 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.717 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.358 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.696 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.362 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.910 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.869 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3305 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4515 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1088 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 535 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3305 ; 10.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 447 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 2574 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.02 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.85 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.63 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9G6S 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_1292140442. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-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 2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.980100 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : STARANISO REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16351 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.373 REMARK 200 RESOLUTION RANGE LOW (A) : 114.002 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 89.7 REMARK 200 DATA REDUNDANCY : 5.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 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 (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % (W/V) PEG 4K 5 %W/V 2-PROPOH 0.1 REMARK 280 M HEPES PH7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.74667 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 63.49333 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 63.49333 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 31.74667 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: 3720 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18810 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 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 133 REMARK 465 LYS H 134 REMARK 465 SER H 135 REMARK 465 SER H 193 REMARK 465 LEU H 194 REMARK 465 GLY H 195 REMARK 465 THR H 196 REMARK 465 GLN H 197 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 GLN H 1 CG CD OE1 NE2 REMARK 470 SER H 132 CA C O CB OG REMARK 470 ARG H 215 CG CD NE CZ NH1 NH2 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 PRO H 41 109.83 -56.87 REMARK 500 GLN H 43 43.14 -98.26 REMARK 500 SER H 85 70.21 44.46 REMARK 500 PHE H 105 98.63 -63.65 REMARK 500 ALA H 130 98.20 -33.80 REMARK 500 ASP H 149 76.69 51.92 REMARK 500 PRO H 152 -157.14 -85.28 REMARK 500 SER H 161 29.78 48.54 REMARK 500 THR H 165 -32.76 -130.58 REMARK 500 SER H 182 116.04 -166.31 REMARK 500 THR L 50 -41.32 65.30 REMARK 500 SER L 127 0.44 -68.66 REMARK 500 ASN L 138 83.60 30.35 REMARK 500 ASN L 152 -5.14 72.37 REMARK 500 REMARK 500 REMARK: NULL DBREF 9G6S H 1 218 PDB 9G6S 9G6S 1 218 DBREF 9G6S L 1 214 PDB 9G6S 9G6S 1 214 SEQRES 1 H 218 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 H 218 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY SEQRES 3 H 218 TYR THR PHE THR SER TYR TRP ILE THR TRP VAL LYS GLN SEQRES 4 H 218 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ASP ILE TYR SEQRES 5 H 218 PRO GLY SER GLY SER SER ASN TYR ASN GLU LYS PHE LYS SEQRES 6 H 218 SER LYS ALA THR LEU THR VAL ASP THR SER SER SER THR SEQRES 7 H 218 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 H 218 ALA VAL TYR TYR CYS ALA ARG LEU GLY SER ARG HIS TYR SEQRES 9 H 218 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SEQRES 10 H 218 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 218 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 218 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 218 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 218 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 218 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 218 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 218 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 1 L 214 GLN ILE VAL LEU THR GLN SER PRO ALA LEU MET SER ALA SEQRES 2 L 214 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER SEQRES 3 L 214 SER SER VAL SER TYR MET TYR TRP TYR GLN GLN LYS PRO SEQRES 4 L 214 GLY SER PRO PRO LYS SER TRP ILE TYR LEU THR SER ASN SEQRES 5 L 214 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 L 214 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU SEQRES 7 L 214 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER SEQRES 8 L 214 PRO ASN PRO PRO ILE THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 L 214 GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS HET RBR H 301 38 HETNAM RBR ROCURONIUM FORMUL 3 RBR C32 H53 N2 O4 1+ FORMUL 4 HOH *122(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 THR H 87 SER H 91 5 5 HELIX 3 AA3 THR H 136 GLY H 138 5 3 HELIX 4 AA4 SER H 161 ALA H 163 5 3 HELIX 5 AA5 GLU L 78 ALA L 82 5 5 HELIX 6 AA6 SER L 121 SER L 127 1 7 HELIX 7 AA7 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 78 LEU H 83 -1 O LEU H 83 N VAL H 18 SHEET 4 AA1 4 ALA H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA2 6 GLU H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 112 VAL H 116 1 O THR H 115 N GLU H 10 SHEET 3 AA2 6 ALA H 92 LEU H 99 -1 N TYR H 94 O THR H 112 SHEET 4 AA2 6 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O ILE H 51 N ILE H 34 SHEET 6 AA2 6 SER H 58 TYR H 60 -1 O ASN H 59 N ASP H 50 SHEET 1 AA3 4 GLU H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 112 VAL H 116 1 O THR H 115 N GLU H 10 SHEET 3 AA3 4 ALA H 92 LEU H 99 -1 N TYR H 94 O THR H 112 SHEET 4 AA3 4 PHE H 105 TRP H 108 -1 O TYR H 107 N ARG H 98 SHEET 1 AA4 4 SER H 125 LEU H 129 0 SHEET 2 AA4 4 THR H 140 TYR H 150 -1 O LYS H 148 N SER H 125 SHEET 3 AA4 4 TYR H 181 PRO H 190 -1 O VAL H 187 N LEU H 143 SHEET 4 AA4 4 VAL H 168 THR H 170 -1 N HIS H 169 O VAL H 186 SHEET 1 AA5 4 SER H 125 LEU H 129 0 SHEET 2 AA5 4 THR H 140 TYR H 150 -1 O LYS H 148 N SER H 125 SHEET 3 AA5 4 TYR H 181 PRO H 190 -1 O VAL H 187 N LEU H 143 SHEET 4 AA5 4 VAL H 174 LEU H 175 -1 N VAL H 174 O SER H 182 SHEET 1 AA6 3 VAL H 155 TRP H 159 0 SHEET 2 AA6 3 ILE H 200 HIS H 205 -1 O ASN H 202 N SER H 158 SHEET 3 AA6 3 THR H 210 ARG H 215 -1 O LYS H 214 N CYS H 201 SHEET 1 AA7 4 LEU L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O SER L 24 N THR L 5 SHEET 3 AA7 4 SER L 69 ILE L 74 -1 O LEU L 72 N MET L 21 SHEET 4 AA7 4 PHE L 61 SER L 66 -1 N SER L 62 O THR L 73 SHEET 1 AA8 6 LEU L 10 ALA L 13 0 SHEET 2 AA8 6 THR L 102 LEU L 106 1 O GLU L 105 N MET L 11 SHEET 3 AA8 6 ALA L 83 TRP L 90 -1 N ALA L 83 O LEU L 104 SHEET 4 AA8 6 TYR L 31 GLN L 37 -1 N TYR L 33 O GLN L 88 SHEET 5 AA8 6 LYS L 44 TYR L 48 -1 O TRP L 46 N TRP L 34 SHEET 6 AA8 6 ASN L 52 LEU L 53 -1 O ASN L 52 N TYR L 48 SHEET 1 AA9 4 SER L 114 PHE L 118 0 SHEET 2 AA9 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114 SHEET 3 AA9 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AA9 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB1 4 ALA L 153 LEU L 154 0 SHEET 2 AB1 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB1 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB1 4 VAL L 205 ASN L 210 -1 O PHE L 209 N TYR L 192 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 2 CYS H 145 CYS H 201 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 87 1555 1555 2.05 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03 CISPEP 1 PHE H 151 PRO H 152 0 -5.41 CISPEP 2 GLU H 153 PRO H 154 0 6.14 CISPEP 3 SER L 7 PRO L 8 0 -0.89 CISPEP 4 TYR L 140 PRO L 141 0 -1.01 CRYST1 131.638 131.638 95.240 90.00 90.00 120.00 P 31 2 1 6 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 0.007597 0.004386 0.000000 0.00000 SCALE2 0.000000 0.008772 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010500 0.00000