HEADER IMMUNE SYSTEM 05-MAR-25 9NN9 TITLE ISG15 COMPLEXED WITH NANOBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: UBIQUITIN-LIKE PROTEIN ISG15; COMPND 3 CHAIN: A, C, E; COMPND 4 FRAGMENT: RESIDUES 1-157; COMPND 5 SYNONYM: INTERFERON-INDUCED 15 KDA PROTEIN,INTERFERON-INDUCED 17 KDA COMPND 6 PROTEIN,IP17,UBIQUITIN CROSS-REACTIVE PROTEIN,HUCRP; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: NANOBODY; COMPND 11 CHAIN: B, D, F; COMPND 12 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: ISG15, G1P2, UCRP; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 10 ORGANISM_TAXID: 30538; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS UBIQUITIN-LIKE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR P.DABHADE,T.U.SCHWARTZ REVDAT 1 01-OCT-25 9NN9 0 JRNL AUTH J.GAN,P.DABHADE,C.WIJNE,W.MCKIBBEN,S.D.DRAGANOV,H.ALRAWILI, JRNL AUTH 2 Z.J.SUN,J.W.HOUGHTON,E.W.TATE,C.LE GALL,P.SURESH,N.PISHESHA, JRNL AUTH 3 A.PINTO-FERNANDEZ,T.U.SCHWARTZ,H.L.PLOEGH JRNL TITL IDENTIFICATION AND CHARACTERIZATION OF NANOBODIES SPECIFIC JRNL TITL 2 FOR THE HUMAN UBIQUITIN-LIKE ISG15 PROTEIN. JRNL REF J.BIOL.CHEM. V. 301 10564 2025 JRNL REFN ESSN 1083-351X JRNL PMID 40774387 JRNL DOI 10.1016/J.JBC.2025.110564 REMARK 2 REMARK 2 RESOLUTION. 2.59 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.27 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 36382 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.192 REMARK 3 R VALUE (WORKING SET) : 0.188 REMARK 3 FREE R VALUE : 0.244 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.240 REMARK 3 FREE R VALUE TEST SET COUNT : 2272 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 76.2700 - 6.5300 0.99 2179 145 0.1848 0.2235 REMARK 3 2 6.5300 - 5.1800 1.00 2150 144 0.1815 0.2086 REMARK 3 3 5.1800 - 4.5300 0.99 2138 143 0.1479 0.1899 REMARK 3 4 4.5300 - 4.1100 0.99 2139 141 0.1488 0.2061 REMARK 3 5 4.1100 - 3.8200 0.99 2106 139 0.1587 0.2188 REMARK 3 6 3.8200 - 3.5900 0.99 2126 141 0.1762 0.2397 REMARK 3 7 3.5900 - 3.4100 1.00 2151 144 0.1935 0.2698 REMARK 3 8 3.4100 - 3.2600 1.00 2118 141 0.1976 0.2918 REMARK 3 9 3.2600 - 3.1400 1.00 2159 143 0.2026 0.2824 REMARK 3 10 3.1400 - 3.0300 1.00 2117 141 0.2100 0.2500 REMARK 3 11 3.0300 - 2.9400 1.00 2131 144 0.2273 0.2936 REMARK 3 12 2.9400 - 2.8500 1.00 2135 142 0.2301 0.3113 REMARK 3 13 2.8500 - 2.7800 1.00 2146 144 0.2422 0.3175 REMARK 3 14 2.7800 - 2.7100 1.00 2132 141 0.2601 0.3399 REMARK 3 15 2.7100 - 2.6500 1.00 2121 141 0.2824 0.3395 REMARK 3 16 2.6500 - 2.5900 0.96 2062 138 0.2861 0.3242 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.620 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 6474 REMARK 3 ANGLE : 1.039 8772 REMARK 3 CHIRALITY : 0.055 988 REMARK 3 PLANARITY : 0.008 1120 REMARK 3 DIHEDRAL : 18.753 2349 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' REMARK 3 ORIGIN FOR THE GROUP (A): 5.4327 -53.2528 29.1630 REMARK 3 T TENSOR REMARK 3 T11: 0.2789 T22: 0.3613 REMARK 3 T33: 0.2742 T12: 0.0138 REMARK 3 T13: -0.0048 T23: -0.0511 REMARK 3 L TENSOR REMARK 3 L11: 1.3134 L22: 6.1655 REMARK 3 L33: 1.7665 L12: -0.0867 REMARK 3 L13: 0.1630 L23: -1.9488 REMARK 3 S TENSOR REMARK 3 S11: 0.1282 S12: 0.1053 S13: -0.0812 REMARK 3 S21: -0.2843 S22: -0.1077 S23: 0.2363 REMARK 3 S31: 0.1602 S32: 0.0285 S33: -0.0097 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' REMARK 3 ORIGIN FOR THE GROUP (A): 15.5359 -24.9856 37.9167 REMARK 3 T TENSOR REMARK 3 T11: 0.3093 T22: 0.3295 REMARK 3 T33: 0.3454 T12: -0.0123 REMARK 3 T13: 0.0050 T23: -0.0206 REMARK 3 L TENSOR REMARK 3 L11: 2.3770 L22: 4.1390 REMARK 3 L33: 1.4147 L12: 1.0121 REMARK 3 L13: 0.7422 L23: 0.0105 REMARK 3 S TENSOR REMARK 3 S11: -0.0244 S12: -0.0028 S13: 0.1733 REMARK 3 S21: 0.1065 S22: -0.1157 S23: -0.0499 REMARK 3 S31: 0.0309 S32: -0.0416 S33: 0.1307 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'C' REMARK 3 ORIGIN FOR THE GROUP (A): 30.4310 9.9970 71.4572 REMARK 3 T TENSOR REMARK 3 T11: 0.5320 T22: 0.4226 REMARK 3 T33: 0.3231 T12: -0.0171 REMARK 3 T13: -0.0670 T23: 0.0001 REMARK 3 L TENSOR REMARK 3 L11: 4.1046 L22: 2.6157 REMARK 3 L33: 1.7431 L12: 2.0636 REMARK 3 L13: -1.8375 L23: -1.1525 REMARK 3 S TENSOR REMARK 3 S11: 0.0729 S12: -0.3524 S13: 0.1181 REMARK 3 S21: 0.1746 S22: -0.2214 S23: -0.1239 REMARK 3 S31: -0.2318 S32: 0.2668 S33: 0.1718 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'D' REMARK 3 ORIGIN FOR THE GROUP (A): 16.2259 -17.1494 62.4527 REMARK 3 T TENSOR REMARK 3 T11: 0.5512 T22: 0.4170 REMARK 3 T33: 0.4114 T12: -0.0467 REMARK 3 T13: 0.0989 T23: 0.0212 REMARK 3 L TENSOR REMARK 3 L11: 2.3998 L22: 2.2936 REMARK 3 L33: 2.7402 L12: -0.2063 REMARK 3 L13: 0.2288 L23: 1.7580 REMARK 3 S TENSOR REMARK 3 S11: -0.0535 S12: -0.2037 S13: -0.2193 REMARK 3 S21: 0.1883 S22: -0.0192 S23: 0.1793 REMARK 3 S31: 0.0380 S32: -0.0683 S33: 0.0494 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'E' REMARK 3 ORIGIN FOR THE GROUP (A): 5.3101 -54.2601 56.9551 REMARK 3 T TENSOR REMARK 3 T11: 0.3261 T22: 0.3165 REMARK 3 T33: 0.3161 T12: 0.0007 REMARK 3 T13: 0.0463 T23: 0.0746 REMARK 3 L TENSOR REMARK 3 L11: 3.0453 L22: 2.7946 REMARK 3 L33: 3.1546 L12: 1.3729 REMARK 3 L13: 1.7725 L23: 2.0018 REMARK 3 S TENSOR REMARK 3 S11: -0.0834 S12: -0.0273 S13: -0.1369 REMARK 3 S21: -0.0338 S22: 0.0516 S23: -0.2672 REMARK 3 S31: -0.1096 S32: 0.1351 S33: 0.0013 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'F' REMARK 3 ORIGIN FOR THE GROUP (A): -25.5893 -56.6704 52.7863 REMARK 3 T TENSOR REMARK 3 T11: 0.2627 T22: 0.3501 REMARK 3 T33: 0.3808 T12: 0.0004 REMARK 3 T13: 0.0040 T23: -0.0697 REMARK 3 L TENSOR REMARK 3 L11: 5.3659 L22: 2.7049 REMARK 3 L33: 2.3756 L12: 0.3955 REMARK 3 L13: 1.0878 L23: -0.3261 REMARK 3 S TENSOR REMARK 3 S11: -0.0091 S12: -0.4642 S13: 0.2562 REMARK 3 S21: 0.0430 S22: -0.0641 S23: 0.3596 REMARK 3 S31: -0.0184 S32: -0.1375 S33: 0.1068 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9NN9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1000293519. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-FEB-24 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 : NSLS-II REMARK 200 BEAMLINE : 17-ID-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979338 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JUN 30, 2024 REMARK 200 BUILT=20241002 REMARK 200 DATA SCALING SOFTWARE : XSCALE VERSION JUN 30, 2024 REMARK 200 BUILT=20241002 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36396 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.590 REMARK 200 RESOLUTION RANGE LOW (A) : 99.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.13430 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.9100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.82630 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.260 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 (%): 57.44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25 % PEG 3350, 0.1 M TRISODIUM CITRATE REMARK 280 PH 5.6, 0.2 M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 57.23500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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 APPLY THE FOLLOWING TO CHAINS: A, B 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F 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 MET A 1 REMARK 465 GLY A 2 REMARK 465 GLY A 156 REMARK 465 GLY A 157 REMARK 465 SER A 158 REMARK 465 SER A 159 REMARK 465 HIS A 160 REMARK 465 HIS A 161 REMARK 465 HIS A 162 REMARK 465 HIS A 163 REMARK 465 HIS A 164 REMARK 465 HIS A 165 REMARK 465 GLY B 121 REMARK 465 GLY B 122 REMARK 465 LEU B 123 REMARK 465 PRO B 124 REMARK 465 GLU B 125 REMARK 465 THR B 126 REMARK 465 GLY B 127 REMARK 465 GLY B 128 REMARK 465 SER B 129 REMARK 465 SER B 130 REMARK 465 TYR B 131 REMARK 465 PRO B 132 REMARK 465 TYR B 133 REMARK 465 ASP B 134 REMARK 465 VAL B 135 REMARK 465 PRO B 136 REMARK 465 ASP B 137 REMARK 465 TYR B 138 REMARK 465 ALA B 139 REMARK 465 GLY B 140 REMARK 465 GLY B 141 REMARK 465 SER B 142 REMARK 465 SER B 143 REMARK 465 HIS B 144 REMARK 465 HIS B 145 REMARK 465 HIS B 146 REMARK 465 HIS B 147 REMARK 465 HIS B 148 REMARK 465 HIS B 149 REMARK 465 MET C 1 REMARK 465 GLY C 2 REMARK 465 GLY C 156 REMARK 465 GLY C 157 REMARK 465 SER C 158 REMARK 465 SER C 159 REMARK 465 HIS C 160 REMARK 465 HIS C 161 REMARK 465 HIS C 162 REMARK 465 HIS C 163 REMARK 465 HIS C 164 REMARK 465 HIS C 165 REMARK 465 GLY D 121 REMARK 465 GLY D 122 REMARK 465 LEU D 123 REMARK 465 PRO D 124 REMARK 465 GLU D 125 REMARK 465 THR D 126 REMARK 465 GLY D 127 REMARK 465 GLY D 128 REMARK 465 SER D 129 REMARK 465 SER D 130 REMARK 465 TYR D 131 REMARK 465 PRO D 132 REMARK 465 TYR D 133 REMARK 465 ASP D 134 REMARK 465 VAL D 135 REMARK 465 PRO D 136 REMARK 465 ASP D 137 REMARK 465 TYR D 138 REMARK 465 ALA D 139 REMARK 465 GLY D 140 REMARK 465 GLY D 141 REMARK 465 SER D 142 REMARK 465 SER D 143 REMARK 465 HIS D 144 REMARK 465 HIS D 145 REMARK 465 HIS D 146 REMARK 465 HIS D 147 REMARK 465 HIS D 148 REMARK 465 HIS D 149 REMARK 465 MET E 1 REMARK 465 GLY E 2 REMARK 465 SER E 21 REMARK 465 SER E 22 REMARK 465 GLY E 156 REMARK 465 GLY E 157 REMARK 465 SER E 158 REMARK 465 SER E 159 REMARK 465 HIS E 160 REMARK 465 HIS E 161 REMARK 465 HIS E 162 REMARK 465 HIS E 163 REMARK 465 HIS E 164 REMARK 465 HIS E 165 REMARK 465 GLY F 121 REMARK 465 GLY F 122 REMARK 465 LEU F 123 REMARK 465 PRO F 124 REMARK 465 GLU F 125 REMARK 465 THR F 126 REMARK 465 GLY F 127 REMARK 465 GLY F 128 REMARK 465 SER F 129 REMARK 465 SER F 130 REMARK 465 TYR F 131 REMARK 465 PRO F 132 REMARK 465 TYR F 133 REMARK 465 ASP F 134 REMARK 465 VAL F 135 REMARK 465 PRO F 136 REMARK 465 ASP F 137 REMARK 465 TYR F 138 REMARK 465 ALA F 139 REMARK 465 GLY F 140 REMARK 465 GLY F 141 REMARK 465 SER F 142 REMARK 465 SER F 143 REMARK 465 HIS F 144 REMARK 465 HIS F 145 REMARK 465 HIS F 146 REMARK 465 HIS F 147 REMARK 465 HIS F 148 REMARK 465 HIS F 149 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 C 57 CG CD NE CZ NH1 NH2 REMARK 470 ARG E 57 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 SER A 21 -93.06 -93.10 REMARK 500 PRO A 144 114.33 -37.23 REMARK 500 ARG B 27 -168.34 -104.33 REMARK 500 SER C 21 -122.63 60.44 REMARK 500 ILE C 36 17.70 -142.91 REMARK 500 GLN C 63 39.85 -98.09 REMARK 500 LEU C 65 79.64 -101.14 REMARK 500 LEU D 86 107.53 -57.90 REMARK 500 ARG E 57 36.25 -94.75 REMARK 500 LYS E 77 99.46 -55.35 REMARK 500 ASN F 77 66.74 32.67 REMARK 500 REMARK 500 REMARK: NULL DBREF 9NN9 A 1 157 UNP P05161 ISG15_HUMAN 1 157 DBREF 9NN9 B 1 149 PDB 9NN9 9NN9 1 149 DBREF 9NN9 C 1 157 UNP P05161 ISG15_HUMAN 1 157 DBREF 9NN9 D 1 149 PDB 9NN9 9NN9 1 149 DBREF 9NN9 E 1 157 UNP P05161 ISG15_HUMAN 1 157 DBREF 9NN9 F 1 149 PDB 9NN9 9NN9 1 149 SEQADV 9NN9 SER A 78 UNP P05161 CYS 78 ENGINEERED MUTATION SEQADV 9NN9 SER A 158 UNP P05161 EXPRESSION TAG SEQADV 9NN9 SER A 159 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS A 160 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS A 161 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS A 162 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS A 163 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS A 164 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS A 165 UNP P05161 EXPRESSION TAG SEQADV 9NN9 SER C 78 UNP P05161 CYS 78 ENGINEERED MUTATION SEQADV 9NN9 SER C 158 UNP P05161 EXPRESSION TAG SEQADV 9NN9 SER C 159 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS C 160 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS C 161 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS C 162 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS C 163 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS C 164 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS C 165 UNP P05161 EXPRESSION TAG SEQADV 9NN9 SER E 78 UNP P05161 CYS 78 ENGINEERED MUTATION SEQADV 9NN9 SER E 158 UNP P05161 EXPRESSION TAG SEQADV 9NN9 SER E 159 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS E 160 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS E 161 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS E 162 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS E 163 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS E 164 UNP P05161 EXPRESSION TAG SEQADV 9NN9 HIS E 165 UNP P05161 EXPRESSION TAG SEQRES 1 A 165 MET GLY TRP ASP LEU THR VAL LYS MET LEU ALA GLY ASN SEQRES 2 A 165 GLU PHE GLN VAL SER LEU SER SER SER MET SER VAL SER SEQRES 3 A 165 GLU LEU LYS ALA GLN ILE THR GLN LYS ILE GLY VAL HIS SEQRES 4 A 165 ALA PHE GLN GLN ARG LEU ALA VAL HIS PRO SER GLY VAL SEQRES 5 A 165 ALA LEU GLN ASP ARG VAL PRO LEU ALA SER GLN GLY LEU SEQRES 6 A 165 GLY PRO GLY SER THR VAL LEU LEU VAL VAL ASP LYS SER SEQRES 7 A 165 ASP GLU PRO LEU SER ILE LEU VAL ARG ASN ASN LYS GLY SEQRES 8 A 165 ARG SER SER THR TYR GLU VAL ARG LEU THR GLN THR VAL SEQRES 9 A 165 ALA HIS LEU LYS GLN GLN VAL SER GLY LEU GLU GLY VAL SEQRES 10 A 165 GLN ASP ASP LEU PHE TRP LEU THR PHE GLU GLY LYS PRO SEQRES 11 A 165 LEU GLU ASP GLN LEU PRO LEU GLY GLU TYR GLY LEU LYS SEQRES 12 A 165 PRO LEU SER THR VAL PHE MET ASN LEU ARG LEU ARG GLY SEQRES 13 A 165 GLY SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 149 GLN LEU GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 B 149 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 149 ARG THR PHE ALA GLY LEU SER VAL LYS TRP PHE ARG GLN SEQRES 4 B 149 PRO PRO GLY ALA GLU ARG GLU TRP VAL ALA HIS ILE THR SEQRES 5 B 149 SER THR GLY SER SER THR HIS TYR ALA ASP SER VAL LYS SEQRES 6 B 149 GLY ARG PHE THR ILE SER ARG ASP TYR ASP ARG ASN MET SEQRES 7 B 149 VAL TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP THR SEQRES 8 B 149 ALA VAL TYR TYR CYS HIS ALA SER THR LEU TRP PRO GLU SEQRES 9 B 149 LYS HIS GLN ASP TYR TRP GLY GLN GLY ILE GLN VAL THR SEQRES 10 B 149 VAL SER SER GLY GLY LEU PRO GLU THR GLY GLY SER SER SEQRES 11 B 149 TYR PRO TYR ASP VAL PRO ASP TYR ALA GLY GLY SER SER SEQRES 12 B 149 HIS HIS HIS HIS HIS HIS SEQRES 1 C 165 MET GLY TRP ASP LEU THR VAL LYS MET LEU ALA GLY ASN SEQRES 2 C 165 GLU PHE GLN VAL SER LEU SER SER SER MET SER VAL SER SEQRES 3 C 165 GLU LEU LYS ALA GLN ILE THR GLN LYS ILE GLY VAL HIS SEQRES 4 C 165 ALA PHE GLN GLN ARG LEU ALA VAL HIS PRO SER GLY VAL SEQRES 5 C 165 ALA LEU GLN ASP ARG VAL PRO LEU ALA SER GLN GLY LEU SEQRES 6 C 165 GLY PRO GLY SER THR VAL LEU LEU VAL VAL ASP LYS SER SEQRES 7 C 165 ASP GLU PRO LEU SER ILE LEU VAL ARG ASN ASN LYS GLY SEQRES 8 C 165 ARG SER SER THR TYR GLU VAL ARG LEU THR GLN THR VAL SEQRES 9 C 165 ALA HIS LEU LYS GLN GLN VAL SER GLY LEU GLU GLY VAL SEQRES 10 C 165 GLN ASP ASP LEU PHE TRP LEU THR PHE GLU GLY LYS PRO SEQRES 11 C 165 LEU GLU ASP GLN LEU PRO LEU GLY GLU TYR GLY LEU LYS SEQRES 12 C 165 PRO LEU SER THR VAL PHE MET ASN LEU ARG LEU ARG GLY SEQRES 13 C 165 GLY SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 D 149 GLN LEU GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 D 149 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 149 ARG THR PHE ALA GLY LEU SER VAL LYS TRP PHE ARG GLN SEQRES 4 D 149 PRO PRO GLY ALA GLU ARG GLU TRP VAL ALA HIS ILE THR SEQRES 5 D 149 SER THR GLY SER SER THR HIS TYR ALA ASP SER VAL LYS SEQRES 6 D 149 GLY ARG PHE THR ILE SER ARG ASP TYR ASP ARG ASN MET SEQRES 7 D 149 VAL TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP THR SEQRES 8 D 149 ALA VAL TYR TYR CYS HIS ALA SER THR LEU TRP PRO GLU SEQRES 9 D 149 LYS HIS GLN ASP TYR TRP GLY GLN GLY ILE GLN VAL THR SEQRES 10 D 149 VAL SER SER GLY GLY LEU PRO GLU THR GLY GLY SER SER SEQRES 11 D 149 TYR PRO TYR ASP VAL PRO ASP TYR ALA GLY GLY SER SER SEQRES 12 D 149 HIS HIS HIS HIS HIS HIS SEQRES 1 E 165 MET GLY TRP ASP LEU THR VAL LYS MET LEU ALA GLY ASN SEQRES 2 E 165 GLU PHE GLN VAL SER LEU SER SER SER MET SER VAL SER SEQRES 3 E 165 GLU LEU LYS ALA GLN ILE THR GLN LYS ILE GLY VAL HIS SEQRES 4 E 165 ALA PHE GLN GLN ARG LEU ALA VAL HIS PRO SER GLY VAL SEQRES 5 E 165 ALA LEU GLN ASP ARG VAL PRO LEU ALA SER GLN GLY LEU SEQRES 6 E 165 GLY PRO GLY SER THR VAL LEU LEU VAL VAL ASP LYS SER SEQRES 7 E 165 ASP GLU PRO LEU SER ILE LEU VAL ARG ASN ASN LYS GLY SEQRES 8 E 165 ARG SER SER THR TYR GLU VAL ARG LEU THR GLN THR VAL SEQRES 9 E 165 ALA HIS LEU LYS GLN GLN VAL SER GLY LEU GLU GLY VAL SEQRES 10 E 165 GLN ASP ASP LEU PHE TRP LEU THR PHE GLU GLY LYS PRO SEQRES 11 E 165 LEU GLU ASP GLN LEU PRO LEU GLY GLU TYR GLY LEU LYS SEQRES 12 E 165 PRO LEU SER THR VAL PHE MET ASN LEU ARG LEU ARG GLY SEQRES 13 E 165 GLY SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 F 149 GLN LEU GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 F 149 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 149 ARG THR PHE ALA GLY LEU SER VAL LYS TRP PHE ARG GLN SEQRES 4 F 149 PRO PRO GLY ALA GLU ARG GLU TRP VAL ALA HIS ILE THR SEQRES 5 F 149 SER THR GLY SER SER THR HIS TYR ALA ASP SER VAL LYS SEQRES 6 F 149 GLY ARG PHE THR ILE SER ARG ASP TYR ASP ARG ASN MET SEQRES 7 F 149 VAL TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP THR SEQRES 8 F 149 ALA VAL TYR TYR CYS HIS ALA SER THR LEU TRP PRO GLU SEQRES 9 F 149 LYS HIS GLN ASP TYR TRP GLY GLN GLY ILE GLN VAL THR SEQRES 10 F 149 VAL SER SER GLY GLY LEU PRO GLU THR GLY GLY SER SER SEQRES 11 F 149 TYR PRO TYR ASP VAL PRO ASP TYR ALA GLY GLY SER SER SEQRES 12 F 149 HIS HIS HIS HIS HIS HIS HET EDO A 201 4 HET SO4 A 202 5 HET EDO D 201 4 HET EDO F 201 4 HETNAM EDO 1,2-ETHANEDIOL HETNAM SO4 SULFATE ION HETSYN EDO ETHYLENE GLYCOL FORMUL 7 EDO 3(C2 H6 O2) FORMUL 8 SO4 O4 S 2- FORMUL 11 HOH *158(H2 O) HELIX 1 AA1 SER A 24 GLY A 37 1 14 HELIX 2 AA2 HIS A 39 PHE A 41 5 3 HELIX 3 AA3 THR A 103 GLY A 116 1 14 HELIX 4 AA4 GLN A 118 ASP A 120 5 3 HELIX 5 AA5 PRO A 136 GLY A 141 5 6 HELIX 6 AA6 ASP B 62 LYS B 65 5 4 HELIX 7 AA7 TYR B 74 ARG B 76 5 3 HELIX 8 AA8 LYS B 87 THR B 91 5 5 HELIX 9 AA9 LEU C 10 GLY C 12 5 3 HELIX 10 AB1 SER C 24 GLY C 37 1 14 HELIX 11 AB2 HIS C 39 PHE C 41 5 3 HELIX 12 AB3 PRO C 59 GLN C 63 5 5 HELIX 13 AB4 THR C 103 GLY C 116 1 14 HELIX 14 AB5 GLN C 118 ASP C 120 5 3 HELIX 15 AB6 PRO C 136 GLY C 141 5 6 HELIX 16 AB7 LYS D 87 THR D 91 5 5 HELIX 17 AB8 SER E 24 GLY E 37 1 14 HELIX 18 AB9 HIS E 39 PHE E 41 5 3 HELIX 19 AC1 PRO E 59 GLY E 64 5 6 HELIX 20 AC2 THR E 103 GLY E 116 1 14 HELIX 21 AC3 GLN E 118 ASP E 120 5 3 HELIX 22 AC4 PRO E 136 GLY E 141 5 6 HELIX 23 AC5 TYR F 74 ARG F 76 5 3 HELIX 24 AC6 LYS F 87 THR F 91 5 5 SHEET 1 AA1 4 GLU A 14 SER A 18 0 SHEET 2 AA1 4 ASP A 4 MET A 9 -1 N VAL A 7 O PHE A 15 SHEET 3 AA1 4 THR A 70 VAL A 75 1 O VAL A 71 N THR A 6 SHEET 4 AA1 4 GLN A 43 VAL A 47 -1 N ARG A 44 O VAL A 74 SHEET 1 AA2 5 SER A 93 VAL A 98 0 SHEET 2 AA2 5 LEU A 82 ARG A 87 -1 N LEU A 82 O VAL A 98 SHEET 3 AA2 5 THR A 147 LEU A 152 1 O VAL A 148 N LEU A 85 SHEET 4 AA2 5 PHE A 122 PHE A 126 -1 N TRP A 123 O ASN A 151 SHEET 5 AA2 5 LYS A 129 PRO A 130 -1 O LYS A 129 N PHE A 126 SHEET 1 AA3 4 LEU B 4 THR B 7 0 SHEET 2 AA3 4 LEU B 18 ALA B 24 -1 O ALA B 23 N VAL B 5 SHEET 3 AA3 4 MET B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AA3 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA4 6 GLY B 10 GLN B 13 0 SHEET 2 AA4 6 ILE B 114 SER B 119 1 O SER B 119 N VAL B 12 SHEET 3 AA4 6 ALA B 92 SER B 99 -1 N TYR B 94 O ILE B 114 SHEET 4 AA4 6 SER B 33 GLN B 39 -1 N PHE B 37 O TYR B 95 SHEET 5 AA4 6 GLU B 46 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA4 6 THR B 58 TYR B 60 -1 O HIS B 59 N HIS B 50 SHEET 1 AA5 4 GLY B 10 GLN B 13 0 SHEET 2 AA5 4 ILE B 114 SER B 119 1 O SER B 119 N VAL B 12 SHEET 3 AA5 4 ALA B 92 SER B 99 -1 N TYR B 94 O ILE B 114 SHEET 4 AA5 4 ASP B 108 TRP B 110 -1 O TYR B 109 N ALA B 98 SHEET 1 AA6 4 GLU C 14 SER C 18 0 SHEET 2 AA6 4 ASP C 4 LYS C 8 -1 N VAL C 7 O PHE C 15 SHEET 3 AA6 4 THR C 70 VAL C 75 1 O VAL C 71 N LYS C 8 SHEET 4 AA6 4 GLN C 43 VAL C 47 -1 N ARG C 44 O VAL C 74 SHEET 1 AA7 5 SER C 93 VAL C 98 0 SHEET 2 AA7 5 LEU C 82 ARG C 87 -1 N ILE C 84 O TYR C 96 SHEET 3 AA7 5 THR C 147 LEU C 152 1 O VAL C 148 N LEU C 85 SHEET 4 AA7 5 PHE C 122 PHE C 126 -1 N THR C 125 O PHE C 149 SHEET 5 AA7 5 LYS C 129 PRO C 130 -1 O LYS C 129 N PHE C 126 SHEET 1 AA8 4 GLN D 3 THR D 7 0 SHEET 2 AA8 4 LEU D 18 SER D 25 -1 O ALA D 23 N VAL D 5 SHEET 3 AA8 4 MET D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 4 AA8 4 PHE D 68 ASP D 73 -1 N ASP D 73 O MET D 78 SHEET 1 AA9 2 VAL D 12 GLN D 13 0 SHEET 2 AA9 2 VAL D 118 SER D 119 1 O SER D 119 N VAL D 12 SHEET 1 AB1 5 THR D 58 TYR D 60 0 SHEET 2 AB1 5 GLU D 46 ILE D 51 -1 N HIS D 50 O HIS D 59 SHEET 3 AB1 5 SER D 33 GLN D 39 -1 N VAL D 34 O ILE D 51 SHEET 4 AB1 5 ALA D 92 SER D 99 -1 O TYR D 95 N PHE D 37 SHEET 5 AB1 5 ASP D 108 TRP D 110 -1 O TYR D 109 N ALA D 98 SHEET 1 AB2 5 THR D 58 TYR D 60 0 SHEET 2 AB2 5 GLU D 46 ILE D 51 -1 N HIS D 50 O HIS D 59 SHEET 3 AB2 5 SER D 33 GLN D 39 -1 N VAL D 34 O ILE D 51 SHEET 4 AB2 5 ALA D 92 SER D 99 -1 O TYR D 95 N PHE D 37 SHEET 5 AB2 5 ILE D 114 VAL D 116 -1 O ILE D 114 N TYR D 94 SHEET 1 AB3 4 GLU E 14 SER E 18 0 SHEET 2 AB3 4 ASP E 4 MET E 9 -1 N VAL E 7 O PHE E 15 SHEET 3 AB3 4 SER E 69 VAL E 75 1 O LEU E 73 N LYS E 8 SHEET 4 AB3 4 GLN E 43 VAL E 47 -1 N ARG E 44 O VAL E 74 SHEET 1 AB4 5 SER E 93 VAL E 98 0 SHEET 2 AB4 5 LEU E 82 ARG E 87 -1 N LEU E 82 O VAL E 98 SHEET 3 AB4 5 THR E 147 LEU E 152 1 O VAL E 148 N LEU E 85 SHEET 4 AB4 5 PHE E 122 PHE E 126 -1 N THR E 125 O PHE E 149 SHEET 5 AB4 5 LYS E 129 PRO E 130 -1 O LYS E 129 N PHE E 126 SHEET 1 AB5 4 GLN F 3 THR F 7 0 SHEET 2 AB5 4 LEU F 18 SER F 25 -1 O SER F 21 N THR F 7 SHEET 3 AB5 4 MET F 78 MET F 83 -1 O LEU F 81 N LEU F 20 SHEET 4 AB5 4 PHE F 68 ASP F 73 -1 N THR F 69 O GLN F 82 SHEET 1 AB6 6 GLY F 10 GLN F 13 0 SHEET 2 AB6 6 ILE F 114 SER F 119 1 O THR F 117 N GLY F 10 SHEET 3 AB6 6 ALA F 92 SER F 99 -1 N TYR F 94 O ILE F 114 SHEET 4 AB6 6 SER F 33 GLN F 39 -1 N PHE F 37 O TYR F 95 SHEET 5 AB6 6 GLU F 46 ILE F 51 -1 O ILE F 51 N VAL F 34 SHEET 6 AB6 6 THR F 58 TYR F 60 -1 O HIS F 59 N HIS F 50 SHEET 1 AB7 4 GLY F 10 GLN F 13 0 SHEET 2 AB7 4 ILE F 114 SER F 119 1 O THR F 117 N GLY F 10 SHEET 3 AB7 4 ALA F 92 SER F 99 -1 N TYR F 94 O ILE F 114 SHEET 4 AB7 4 ASP F 108 TRP F 110 -1 O TYR F 109 N ALA F 98 SSBOND 1 CYS B 22 CYS B 96 1555 1555 2.05 SSBOND 2 CYS D 22 CYS D 96 1555 1555 2.03 SSBOND 3 CYS F 22 CYS F 96 1555 1555 2.06 CISPEP 1 HIS A 48 PRO A 49 0 13.36 CISPEP 2 TRP B 102 PRO B 103 0 6.02 CISPEP 3 HIS C 48 PRO C 49 0 6.46 CISPEP 4 TRP D 102 PRO D 103 0 7.82 CISPEP 5 HIS E 48 PRO E 49 0 4.46 CISPEP 6 TRP F 102 PRO F 103 0 8.71 CRYST1 68.460 114.470 79.290 90.00 105.86 90.00 P 1 21 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 0.014607 0.000000 0.004150 0.00000 SCALE2 0.000000 0.008736 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013111 0.00000