HEADER IMMUNE SYSTEM 13-APR-24 8Z2V TITLE CRYSTAL STRUCTURE OF SONIC HEDGEHOG IN COMPLEX WITH ANTIBODY 5E1 TITLE 2 MUTANT H-R102A WITH METALS COMPND MOL_ID: 1; COMPND 2 MOLECULE: SONIC HEDGEHOG PROTEIN N-PRODUCT; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SHHN,SHH N-TERMINAL PROCESSED SIGNALING DOMAINS,SHHNP; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEAVY CHAIN OF ANTIBODY 5E1; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MUTATION: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: LIGHT CHAIN OF ANTIBODY 5E1; COMPND 13 CHAIN: L; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: SHH; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3); SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: IGG; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: IGG; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: EXPI293 KEYWDS SONIC HEDGEHOG PROTEIN (SHH), ANTIBODY, FLEXIBLE/FLUCTUATED EPITOPE, KEYWDS 2 AFFINITY IMPROVEMENT, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.M.M.CAAVEIRO,I.KANEDA,K.TSUMOTO REVDAT 1 16-APR-25 8Z2V 0 JRNL AUTH I.KANEDA,R.MATSUNAGA,S.NAGATOISHI,A.SENOO,J.M.M.CAAVEIRO, JRNL AUTH 2 D.KURODA,K.TSUMOTO JRNL TITL BIOPHYSICAL INSIGHTS TO IMPROVE AFFINITY OF ANTIBODIES TO JRNL TITL 2 FLUCTUATED EPITOPE OF ANTIGEN: A CASE OF ANTI-SHH ANTIBODY JRNL TITL 3 5E1 AGAINST SHH ANTIGEN. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.89 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0238 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) : 1.89 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.48 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 3 NUMBER OF REFLECTIONS : 56074 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) : 0.187 REMARK 3 R VALUE (WORKING SET) : 0.186 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2384 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) : 1.89 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.94 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3838 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.90 REMARK 3 BIN R VALUE (WORKING SET) : 0.3240 REMARK 3 BIN FREE R VALUE SET COUNT : 150 REMARK 3 BIN FREE R VALUE : 0.3310 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4463 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 10 REMARK 3 SOLVENT ATOMS : 409 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.98 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.71000 REMARK 3 B22 (A**2) : -1.03000 REMARK 3 B33 (A**2) : -0.33000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -3.37000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.132 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.130 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.165 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4609 ; 0.018 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 4139 ; 0.003 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6270 ; 2.140 ; 1.646 REMARK 3 BOND ANGLES OTHERS (DEGREES): 9663 ; 1.511 ; 1.576 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 599 ;18.286 ; 5.342 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 214 ;33.386 ;23.178 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 749 ;15.430 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;18.872 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 607 ; 0.093 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5745 ; 0.012 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 947 ; 0.002 ; 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): 2304 ; 0.947 ; 1.118 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2303 ; 0.946 ; 1.117 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2876 ; 1.586 ; 1.670 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2877 ; 1.586 ; 1.671 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2305 ; 1.319 ; 1.269 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2306 ; 1.319 ; 1.270 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3389 ; 2.148 ; 1.833 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5199 ; 5.619 ;14.295 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5103 ; 5.522 ;13.640 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 : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 39 A 188 REMARK 3 ORIGIN FOR THE GROUP (A): 2.9073 16.1997 57.3239 REMARK 3 T TENSOR REMARK 3 T11: 0.2440 T22: 0.1306 REMARK 3 T33: 0.1480 T12: -0.0465 REMARK 3 T13: -0.0309 T23: -0.0202 REMARK 3 L TENSOR REMARK 3 L11: 1.7253 L22: 3.1766 REMARK 3 L33: 3.4284 L12: 0.2143 REMARK 3 L13: 0.7800 L23: 0.0096 REMARK 3 S TENSOR REMARK 3 S11: 0.1722 S12: -0.1606 S13: -0.0416 REMARK 3 S21: 0.5148 S22: -0.0941 S23: 0.0706 REMARK 3 S31: 0.2920 S32: -0.2016 S33: -0.0781 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 219 REMARK 3 ORIGIN FOR THE GROUP (A): -7.3564 13.5347 18.2777 REMARK 3 T TENSOR REMARK 3 T11: 0.0503 T22: 0.1112 REMARK 3 T33: 0.1726 T12: -0.0205 REMARK 3 T13: 0.0600 T23: 0.0109 REMARK 3 L TENSOR REMARK 3 L11: 1.6893 L22: 1.4178 REMARK 3 L33: 2.9260 L12: -0.0975 REMARK 3 L13: 1.4748 L23: -0.0643 REMARK 3 S TENSOR REMARK 3 S11: -0.0582 S12: 0.0395 S13: 0.1018 REMARK 3 S21: 0.1773 S22: -0.0411 S23: -0.0016 REMARK 3 S31: -0.0362 S32: 0.1136 S33: 0.0994 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 1 L 211 REMARK 3 ORIGIN FOR THE GROUP (A): -20.1895 -0.1815 21.6284 REMARK 3 T TENSOR REMARK 3 T11: 0.0901 T22: 0.2029 REMARK 3 T33: 0.2013 T12: -0.0895 REMARK 3 T13: 0.0688 T23: 0.0198 REMARK 3 L TENSOR REMARK 3 L11: 1.0001 L22: 0.6857 REMARK 3 L33: 2.0875 L12: 0.2300 REMARK 3 L13: 1.3945 L23: 0.6003 REMARK 3 S TENSOR REMARK 3 S11: 0.1522 S12: -0.0740 S13: -0.0198 REMARK 3 S21: 0.1746 S22: -0.1353 S23: 0.1107 REMARK 3 S31: 0.2842 S32: -0.2067 S33: -0.0169 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 8Z2V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-APR-24. REMARK 100 THE DEPOSITION ID IS D_1300046916. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-MAR-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 : PHOTON FACTORY REMARK 200 BEAMLINE : BL-1A 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 EIGER X 4M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM 7.2.2 REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58458 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890 REMARK 200 RESOLUTION RANGE LOW (A) : 56.480 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 4.900 REMARK 200 R MERGE (I) : 0.06400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.43600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.200 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 (%): 53.89 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM MGCL2, 20% PEG 3350, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K 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 48.32050 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.87600 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 48.32050 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.87600 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH H 533 LIES ON A SPECIAL POSITION. REMARK 375 HOH H 557 LIES ON A SPECIAL POSITION. 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 GLY A 29 REMARK 465 PHE A 30 REMARK 465 GLY A 31 REMARK 465 LYS A 32 REMARK 465 ARG A 33 REMARK 465 ARG A 34 REMARK 465 HIS A 35 REMARK 465 PRO A 36 REMARK 465 LYS A 37 REMARK 465 LYS A 38 REMARK 465 ASN A 189 REMARK 465 SER A 190 REMARK 465 VAL A 191 REMARK 465 ALA A 192 REMARK 465 ALA A 193 REMARK 465 LYS A 194 REMARK 465 SER A 195 REMARK 465 GLY A 196 REMARK 465 GLY A 197 REMARK 465 SER H 134 REMARK 465 LYS H 135 REMARK 465 SER H 136 REMARK 465 THR H 137 REMARK 465 SER H 138 REMARK 465 GLY H 139 REMARK 465 LYS H 220 REMARK 465 GLU H 221 REMARK 465 GLN H 222 REMARK 465 LYS H 223 REMARK 465 LEU H 224 REMARK 465 ILE H 225 REMARK 465 SER H 226 REMARK 465 GLU H 227 REMARK 465 GLU H 228 REMARK 465 ASP H 229 REMARK 465 LEU H 230 REMARK 465 ASN H 231 REMARK 465 SER H 232 REMARK 465 ALA H 233 REMARK 465 VAL H 234 REMARK 465 ASP H 235 REMARK 465 HIS H 236 REMARK 465 HIS H 237 REMARK 465 HIS H 238 REMARK 465 HIS H 239 REMARK 465 HIS H 240 REMARK 465 HIS H 241 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 GLU L 215 REMARK 465 GLN L 216 REMARK 465 LYS L 217 REMARK 465 LEU L 218 REMARK 465 ILE L 219 REMARK 465 SER L 220 REMARK 465 GLU L 221 REMARK 465 GLU L 222 REMARK 465 ASP L 223 REMARK 465 LEU L 224 REMARK 465 ASN L 225 REMARK 465 SER L 226 REMARK 465 ALA L 227 REMARK 465 VAL L 228 REMARK 465 ASP L 229 REMARK 465 HIS L 230 REMARK 465 HIS L 231 REMARK 465 HIS L 232 REMARK 465 HIS L 233 REMARK 465 HIS L 234 REMARK 465 HIS L 235 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 OE2 GLU L 161 O HOH L 301 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 GLY H 140 N GLY H 140 CA 0.108 REMARK 500 GLU H 154 CD GLU H 154 OE1 0.127 REMARK 500 SER H 193 CB SER H 193 OG 0.112 REMARK 500 GLU L 105 CD GLU L 105 OE1 0.067 REMARK 500 GLU L 165 CD GLU L 165 OE1 0.067 REMARK 500 GLU L 195 CD GLU L 195 OE1 0.079 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 A 96 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 ARG A 123 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG A 153 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES REMARK 500 ARG L 54 NE - CZ - NH2 ANGL. DEV. = -3.1 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 LYS A 45 -2.97 79.81 REMARK 500 ASN A 50 45.65 -66.19 REMARK 500 ALA A 58 -113.24 -103.21 REMARK 500 SER H 44 -134.48 45.15 REMARK 500 ALA H 92 168.49 177.57 REMARK 500 ASP H 150 59.03 77.32 REMARK 500 SER L 30 -119.78 48.21 REMARK 500 ALA L 51 -31.34 63.93 REMARK 500 ALA L 84 167.40 175.98 REMARK 500 ASN L 138 69.46 64.21 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 CA A 203 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 89 OE1 REMARK 620 2 GLU A 89 OE2 55.9 REMARK 620 3 GLU A 90 OE1 77.9 81.7 REMARK 620 4 GLU A 90 OE2 115.2 78.9 49.5 REMARK 620 5 ASP A 95 OD1 136.1 160.9 86.8 82.0 REMARK 620 6 ASP A 95 OD2 84.2 139.2 82.0 116.3 52.8 REMARK 620 7 THR A 125 O 93.5 109.6 158.9 148.3 86.3 77.9 REMARK 620 8 GLU A 126 OE2 138.5 87.0 117.7 68.3 84.9 133.5 81.4 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 204 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 90 OE2 REMARK 620 2 GLU A 126 OE1 119.9 REMARK 620 3 GLU A 126 OE2 68.6 51.7 REMARK 620 4 ASP A 129 OD1 156.9 80.6 132.1 REMARK 620 5 ASP A 131 OD2 87.2 146.0 143.0 78.7 REMARK 620 6 HOH A 304 O 75.5 85.9 78.5 97.1 123.2 REMARK 620 7 HOH A 334 O 83.8 137.2 138.8 73.4 59.6 64.9 REMARK 620 8 HOH A 353 O 99.0 78.0 79.1 95.7 77.5 157.5 137.0 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 202 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 140 NE2 REMARK 620 2 ASP A 147 OD1 122.9 REMARK 620 3 HIS A 182 ND1 109.9 104.4 REMARK 620 4 HOH A 348 O 97.0 121.9 97.9 REMARK 620 N 1 2 3 DBREF 8Z2V A 29 197 UNP Q15465 SHH_HUMAN 29 197 DBREF 8Z2V H 1 241 PDB 8Z2V 8Z2V 1 241 DBREF 8Z2V L 1 235 PDB 8Z2V 8Z2V 1 235 SEQRES 1 A 169 GLY PHE GLY LYS ARG ARG HIS PRO LYS LYS LEU THR PRO SEQRES 2 A 169 LEU ALA TYR LYS GLN PHE ILE PRO ASN VAL ALA GLU LYS SEQRES 3 A 169 THR LEU GLY ALA SER GLY ARG TYR GLU GLY LYS ILE SER SEQRES 4 A 169 ARG ASN SER GLU ARG PHE LYS GLU LEU THR PRO ASN TYR SEQRES 5 A 169 ASN PRO ASP ILE ILE PHE LYS ASP GLU GLU ASN THR GLY SEQRES 6 A 169 ALA ASP ARG LEU MET THR GLN ARG CYS LYS ASP LYS LEU SEQRES 7 A 169 ASN ALA LEU ALA ILE SER VAL MET ASN GLN TRP PRO GLY SEQRES 8 A 169 VAL LYS LEU ARG VAL THR GLU GLY TRP ASP GLU ASP GLY SEQRES 9 A 169 HIS HIS SER GLU GLU SER LEU HIS TYR GLU GLY ARG ALA SEQRES 10 A 169 VAL ASP ILE THR THR SER ASP ARG ASP ARG SER LYS TYR SEQRES 11 A 169 GLY MET LEU ALA ARG LEU ALA VAL GLU ALA GLY PHE ASP SEQRES 12 A 169 TRP VAL TYR TYR GLU SER LYS ALA HIS ILE HIS CYS SER SEQRES 13 A 169 VAL LYS ALA GLU ASN SER VAL ALA ALA LYS SER GLY GLY SEQRES 1 H 241 GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL ARG SEQRES 2 H 241 PRO GLY VAL SER VAL LYS ILE SER CYS LYS GLY SER GLY SEQRES 3 H 241 TYR THR PHE ILE ASP GLU ALA LEU HIS TRP VAL LYS GLN SEQRES 4 H 241 SER HIS ALA GLU SER LEU GLU TRP ILE GLY VAL ILE ARG SEQRES 5 H 241 PRO TYR SER GLY GLU THR ASN TYR ASN GLN LYS PHE LYS SEQRES 6 H 241 ASP LYS ALA THR MET THR VAL ASP ILE SER SER SER THR SEQRES 7 H 241 ALA TYR LEU GLU LEU ALA ARG LEU THR SER GLU ASP SER SEQRES 8 H 241 ALA ILE TYR TYR CYS ALA ARG ASP TRP GLU ALA GLY ASP SEQRES 9 H 241 PHE PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 H 241 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 H 241 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 H 241 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 H 241 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 H 241 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 H 241 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 H 241 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 H 241 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS GLU SEQRES 18 H 241 GLN LYS LEU ILE SER GLU GLU ASP LEU ASN SER ALA VAL SEQRES 19 H 241 ASP HIS HIS HIS HIS HIS HIS SEQRES 1 L 235 ASP ILE VAL MET THR GLN THR PRO LYS PHE LEU LEU VAL SEQRES 2 L 235 SER ALA GLY ASP LYS VAL THR ILE THR CYS LYS ALA SER SEQRES 3 L 235 GLN SER VAL SER ASN ASP LEU THR TRP TYR GLN GLN LYS SEQRES 4 L 235 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TYR ALA SER SEQRES 5 L 235 ASN ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 L 235 GLY TYR GLY THR ASP PHE THR PHE THR ILE SER THR VAL SEQRES 7 L 235 GLN ALA GLU ASP LEU ALA VAL TYR PHE CYS GLN GLN ASP SEQRES 8 L 235 TYR GLY SER PRO PRO THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 L 235 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 235 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 235 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 235 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 235 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 235 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 235 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 235 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 235 PHE ASN ARG GLY GLU CYS GLU GLN LYS LEU ILE SER GLU SEQRES 18 L 235 GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS SEQRES 19 L 235 HIS HET CL A 201 1 HET ZN A 202 1 HET CA A 203 1 HET CA A 204 1 HET GOL H 301 6 HETNAM CL CHLORIDE ION HETNAM ZN ZINC ION HETNAM CA CALCIUM ION HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 CL CL 1- FORMUL 5 ZN ZN 2+ FORMUL 6 CA 2(CA 2+) FORMUL 8 GOL C3 H8 O3 FORMUL 9 HOH *409(H2 O) HELIX 1 AA1 SER A 70 LEU A 76 5 7 HELIX 2 AA2 GLY A 93 ASP A 95 5 3 HELIX 3 AA3 THR A 99 TRP A 117 1 19 HELIX 4 AA4 SER A 138 GLY A 143 5 6 HELIX 5 AA5 ASP A 154 SER A 156 5 3 HELIX 6 AA6 LYS A 157 ALA A 168 1 12 HELIX 7 AA7 THR H 28 GLU H 32 5 5 HELIX 8 AA8 GLN H 62 LYS H 65 5 4 HELIX 9 AA9 THR H 87 SER H 91 5 5 HELIX 10 AB1 SER H 162 ALA H 164 5 3 HELIX 11 AB2 LYS H 207 ASN H 210 5 4 HELIX 12 AB3 GLN L 79 LEU L 83 5 5 HELIX 13 AB4 SER L 121 SER L 127 1 7 HELIX 14 AB5 LYS L 183 LYS L 188 1 6 SHEET 1 AA1 6 PHE A 47 ILE A 48 0 SHEET 2 AA1 6 TRP A 172 SER A 177 -1 O VAL A 173 N ILE A 48 SHEET 3 AA1 6 HIS A 180 SER A 184 -1 O HIS A 182 N TYR A 174 SHEET 4 AA1 6 ALA A 145 THR A 150 -1 N VAL A 146 O CYS A 183 SHEET 5 AA1 6 LEU A 122 GLU A 126 -1 N ARG A 123 O THR A 149 SHEET 6 AA1 6 ILE A 84 PHE A 86 1 N ILE A 85 O VAL A 124 SHEET 1 AA2 2 THR A 77 PRO A 78 0 SHEET 2 AA2 2 LEU A 97 MET A 98 -1 O MET A 98 N THR A 77 SHEET 1 AA3 4 GLN H 3 GLN H 6 0 SHEET 2 AA3 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA3 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AA3 4 ALA H 68 ASP H 73 -1 N THR H 71 O TYR H 80 SHEET 1 AA4 6 GLU H 10 VAL H 12 0 SHEET 2 AA4 6 THR H 113 VAL H 117 1 O THR H 116 N GLU H 10 SHEET 3 AA4 6 ALA H 92 ARG H 98 -1 N ALA H 92 O VAL H 115 SHEET 4 AA4 6 LEU H 34 SER H 40 -1 N GLN H 39 O ILE H 93 SHEET 5 AA4 6 SER H 44 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AA4 6 THR H 58 TYR H 60 -1 O ASN H 59 N VAL H 50 SHEET 1 AA5 4 GLU H 10 VAL H 12 0 SHEET 2 AA5 4 THR H 113 VAL H 117 1 O THR H 116 N GLU H 10 SHEET 3 AA5 4 ALA H 92 ARG H 98 -1 N ALA H 92 O VAL H 115 SHEET 4 AA5 4 TYR H 108 TRP H 109 -1 O TYR H 108 N ARG H 98 SHEET 1 AA6 4 SER H 126 LEU H 130 0 SHEET 2 AA6 4 THR H 141 TYR H 151 -1 O GLY H 145 N LEU H 130 SHEET 3 AA6 4 TYR H 182 PRO H 191 -1 O LEU H 184 N VAL H 148 SHEET 4 AA6 4 VAL H 169 THR H 171 -1 N HIS H 170 O VAL H 187 SHEET 1 AA7 4 SER H 126 LEU H 130 0 SHEET 2 AA7 4 THR H 141 TYR H 151 -1 O GLY H 145 N LEU H 130 SHEET 3 AA7 4 TYR H 182 PRO H 191 -1 O LEU H 184 N VAL H 148 SHEET 4 AA7 4 VAL H 175 LEU H 176 -1 N VAL H 175 O SER H 183 SHEET 1 AA8 3 THR H 157 TRP H 160 0 SHEET 2 AA8 3 ILE H 201 HIS H 206 -1 O ASN H 203 N SER H 159 SHEET 3 AA8 3 THR H 211 LYS H 216 -1 O VAL H 213 N VAL H 204 SHEET 1 AA9 4 MET L 4 THR L 7 0 SHEET 2 AA9 4 VAL L 19 ALA L 25 -1 O THR L 22 N THR L 7 SHEET 3 AA9 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21 SHEET 4 AA9 4 PHE L 62 GLY L 66 -1 N THR L 63 O THR L 74 SHEET 1 AB1 6 PHE L 10 SER L 14 0 SHEET 2 AB1 6 THR L 102 LYS L 107 1 O GLU L 105 N VAL L 13 SHEET 3 AB1 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AB1 6 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AB1 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB1 6 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AB2 4 PHE L 10 SER L 14 0 SHEET 2 AB2 4 THR L 102 LYS L 107 1 O GLU L 105 N VAL L 13 SHEET 3 AB2 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AB2 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB3 4 SER L 114 PHE L 118 0 SHEET 2 AB3 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB3 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AB3 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB4 4 ALA L 153 LEU L 154 0 SHEET 2 AB4 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB4 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB4 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.14 SSBOND 2 CYS H 146 CYS H 202 1555 1555 2.10 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.22 SSBOND 4 CYS L 134 CYS L 194 1555 1555 1.98 LINK OE1 GLU A 89 CA CA A 203 1555 1555 2.43 LINK OE2 GLU A 89 CA CA A 203 1555 1555 2.40 LINK OE1 GLU A 90 CA CA A 203 1555 1555 2.65 LINK OE2 GLU A 90 CA CA A 203 1555 1555 2.41 LINK OE2 GLU A 90 CA CA A 204 1555 1555 2.35 LINK OD1 ASP A 95 CA CA A 203 1555 1555 2.53 LINK OD2 ASP A 95 CA CA A 203 1555 1555 2.53 LINK O THR A 125 CA CA A 203 1555 1555 2.29 LINK OE2 GLU A 126 CA CA A 203 1555 1555 2.40 LINK OE1 GLU A 126 CA CA A 204 1555 1555 2.44 LINK OE2 GLU A 126 CA CA A 204 1555 1555 2.44 LINK OD1 ASP A 129 CA CA A 204 1555 1555 2.19 LINK OD2 ASP A 131 CA CA A 204 1555 1555 2.33 LINK NE2 HIS A 140 ZN ZN A 202 1555 1555 1.89 LINK OD1 ASP A 147 ZN ZN A 202 1555 1555 1.92 LINK ND1 HIS A 182 ZN ZN A 202 1555 1555 2.00 LINK ZN ZN A 202 O HOH A 348 1555 1555 2.30 LINK CA CA A 204 O HOH A 304 1555 1555 2.64 LINK CA CA A 204 O HOH A 334 1555 1555 3.08 LINK CA CA A 204 O HOH A 353 1555 1555 2.53 CISPEP 1 ILE A 48 PRO A 49 0 -0.90 CISPEP 2 PHE H 152 PRO H 153 0 -5.00 CISPEP 3 GLU H 154 PRO H 155 0 -6.62 CISPEP 4 THR L 7 PRO L 8 0 -3.99 CISPEP 5 SER L 94 PRO L 95 0 3.76 CISPEP 6 TYR L 140 PRO L 141 0 -0.58 CRYST1 96.641 69.752 119.270 90.00 108.73 90.00 C 1 2 1 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 0.010348 0.000000 0.003509 0.00000 SCALE2 0.000000 0.014337 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008853 0.00000