HEADER IMMUNE SYSTEM 19-JUL-24 9G6Q TITLE SCFV IP11 IN COMPLEX WITH ROCURONIUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: SCFV-IP11; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SCFV-IP11; 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: DROSOPHILA MELANOGASTER; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: S2; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: S2 KEYWDS IMMUNOTHERAPY, ANAPHYLAXIS, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.HAOUZ,F.A.SAUL,P.BRUHNS REVDAT 1 12-FEB-25 9G6Q 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. 1.20 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) : 1.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.97 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 80214 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) : 0.169 REMARK 3 R VALUE (WORKING SET) : 0.168 REMARK 3 FREE R VALUE : 0.189 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1579 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) : 1.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.22 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2945 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.79 REMARK 3 BIN R VALUE (WORKING SET) : 0.2770 REMARK 3 BIN FREE R VALUE SET COUNT : 61 REMARK 3 BIN FREE R VALUE : 0.2610 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1786 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 38 REMARK 3 SOLVENT ATOMS : 288 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.93 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.00000 REMARK 3 B22 (A**2) : -0.57000 REMARK 3 B33 (A**2) : -0.43000 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 OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.035 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.037 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.027 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.613 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.969 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1900 ; 0.015 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 1731 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2589 ; 1.964 ; 1.838 REMARK 3 BOND ANGLES OTHERS (DEGREES): 4003 ; 0.690 ; 1.781 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 239 ; 7.030 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 10 ; 6.714 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 298 ;10.995 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 286 ; 0.288 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2234 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 454 ; 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): 945 ; 1.785 ; 1.771 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 945 ; 1.784 ; 1.770 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1181 ; 2.629 ; 3.562 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1182 ; 2.628 ; 3.567 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 955 ; 3.720 ; 2.169 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 956 ; 3.718 ; 2.171 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1406 ; 5.337 ; 4.234 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2124 ; 6.481 ;15.630 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2034 ; 6.313 ;14.150 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 9G6Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1292139261. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-SEP-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) : 0.9801 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 : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81866 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200 REMARK 200 RESOLUTION RANGE LOW (A) : 50.800 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 200 DATA REDUNDANCY : 7.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22 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 (%): 48.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % (W/V) PEG 4K 10 % (V/V) 2-PROPOH REMARK 280 0.1 M HEPES PH 7.5, VAPOR DIFFUSION, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-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 25.43950 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.30500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.84250 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.30500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.43950 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.84250 REMARK 290 SMTRY3 4 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: 1810 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10510 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 113 REMARK 465 GLY L -19 REMARK 465 THR L -18 REMARK 465 GLY L -17 REMARK 465 GLY L -16 REMARK 465 SER L -15 REMARK 465 GLY L -14 REMARK 465 GLY L -13 REMARK 465 GLY L -12 REMARK 465 GLY L -11 REMARK 465 SER L -10 REMARK 465 GLY L -9 REMARK 465 GLY L -8 REMARK 465 GLY L -7 REMARK 465 GLY L -6 REMARK 465 SER L -5 REMARK 465 GLY L -4 REMARK 465 GLY L -3 REMARK 465 SER L 10 REMARK 465 ASN L 11 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 ARG H 13 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 85 CG CD OE1 OE2 REMARK 470 GLU L 8 CG CD OE1 OE2 REMARK 470 LYS L 27 CG CD CE NZ REMARK 470 LYS L 107 CG CD CE NZ 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 O HOH H 348 O HOH H 457 1.97 REMARK 500 O HOH H 412 O HOH H 420 2.06 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 CD - NE - CZ ANGL. DEV. = 15.0 DEGREES REMARK 500 ARG H 40 NE - CZ - NH1 ANGL. DEV. = 9.5 DEGREES REMARK 500 ARG H 40 NE - CZ - NH2 ANGL. DEV. = -7.3 DEGREES REMARK 500 ARG L 61 NE - CZ - NH1 ANGL. DEV. = 3.4 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 MET L 51 -43.69 75.77 REMARK 500 ASP L 60 2.18 -69.36 REMARK 500 REMARK 500 REMARK: NULL DBREF 9G6Q H 1 113 PDB 9G6Q 9G6Q 1 113 DBREF 9G6Q L -19 107 PDB 9G6Q 9G6Q -19 107 SEQRES 1 H 121 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU ALA ARG SEQRES 2 H 121 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 H 121 TYR THR PHE THR SER TYR GLY ILE THR TRP VAL LYS GLN SEQRES 4 H 121 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY GLU ILE TYR SEQRES 5 H 121 PRO ARG SER THR TYR THR SER TYR ASN GLU LYS PHE LYS SEQRES 6 H 121 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 H 121 ALA TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 H 121 ALA VAL TYR PHE CYS ALA ARG ALA GLY ASN TRP GLY GLY SEQRES 9 H 121 GLU ASN PHE PHE ASP TYR TRP GLY GLN GLY THR THR LEU SEQRES 10 H 121 THR VAL SER SER SEQRES 1 L 132 GLY THR GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY SEQRES 2 L 132 GLY SER GLY GLY GLY ALA SER ASP ILE VAL ILE THR GLN SEQRES 3 L 132 ASP GLU LEU SER ASN PRO VAL THR SER GLY GLU SER VAL SEQRES 4 L 132 SER ILE SER CYS ARG SER SER LYS SER LEU LEU TYR LYS SEQRES 5 L 132 ASP GLY LYS THR TYR LEU ASN TRP PHE LEU GLN ARG PRO SEQRES 6 L 132 GLY GLN SER PRO GLN LEU LEU ILE TYR LEU MET SER THR SEQRES 7 L 132 ARG ALA SER GLY VAL SER ASP ARG PHE SER GLY SER GLY SEQRES 8 L 132 SER GLY THR ASP PHE THR LEU GLU ILE ARG ARG VAL LYS SEQRES 9 L 132 ALA GLU ASP VAL GLY VAL TYR TYR CYS GLN GLN LEU VAL SEQRES 10 L 132 GLU TYR PRO TYR THR PHE GLY GLY GLY THR LYS LEU GLU SEQRES 11 L 132 ILE LYS HET RBR H 201 38 HETNAM RBR ROCURONIUM FORMUL 3 RBR C32 H53 N2 O4 1+ FORMUL 4 HOH *288(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 GLU H 61 LYS H 64 5 4 HELIX 3 AA3 THR H 83 SER H 87 5 5 HELIX 4 AA4 LYS L 79 VAL L 83 5 5 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 ALA H 95 -1 N ALA H 88 O LEU H 109 SHEET 4 AA2 6 GLY H 33 GLN H 39 -1 N THR H 35 O ALA H 93 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O SER H 58 N GLU H 50 SHEET 1 AA3 4 ILE L 4 GLN L 6 0 SHEET 2 AA3 4 VAL L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA3 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA3 4 PHE L 62 GLY L 66 -1 N SER L 63 O GLU L 74 SHEET 1 AA4 5 THR L 53 ARG L 54 0 SHEET 2 AA4 5 GLN L 45 TYR L 49 -1 N TYR L 49 O THR L 53 SHEET 3 AA4 5 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 AA4 5 GLY L 84 GLN L 90 -1 O VAL L 85 N GLN L 38 SHEET 5 AA4 5 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AA5 5 THR L 53 ARG L 54 0 SHEET 2 AA5 5 GLN L 45 TYR L 49 -1 N TYR L 49 O THR L 53 SHEET 3 AA5 5 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 AA5 5 GLY L 84 GLN L 90 -1 O VAL L 85 N GLN L 38 SHEET 5 AA5 5 THR L 102 LEU L 104 -1 O LEU L 104 N GLY L 84 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.09 SSBOND 2 CYS L 23 CYS L 88 1555 1555 2.17 CISPEP 1 TYR L 94 PRO L 95 0 -8.15 CRYST1 50.879 63.685 80.610 90.00 90.00 90.00 P 21 21 21 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 0.019654 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015702 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012405 0.00000