HEADER ANTITOXIN/IMMUNE SYSTEM 19-NOV-23 8V13 TITLE CRYSTAL STRUCTURE OF BLACK MAMBA TOXIN IN COMPLEX WITH CENTI-SNX-B03 TITLE 2 ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: CENTI-SNX-B03 FAB HEAVY CHAIN; COMPND 3 CHAIN: H, h; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CENTI-SNX-B03 FAB LIGHT CHAIN; COMPND 7 CHAIN: L, l; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SHORT NEUROTOXIN 1; COMPND 11 CHAIN: T, t; COMPND 12 SYNONYM: NEUROTOXIN ALPHA; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: DENDRASPIS POLYLEPIS POLYLEPIS; SOURCE 13 ORGANISM_COMMON: BLACK MAMBA; SOURCE 14 ORGANISM_TAXID: 8620; SOURCE 15 EXPRESSION_SYSTEM: DENDROASPIS POLYLEPIS POLYLEPIS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 8620 KEYWDS ANTIVENOM, 3-FINGER TOXIN, SHORT NEUROTOXIN, ANTIBODY, ANTITOXIN- KEYWDS 2 IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR S.PLETNEV,J.GLANVILLE,P.D.KWONG REVDAT 1 29-JAN-25 8V13 0 JRNL AUTH J.GLANVILLE,J.ANDRADE,M.BELLIN,S.KIM,S.PLETNEV,D.TSAO, JRNL AUTH 2 R.VERARDI,R.BEDI,T.FRIEDE,E.TULLY,B.ZHANG,T.BYLUND,T.LIU, JRNL AUTH 3 P.D.KWONG JRNL TITL VENOM PROTECTION BY BROADLY NEUTRALIZING ANTIBODY FROM A JRNL TITL 2 SNAKEBITE SUBJECT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 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) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.01 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 3 NUMBER OF REFLECTIONS : 119970 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) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.181 REMARK 3 FREE R VALUE : 0.229 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1158 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) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85 REMARK 3 REFLECTION IN BIN (WORKING SET) : 8581 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.76 REMARK 3 BIN R VALUE (WORKING SET) : 0.3060 REMARK 3 BIN FREE R VALUE SET COUNT : 90 REMARK 3 BIN FREE R VALUE : 0.3520 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7409 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 2 REMARK 3 SOLVENT ATOMS : 860 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.14 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.85000 REMARK 3 B22 (A**2) : -0.46000 REMARK 3 B33 (A**2) : -1.36000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.33000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.102 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.091 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.135 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7642 ; 0.012 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 6944 ; 0.001 ; 0.014 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10409 ; 1.704 ; 1.646 REMARK 3 BOND ANGLES OTHERS (DEGREES): 16113 ; 1.398 ; 1.578 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 993 ; 7.819 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 320 ;31.710 ;22.656 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1193 ;15.106 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;17.840 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1016 ; 0.078 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8716 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1676 ; 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): 3990 ; 3.526 ; 3.608 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3989 ; 3.523 ; 3.608 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4977 ; 5.133 ; 5.383 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4978 ; 5.134 ; 5.384 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3652 ; 4.340 ; 3.963 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3653 ; 4.339 ; 3.965 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5433 ; 6.520 ; 5.743 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8396 ; 9.096 ;43.358 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8194 ; 9.039 ;42.848 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 8V13 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-23. REMARK 100 THE DEPOSITION ID IS D_1000279323. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-OCT-23 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 : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979497 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121160 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 30.010 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : 0.04700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.80 REMARK 200 R MERGE FOR SHELL (I) : 0.80900 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: BALBES REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.41 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.5, 20% PEG4000, 0.2M REMARK 280 SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 51.76950 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.12600 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.76950 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.12600 REMARK 290 SMTRY3 4 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: 5360 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, T 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: 5080 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22120 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: h, l, t 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 GLN H 1 REMARK 465 SER L 1 REMARK 465 GLN L 2 REMARK 465 CYS L 211 REMARK 465 SER L 212 REMARK 465 GLN h 1 REMARK 465 ASP h 217 REMARK 465 LYS h 218 REMARK 465 GLY h 219 REMARK 465 LEU h 220 REMARK 465 GLU h 221 REMARK 465 VAL h 222 REMARK 465 LEU h 223 REMARK 465 PHE h 224 REMARK 465 GLN h 225 REMARK 465 SER l 1 REMARK 465 GLN l 2 REMARK 465 CYS l 211 REMARK 465 SER l 212 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 NH1 ARG t 1 OD1 ASP t 56 2.19 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 ASP T 29 CB - CA - C ANGL. DEV. = 12.1 DEGREES REMARK 500 ARG l 77 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 ARG l 77 NE - CZ - NH2 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 SER H 127 -155.60 -140.76 REMARK 500 ASP L 51 -50.05 79.27 REMARK 500 SER L 52 -6.60 -147.89 REMARK 500 ASP L 151 -113.77 49.92 REMARK 500 ASN L 170 -3.75 74.28 REMARK 500 ASN T 5 15.54 -145.64 REMARK 500 SER T 8 -116.55 47.89 REMARK 500 SER T 55 -166.79 -67.64 REMARK 500 ALA h 88 163.89 175.67 REMARK 500 ASP h 144 54.29 71.51 REMARK 500 ASP l 51 -44.19 73.18 REMARK 500 SER l 52 -3.09 -147.31 REMARK 500 ASP l 151 -117.36 53.98 REMARK 500 ASN l 170 -2.16 79.52 REMARK 500 THR l 209 36.60 -83.16 REMARK 500 SER t 8 -116.93 48.64 REMARK 500 CYS t 53 -165.98 -115.78 REMARK 500 GLN t 54 55.06 -146.31 REMARK 500 ASN t 59 40.72 -100.86 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 LEU L 106A -12.23 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA L 301 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH H 326 O REMARK 620 2 ASP L 92 O 161.7 REMARK 620 3 SER L 95 O 112.2 85.2 REMARK 620 4 HOH L 545 O 102.3 83.8 86.5 REMARK 620 5 HOH T 103 O 83.6 90.3 92.5 174.0 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA l 301 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH h 342 O REMARK 620 2 ASP l 92 O 169.2 REMARK 620 3 SER l 95 O 103.6 87.1 REMARK 620 4 HOH l 513 O 101.4 80.4 84.3 REMARK 620 5 HOH t 113 O 85.8 91.6 99.0 171.2 REMARK 620 N 1 2 3 4 DBREF 8V13 H 1 225 PDB 8V13 8V13 1 225 DBREF 8V13 L 1 212 PDB 8V13 8V13 1 212 DBREF 8V13 T 1 60 UNP P01416 3S11_DENPO 1 60 DBREF 8V13 h 1 225 PDB 8V13 8V13 1 225 DBREF 8V13 l 1 212 PDB 8V13 8V13 1 212 DBREF 8V13 t 1 60 UNP P01416 3S11_DENPO 1 60 SEQRES 1 H 230 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY VAL VAL ARG SEQRES 2 H 230 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 230 PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 H 230 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE SER SEQRES 5 H 230 GLY SER GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 230 GLY ARG PHE THR ILE SER ARG ASP SER SER LYS ASN THR SEQRES 7 H 230 LEU TYR LEU GLN ILE ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 230 ALA LEU TYR TYR CYS ALA ARG GLU GLY ASP TYR ASP SER SEQRES 9 H 230 MET ASP VAL TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 H 230 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 230 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 230 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 230 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 230 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 230 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 230 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 230 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 H 230 ASP LYS GLY LEU GLU VAL LEU PHE GLN SEQRES 1 L 215 SER GLN SER VAL VAL THR GLN PRO PRO SER VAL SER VAL SEQRES 2 L 215 ALA PRO GLY LYS THR ALA ARG ILE THR CYS GLY GLY ASN SEQRES 3 L 215 ASN ILE GLY SER LYS SER VAL HIS TRP TYR GLN GLN LYS SEQRES 4 L 215 PRO GLY GLN ALA PRO VAL LEU VAL VAL PHE ASP ASP SER SEQRES 5 L 215 ALA ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER SEQRES 6 L 215 ASN SER GLY ASN THR ALA THR LEU THR ILE SER ARG VAL SEQRES 7 L 215 GLU ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN VAL TRP SEQRES 8 L 215 ASP ASN ASN SER ASP ASP VAL VAL PHE GLY GLY GLY THR SEQRES 9 L 215 LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER SEQRES 10 L 215 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA SEQRES 11 L 215 ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR SEQRES 12 L 215 PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER SEQRES 13 L 215 PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS SEQRES 14 L 215 GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER SEQRES 15 L 215 LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER SEQRES 16 L 215 CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR SEQRES 17 L 215 VAL ALA PRO THR GLU CYS SER SEQRES 1 T 60 ARG ILE CYS TYR ASN HIS GLN SER THR THR ARG ALA THR SEQRES 2 T 60 THR LYS SER CYS GLU GLU ASN SER CYS TYR LYS LYS TYR SEQRES 3 T 60 TRP ARG ASP HIS ARG GLY THR ILE ILE GLU ARG GLY CYS SEQRES 4 T 60 GLY CYS PRO LYS VAL LYS PRO GLY VAL GLY ILE HIS CYS SEQRES 5 T 60 CYS GLN SER ASP LYS CYS ASN TYR SEQRES 1 h 230 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY VAL VAL ARG SEQRES 2 h 230 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 h 230 PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 h 230 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE SER SEQRES 5 h 230 GLY SER GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 h 230 GLY ARG PHE THR ILE SER ARG ASP SER SER LYS ASN THR SEQRES 7 h 230 LEU TYR LEU GLN ILE ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 h 230 ALA LEU TYR TYR CYS ALA ARG GLU GLY ASP TYR ASP SER SEQRES 9 h 230 MET ASP VAL TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 h 230 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 h 230 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 h 230 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 h 230 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 h 230 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 h 230 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 h 230 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 h 230 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 h 230 ASP LYS GLY LEU GLU VAL LEU PHE GLN SEQRES 1 l 215 SER GLN SER VAL VAL THR GLN PRO PRO SER VAL SER VAL SEQRES 2 l 215 ALA PRO GLY LYS THR ALA ARG ILE THR CYS GLY GLY ASN SEQRES 3 l 215 ASN ILE GLY SER LYS SER VAL HIS TRP TYR GLN GLN LYS SEQRES 4 l 215 PRO GLY GLN ALA PRO VAL LEU VAL VAL PHE ASP ASP SER SEQRES 5 l 215 ALA ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER SEQRES 6 l 215 ASN SER GLY ASN THR ALA THR LEU THR ILE SER ARG VAL SEQRES 7 l 215 GLU ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN VAL TRP SEQRES 8 l 215 ASP ASN ASN SER ASP ASP VAL VAL PHE GLY GLY GLY THR SEQRES 9 l 215 LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER SEQRES 10 l 215 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA SEQRES 11 l 215 ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR SEQRES 12 l 215 PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER SEQRES 13 l 215 PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS SEQRES 14 l 215 GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER SEQRES 15 l 215 LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER SEQRES 16 l 215 CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR SEQRES 17 l 215 VAL ALA PRO THR GLU CYS SER SEQRES 1 t 60 ARG ILE CYS TYR ASN HIS GLN SER THR THR ARG ALA THR SEQRES 2 t 60 THR LYS SER CYS GLU GLU ASN SER CYS TYR LYS LYS TYR SEQRES 3 t 60 TRP ARG ASP HIS ARG GLY THR ILE ILE GLU ARG GLY CYS SEQRES 4 t 60 GLY CYS PRO LYS VAL LYS PRO GLY VAL GLY ILE HIS CYS SEQRES 5 t 60 CYS GLN SER ASP LYS CYS ASN TYR HET NA L 301 1 HET NA l 301 1 HETNAM NA SODIUM ION FORMUL 7 NA 2(NA 1+) FORMUL 9 HOH *860(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 ASP H 61 LYS H 64 5 4 HELIX 3 AA3 SER H 73 LYS H 75 5 3 HELIX 4 AA4 ARG H 83 THR H 87 5 5 HELIX 5 AA5 ASP H 97 ASP H 99 5 3 HELIX 6 AA6 SER H 156 ALA H 158 5 3 HELIX 7 AA7 SER H 187 THR H 191 5 5 HELIX 8 AA8 LYS H 201 ASN H 204 5 4 HELIX 9 AA9 ASP H 217 GLU H 221 5 5 HELIX 10 AB1 ASN L 27 LYS L 31 5 5 HELIX 11 AB2 GLU L 79 GLU L 83 5 5 HELIX 12 AB3 SER L 121 ALA L 127 1 7 HELIX 13 AB4 THR L 181 SER L 187 1 7 HELIX 14 AB5 THR h 28 TYR h 32 5 5 HELIX 15 AB6 ASP h 61 LYS h 64 5 4 HELIX 16 AB7 ARG h 83 THR h 87 5 5 HELIX 17 AB8 ASP h 97 ASP h 99 5 3 HELIX 18 AB9 SER h 156 ALA h 158 5 3 HELIX 19 AC1 SER h 187 THR h 191 5 5 HELIX 20 AC2 LYS h 201 ASN h 204 5 4 HELIX 21 AC3 ASN l 27 LYS l 31 5 5 HELIX 22 AC4 GLU l 79 GLU l 83 5 5 HELIX 23 AC5 SER l 121 ALA l 127 1 7 HELIX 24 AC6 THR l 181 SER l 187 1 7 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA1 4 THR H 77 ILE H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AA2 6 VAL H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 GLU H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O TYR H 58 N ALA H 50 SHEET 1 AA3 4 VAL H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 GLU H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AA3 4 MET H 100A TRP H 103 -1 O VAL H 102 N ARG H 94 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 VAL H 184 N ALA H 136 SHEET 4 AA4 4 VAL H 163 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 VAL H 184 N ALA H 136 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 199 N THR H 151 SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 5 SER L 10 VAL L 13 0 SHEET 2 AA7 5 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11 SHEET 3 AA7 5 ALA L 84 TRP L 91 -1 N ALA L 84 O LEU L 104 SHEET 4 AA7 5 SER L 32 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AA7 5 VAL L 45 VAL L 48 -1 O VAL L 47 N TRP L 35 SHEET 1 AA8 4 SER L 10 VAL L 13 0 SHEET 2 AA8 4 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11 SHEET 3 AA8 4 ALA L 84 TRP L 91 -1 N ALA L 84 O LEU L 104 SHEET 4 AA8 4 VAL L 97 PHE L 98 -1 O VAL L 97 N VAL L 90 SHEET 1 AA9 3 ALA L 19 GLY L 24 0 SHEET 2 AA9 3 THR L 70 ILE L 75 -1 O ILE L 75 N ALA L 19 SHEET 3 AA9 3 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 ALA L 130 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB1 4 TYR L 172 LEU L 180 -1 O SER L 176 N CYS L 134 SHEET 4 AB1 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 177 SHEET 1 AB2 4 SER L 114 PHE L 118 0 SHEET 2 AB2 4 ALA L 130 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB2 4 TYR L 172 LEU L 180 -1 O SER L 176 N CYS L 134 SHEET 4 AB2 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173 SHEET 1 AB3 4 SER L 153 VAL L 155 0 SHEET 2 AB3 4 THR L 145 ALA L 150 -1 N ALA L 150 O SER L 153 SHEET 3 AB3 4 TYR L 191 HIS L 197 -1 O GLN L 194 N ALA L 147 SHEET 4 AB3 4 SER L 200 VAL L 206 -1 O VAL L 202 N VAL L 195 SHEET 1 AB4 2 ILE T 2 TYR T 4 0 SHEET 2 AB4 2 THR T 14 SER T 16 -1 O LYS T 15 N CYS T 3 SHEET 1 AB5 3 GLY T 32 CYS T 39 0 SHEET 2 AB5 3 CYS T 22 ASP T 29 -1 N LYS T 25 O GLU T 36 SHEET 3 AB5 3 GLY T 49 CYS T 53 -1 O GLY T 49 N TYR T 26 SHEET 1 AB6 4 GLN h 3 SER h 7 0 SHEET 2 AB6 4 LEU h 18 SER h 25 -1 O ALA h 23 N GLN h 5 SHEET 3 AB6 4 THR h 77 ILE h 82 -1 O ILE h 82 N LEU h 18 SHEET 4 AB6 4 PHE h 67 ASP h 72 -1 N THR h 68 O GLN h 81 SHEET 1 AB7 6 VAL h 11 VAL h 12 0 SHEET 2 AB7 6 THR h 107 VAL h 111 1 O THR h 110 N VAL h 12 SHEET 3 AB7 6 ALA h 88 GLU h 95 -1 N ALA h 88 O VAL h 109 SHEET 4 AB7 6 MET h 34 GLN h 39 -1 N VAL h 37 O TYR h 91 SHEET 5 AB7 6 LEU h 45 ILE h 51 -1 O VAL h 48 N TRP h 36 SHEET 6 AB7 6 THR h 57 TYR h 59 -1 O TYR h 58 N ALA h 50 SHEET 1 AB8 4 VAL h 11 VAL h 12 0 SHEET 2 AB8 4 THR h 107 VAL h 111 1 O THR h 110 N VAL h 12 SHEET 3 AB8 4 ALA h 88 GLU h 95 -1 N ALA h 88 O VAL h 109 SHEET 4 AB8 4 MET h 100A TRP h 103 -1 O VAL h 102 N ARG h 94 SHEET 1 AB9 4 SER h 120 LEU h 124 0 SHEET 2 AB9 4 THR h 135 TYR h 145 -1 O LYS h 143 N SER h 120 SHEET 3 AB9 4 TYR h 176 PRO h 185 -1 O LEU h 178 N VAL h 142 SHEET 4 AB9 4 VAL h 163 THR h 165 -1 N HIS h 164 O VAL h 181 SHEET 1 AC1 4 THR h 131 SER h 132 0 SHEET 2 AC1 4 THR h 135 TYR h 145 -1 O THR h 135 N SER h 132 SHEET 3 AC1 4 TYR h 176 PRO h 185 -1 O LEU h 178 N VAL h 142 SHEET 4 AC1 4 VAL h 169 LEU h 170 -1 N VAL h 169 O SER h 177 SHEET 1 AC2 3 THR h 151 TRP h 154 0 SHEET 2 AC2 3 TYR h 194 HIS h 200 -1 O ASN h 197 N SER h 153 SHEET 3 AC2 3 THR h 205 VAL h 211 -1 O VAL h 207 N VAL h 198 SHEET 1 AC3 5 SER l 10 VAL l 13 0 SHEET 2 AC3 5 THR l 102 VAL l 106 1 O THR l 105 N VAL l 11 SHEET 3 AC3 5 ALA l 84 TRP l 91 -1 N ALA l 84 O LEU l 104 SHEET 4 AC3 5 SER l 32 GLN l 38 -1 N GLN l 38 O ASP l 85 SHEET 5 AC3 5 VAL l 45 VAL l 48 -1 O VAL l 47 N TRP l 35 SHEET 1 AC4 4 SER l 10 VAL l 13 0 SHEET 2 AC4 4 THR l 102 VAL l 106 1 O THR l 105 N VAL l 11 SHEET 3 AC4 4 ALA l 84 TRP l 91 -1 N ALA l 84 O LEU l 104 SHEET 4 AC4 4 VAL l 97 PHE l 98 -1 O VAL l 97 N VAL l 90 SHEET 1 AC5 3 ALA l 19 GLY l 24 0 SHEET 2 AC5 3 THR l 70 ILE l 75 -1 O ILE l 75 N ALA l 19 SHEET 3 AC5 3 PHE l 62 SER l 67 -1 N SER l 63 O THR l 74 SHEET 1 AC6 4 SER l 114 PHE l 118 0 SHEET 2 AC6 4 ALA l 130 PHE l 139 -1 O VAL l 133 N PHE l 118 SHEET 3 AC6 4 TYR l 172 LEU l 180 -1 O LEU l 180 N ALA l 130 SHEET 4 AC6 4 VAL l 159 THR l 161 -1 N GLU l 160 O TYR l 177 SHEET 1 AC7 4 SER l 114 PHE l 118 0 SHEET 2 AC7 4 ALA l 130 PHE l 139 -1 O VAL l 133 N PHE l 118 SHEET 3 AC7 4 TYR l 172 LEU l 180 -1 O LEU l 180 N ALA l 130 SHEET 4 AC7 4 SER l 165 LYS l 166 -1 N SER l 165 O ALA l 173 SHEET 1 AC8 4 SER l 153 VAL l 155 0 SHEET 2 AC8 4 THR l 145 ALA l 150 -1 N ALA l 150 O SER l 153 SHEET 3 AC8 4 TYR l 191 HIS l 197 -1 O THR l 196 N THR l 145 SHEET 4 AC8 4 SER l 200 VAL l 206 -1 O VAL l 202 N VAL l 195 SHEET 1 AC9 2 ILE t 2 TYR t 4 0 SHEET 2 AC9 2 THR t 14 SER t 16 -1 O LYS t 15 N CYS t 3 SHEET 1 AD1 3 GLY t 32 CYS t 39 0 SHEET 2 AD1 3 CYS t 22 ASP t 29 -1 N LYS t 25 O GLU t 36 SHEET 3 AD1 3 GLY t 49 CYS t 53 -1 O GLY t 49 N TYR t 26 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.10 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.08 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.19 SSBOND 4 CYS L 134 CYS L 193 1555 1555 2.05 SSBOND 5 CYS T 3 CYS T 22 1555 1555 2.03 SSBOND 6 CYS T 17 CYS T 39 1555 1555 2.05 SSBOND 7 CYS T 41 CYS T 52 1555 1555 2.09 SSBOND 8 CYS T 53 CYS T 58 1555 1555 2.03 SSBOND 9 CYS h 22 CYS h 92 1555 1555 2.10 SSBOND 10 CYS h 140 CYS h 196 1555 1555 2.10 SSBOND 11 CYS l 23 CYS l 88 1555 1555 2.19 SSBOND 12 CYS l 134 CYS l 193 1555 1555 2.00 SSBOND 13 CYS t 3 CYS t 22 1555 1555 2.06 SSBOND 14 CYS t 17 CYS t 39 1555 1555 2.05 SSBOND 15 CYS t 41 CYS t 52 1555 1555 2.09 SSBOND 16 CYS t 53 CYS t 58 1555 1555 2.00 LINK O HOH H 326 NA NA L 301 1555 1555 2.29 LINK O ASP L 92 NA NA L 301 1555 1555 2.29 LINK O SER L 95 NA NA L 301 1555 1555 2.31 LINK NA NA L 301 O HOH L 545 1555 1555 2.44 LINK NA NA L 301 O HOH T 103 1555 1555 2.44 LINK O HOH h 342 NA NA l 301 1555 1555 2.41 LINK O ASP l 92 NA NA l 301 1555 1555 2.30 LINK O SER l 95 NA NA l 301 1555 1555 2.22 LINK NA NA l 301 O HOH l 513 1555 1555 2.45 LINK NA NA l 301 O HOH t 113 1555 1555 2.32 CISPEP 1 PHE H 146 PRO H 147 0 -9.48 CISPEP 2 GLU H 148 PRO H 149 0 -2.49 CISPEP 3 TYR L 140 PRO L 141 0 1.94 CISPEP 4 PHE h 146 PRO h 147 0 -9.47 CISPEP 5 GLU h 148 PRO h 149 0 -0.30 CISPEP 6 TYR l 140 PRO l 141 0 -2.12 CRYST1 103.539 72.252 179.656 90.00 91.99 90.00 C 1 2 1 8 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 0.009658 0.000000 0.000335 0.00000 SCALE2 0.000000 0.013840 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005570 0.00000