HEADER IMMUNE SYSTEM 26-MAR-25 9U8G TITLE CRYSTAL STRUCTURE OF TMPRSS2 IN COMPLEX WITH NANOBODY77_10 COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSMEMBRANE PROTEASE SERINE 2 NON-CATALYTIC CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 OTHER_DETAILS: WE CHOOSE THE ECTODOMAIN OF TRANSMEMBRANE PROTEASE COMPND 7 SERINE 2 (RESIDUES: 109-492) FOR EXPRESSION WITH A 6XHIS TAG AT C- COMPND 8 TERMINI. RESIDUES 250-255 RESPONSIBLE FOR AUTOCLEAVAGE ARE COMPND 9 SUBSTITUTED WITH ENTEROKINASE CLEAVAGE SITE DDDDK. THE RECOMBINANT COMPND 10 PROTEIN WAS CLEAVED INTO TWO CHAINS IN THE PURIFICATION.; COMPND 11 MOL_ID: 2; COMPND 12 MOLECULE: TRANSMEMBRANE PROTEASE SERINE 2 CATALYTIC CHAIN; COMPND 13 CHAIN: B, D; COMPND 14 ENGINEERED: YES; COMPND 15 OTHER_DETAILS: WE CHOOSE THE ECTODOMAIN OF TRANSMEMBRANE PROTEASE COMPND 16 SERINE 2 (RESIDUES: 109-492) FOR EXPRESSION WITH A 6XHIS TAG AT C- COMPND 17 TERMINI. RESIDUES 250-255 RESPONSIBLE FOR AUTOCLEAVAGE ARE COMPND 18 SUBSTITUTED WITH ENTEROKINASE CLEAVAGE SITE DDDDK. THE RECOMBINANT COMPND 19 PROTEIN WAS CLEAVED INTO TWO CHAINS IN THE PURIFICATION.; COMPND 20 MOL_ID: 3; COMPND 21 MOLECULE: NANOBODY; COMPND 22 CHAIN: E, F; COMPND 23 ENGINEERED: YES; COMPND 24 OTHER_DETAILS: THE RECOMBINANT PROTEIN ENCOMPASSES A C-TERMINAL COMPND 25 LINKER ("GS") FOLLOWED BY A 6 X HIS TAG. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: TMPRSS2, PRSS10; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: TMPRSS2, PRSS10; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 17 ORGANISM_TAXID: 30538; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS COMPLEX, ANTIBODY, HOST PROTEASE, ANTIVIRAL PROTEIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Y.DUAN,Z.ZHAO,X.LIU,H.WANG,H.YANG REVDAT 1 30-JUL-25 9U8G 0 JRNL AUTH Z.ZHAO,Q.YANG,X.LIU,M.LI,Y.DUAN,M.DU,A.ZHOU,H.LIU,Y.HE, JRNL AUTH 2 W.WANG,Y.LU,X.ZHANG,H.WANG,X.YANG,H.ZHANG,X.CHEN,Z.RAO, JRNL AUTH 3 H.YANG JRNL TITL THE CRYSTAL STRUCTURE OF CORONAVIRUS RBD-TMPRSS2 COMPLEX JRNL TITL 2 PROVIDES BASIS FOR THE DISCOVERY OF THERAPEUTIC ANTIBODIES. JRNL REF NAT COMMUN V. 16 6636 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 40681508 JRNL DOI 10.1038/S41467-025-62023-2 REMARK 2 REMARK 2 RESOLUTION. 2.00 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) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.29 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6 REMARK 3 NUMBER OF REFLECTIONS : 81780 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.195 REMARK 3 R VALUE (WORKING SET) : 0.193 REMARK 3 FREE R VALUE : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4088 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 18.2900 - 6.0700 0.94 2605 138 0.1600 0.1832 REMARK 3 2 6.0700 - 4.8500 0.97 2693 142 0.1581 0.1967 REMARK 3 3 4.8500 - 4.2400 0.98 2713 142 0.1370 0.1455 REMARK 3 4 4.2400 - 3.8600 0.98 2718 143 0.1580 0.2031 REMARK 3 5 3.8600 - 3.5900 0.98 2697 142 0.1690 0.1900 REMARK 3 6 3.5900 - 3.3800 0.97 2696 142 0.1798 0.2115 REMARK 3 7 3.3800 - 3.2100 0.97 2679 141 0.1959 0.2746 REMARK 3 8 3.2100 - 3.0700 0.98 2717 143 0.1963 0.2159 REMARK 3 9 3.0700 - 2.9500 0.98 2731 144 0.2058 0.2268 REMARK 3 10 2.9500 - 2.8500 0.97 2707 142 0.2052 0.2632 REMARK 3 11 2.8500 - 2.7600 0.97 2687 142 0.2040 0.2813 REMARK 3 12 2.7600 - 2.6800 0.97 2681 141 0.2055 0.2566 REMARK 3 13 2.6800 - 2.6100 0.98 2686 142 0.1974 0.2444 REMARK 3 14 2.6100 - 2.5500 0.97 2733 143 0.2018 0.2348 REMARK 3 15 2.5500 - 2.4900 0.97 2690 142 0.2158 0.2527 REMARK 3 16 2.4900 - 2.4400 0.97 2713 143 0.2188 0.2996 REMARK 3 17 2.4400 - 2.3900 0.97 2679 141 0.2192 0.2242 REMARK 3 18 2.3900 - 2.3400 0.97 2687 141 0.2202 0.2914 REMARK 3 19 2.3400 - 2.3000 0.96 2698 142 0.2319 0.2605 REMARK 3 20 2.3000 - 2.2600 0.97 2619 138 0.2463 0.3261 REMARK 3 21 2.2600 - 2.2300 0.97 2732 144 0.2677 0.3302 REMARK 3 22 2.2300 - 2.1900 0.96 2631 138 0.2635 0.3211 REMARK 3 23 2.1900 - 2.1600 0.96 2683 141 0.2643 0.3250 REMARK 3 24 2.1600 - 2.1300 0.96 2679 142 0.2638 0.2912 REMARK 3 25 2.1300 - 2.1000 0.96 2633 138 0.2772 0.3146 REMARK 3 26 2.1000 - 2.0700 0.96 2677 140 0.2810 0.3302 REMARK 3 27 2.0700 - 2.0500 0.95 2589 135 0.2908 0.3151 REMARK 3 28 2.0500 - 2.0200 0.96 2696 142 0.3146 0.3221 REMARK 3 29 2.0200 - 2.0000 0.92 2543 134 0.3238 0.3472 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) : 0.260 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.990 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 : 0.004 7831 REMARK 3 ANGLE : 0.719 10660 REMARK 3 CHIRALITY : 0.051 1143 REMARK 3 PLANARITY : 0.006 1382 REMARK 3 DIHEDRAL : 13.234 2789 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 9U8G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 01-APR-25. REMARK 100 THE DEPOSITION ID IS D_1300057877. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-MAR-25 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 : SSRF REMARK 200 BEAMLINE : BL10U2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979183 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 REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81800 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 18.290 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2 REMARK 200 DATA REDUNDANCY : 3.180 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.1800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12 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 : 1.670 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 (%): 55.41 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES/ SODIUM HYDROXIDE PH 7.0, REMARK 280 10% W/V PEG 6000, EVAPORATION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 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: 5460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20470 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E 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: 5450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 109 REMARK 465 GLY A 110 REMARK 465 SER A 111 REMARK 465 LYS A 112 REMARK 465 ASN A 249 REMARK 465 ASP A 250 REMARK 465 ASP A 251 REMARK 465 ASP A 252 REMARK 465 ASP A 253 REMARK 465 LYS A 254 REMARK 465 PHE B 494 REMARK 465 VAL B 495 REMARK 465 GLU B 496 REMARK 465 HIS B 497 REMARK 465 HIS B 498 REMARK 465 HIS B 499 REMARK 465 HIS B 500 REMARK 465 HIS B 501 REMARK 465 HIS B 502 REMARK 465 HIS B 503 REMARK 465 HIS B 504 REMARK 465 MET C 109 REMARK 465 GLY C 110 REMARK 465 SER C 111 REMARK 465 LYS C 112 REMARK 465 ASP C 202 REMARK 465 ASP C 203 REMARK 465 SER C 204 REMARK 465 GLY C 205 REMARK 465 ASN C 249 REMARK 465 ASP C 250 REMARK 465 ASP C 251 REMARK 465 ASP C 252 REMARK 465 ASP C 253 REMARK 465 LYS C 254 REMARK 465 PHE D 494 REMARK 465 VAL D 495 REMARK 465 GLU D 496 REMARK 465 HIS D 497 REMARK 465 HIS D 498 REMARK 465 HIS D 499 REMARK 465 HIS D 500 REMARK 465 HIS D 501 REMARK 465 HIS D 502 REMARK 465 HIS D 503 REMARK 465 HIS D 504 REMARK 465 ALA E 1 REMARK 465 TRP E 113 REMARK 465 GLY E 114 REMARK 465 GLY E 124 REMARK 465 SER E 125 REMARK 465 HIS E 126 REMARK 465 HIS E 127 REMARK 465 HIS E 128 REMARK 465 HIS E 129 REMARK 465 HIS E 130 REMARK 465 HIS E 131 REMARK 465 ALA F 1 REMARK 465 TRP F 113 REMARK 465 GLY F 114 REMARK 465 GLY F 124 REMARK 465 SER F 125 REMARK 465 HIS F 126 REMARK 465 HIS F 127 REMARK 465 HIS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 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 ASP A 121 CG OD1 OD2 REMARK 470 GLN A 198 CG CD OE1 NE2 REMARK 470 GLU B 260 CG CD OE1 OE2 REMARK 470 LYS B 340 CG CD CE NZ REMARK 470 LYS B 390 CG CD CE NZ REMARK 470 ARG B 409 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 413 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 493 CG CD OE1 OE2 REMARK 470 ASP C 121 CG OD1 OD2 REMARK 470 ASN C 192 CG OD1 ND2 REMARK 470 GLU D 260 CG CD OE1 OE2 REMARK 470 TYR D 322 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS D 340 CG CD CE NZ REMARK 470 LYS D 390 CG CD CE NZ REMARK 470 ARG D 409 CG CD NE CZ NH1 NH2 REMARK 470 ARG D 413 CG CD NE CZ NH1 NH2 REMARK 470 TYR D 414 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN D 431 CG CD OE1 NE2 REMARK 470 GLU D 493 CG CD OE1 OE2 REMARK 470 GLN E 5 CG CD OE1 NE2 REMARK 470 PHE E 11 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN E 13 CG CD OE1 NE2 REMARK 470 LYS E 43 CG CD CE NZ REMARK 470 ARG E 87 CG CD NE CZ NH1 NH2 REMARK 470 GLU E 89 CG CD OE1 OE2 REMARK 470 ARG E 110 CG CD NE CZ NH1 NH2 REMARK 470 GLN E 115 CG CD OE1 NE2 REMARK 470 SER E 123 OG REMARK 470 GLU F 89 CG CD OE1 OE2 REMARK 470 ARG F 110 CG CD NE CZ NH1 NH2 REMARK 470 GLN F 115 CG CD OE1 NE2 REMARK 470 SER F 123 OG 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 CYS A 120 88.28 -68.37 REMARK 500 ASP A 121 -116.38 53.81 REMARK 500 LYS A 191 -121.15 56.86 REMARK 500 TYR A 195 -70.55 -117.21 REMARK 500 ASN A 247 -155.72 -129.41 REMARK 500 MET B 320 73.08 -100.07 REMARK 500 ASN B 358 -155.01 -155.63 REMARK 500 VAL B 415 -92.82 -118.57 REMARK 500 ASN B 433 -30.53 75.71 REMARK 500 CYS C 120 88.62 -67.44 REMARK 500 ASP C 121 -117.58 53.65 REMARK 500 LYS C 191 -118.72 52.77 REMARK 500 TYR C 195 -70.55 -115.62 REMARK 500 ASN C 247 -155.63 -127.77 REMARK 500 MET D 320 73.35 -101.07 REMARK 500 ASN D 358 -155.07 -154.85 REMARK 500 VAL D 415 -90.42 -120.69 REMARK 500 ASN D 433 -30.46 75.55 REMARK 500 THR E 55 15.07 59.90 REMARK 500 TRP E 111 37.87 -80.65 REMARK 500 THR F 55 14.99 58.83 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH B 883 DISTANCE = 5.83 ANGSTROMS 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 301 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN A 131 O REMARK 620 2 ASP A 134 OD1 88.1 REMARK 620 3 VAL A 136 O 170.9 83.4 REMARK 620 4 ASP A 144 OD2 99.1 166.9 89.9 REMARK 620 5 GLU A 145 OE2 98.0 80.1 83.7 88.0 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 301 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN C 131 O REMARK 620 2 ASP C 134 OD1 87.7 REMARK 620 3 VAL C 136 O 174.4 87.0 REMARK 620 4 ASP C 144 OD2 97.4 165.8 88.1 REMARK 620 5 GLU C 145 OE2 98.1 79.3 82.5 86.9 REMARK 620 N 1 2 3 4 DBREF 9U8G A 109 254 UNP O15393 TMPS2_HUMAN 109 254 DBREF 9U8G B 256 492 UNP O15393 TMPS2_HUMAN 256 492 DBREF 9U8G C 109 254 UNP O15393 TMPS2_HUMAN 109 254 DBREF 9U8G D 256 492 UNP O15393 TMPS2_HUMAN 256 492 DBREF 9U8G E 1 131 PDB 9U8G 9U8G 1 131 DBREF 9U8G F 1 131 PDB 9U8G 9U8G 1 131 SEQADV 9U8G ASP A 250 UNP O15393 SER 250 ENGINEERED MUTATION SEQADV 9U8G ASP A 251 UNP O15393 SER 251 ENGINEERED MUTATION SEQADV 9U8G ASP A 252 UNP O15393 ARG 252 ENGINEERED MUTATION SEQADV 9U8G ASP A 253 UNP O15393 GLN 253 ENGINEERED MUTATION SEQADV 9U8G LYS A 254 UNP O15393 SER 254 ENGINEERED MUTATION SEQADV 9U8G GLU B 493 UNP O15393 EXPRESSION TAG SEQADV 9U8G PHE B 494 UNP O15393 EXPRESSION TAG SEQADV 9U8G VAL B 495 UNP O15393 EXPRESSION TAG SEQADV 9U8G GLU B 496 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS B 497 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS B 498 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS B 499 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS B 500 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS B 501 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS B 502 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS B 503 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS B 504 UNP O15393 EXPRESSION TAG SEQADV 9U8G ASP C 250 UNP O15393 SER 250 ENGINEERED MUTATION SEQADV 9U8G ASP C 251 UNP O15393 SER 251 ENGINEERED MUTATION SEQADV 9U8G ASP C 252 UNP O15393 ARG 252 ENGINEERED MUTATION SEQADV 9U8G ASP C 253 UNP O15393 GLN 253 ENGINEERED MUTATION SEQADV 9U8G LYS C 254 UNP O15393 SER 254 ENGINEERED MUTATION SEQADV 9U8G GLU D 493 UNP O15393 EXPRESSION TAG SEQADV 9U8G PHE D 494 UNP O15393 EXPRESSION TAG SEQADV 9U8G VAL D 495 UNP O15393 EXPRESSION TAG SEQADV 9U8G GLU D 496 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS D 497 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS D 498 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS D 499 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS D 500 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS D 501 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS D 502 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS D 503 UNP O15393 EXPRESSION TAG SEQADV 9U8G HIS D 504 UNP O15393 EXPRESSION TAG SEQRES 1 A 146 MET GLY SER LYS CYS SER ASN SER GLY ILE GLU CYS ASP SEQRES 2 A 146 SER SER GLY THR CYS ILE ASN PRO SER ASN TRP CYS ASP SEQRES 3 A 146 GLY VAL SER HIS CYS PRO GLY GLY GLU ASP GLU ASN ARG SEQRES 4 A 146 CYS VAL ARG LEU TYR GLY PRO ASN PHE ILE LEU GLN VAL SEQRES 5 A 146 TYR SER SER GLN ARG LYS SER TRP HIS PRO VAL CYS GLN SEQRES 6 A 146 ASP ASP TRP ASN GLU ASN TYR GLY ARG ALA ALA CYS ARG SEQRES 7 A 146 ASP MET GLY TYR LYS ASN ASN PHE TYR SER SER GLN GLY SEQRES 8 A 146 ILE VAL ASP ASP SER GLY SER THR SER PHE MET LYS LEU SEQRES 9 A 146 ASN THR SER ALA GLY ASN VAL ASP ILE TYR LYS LYS LEU SEQRES 10 A 146 TYR HIS SER ASP ALA CYS SER SER LYS ALA VAL VAL SER SEQRES 11 A 146 LEU ARG CYS ILE ALA CYS GLY VAL ASN LEU ASN ASP ASP SEQRES 12 A 146 ASP ASP LYS SEQRES 1 B 249 ILE VAL GLY GLY GLU SER ALA LEU PRO GLY ALA TRP PRO SEQRES 2 B 249 TRP GLN VAL SER LEU HIS VAL GLN ASN VAL HIS VAL CYS SEQRES 3 B 249 GLY GLY SER ILE ILE THR PRO GLU TRP ILE VAL THR ALA SEQRES 4 B 249 ALA HIS CYS VAL GLU LYS PRO LEU ASN ASN PRO TRP HIS SEQRES 5 B 249 TRP THR ALA PHE ALA GLY ILE LEU ARG GLN SER PHE MET SEQRES 6 B 249 PHE TYR GLY ALA GLY TYR GLN VAL GLU LYS VAL ILE SER SEQRES 7 B 249 HIS PRO ASN TYR ASP SER LYS THR LYS ASN ASN ASP ILE SEQRES 8 B 249 ALA LEU MET LYS LEU GLN LYS PRO LEU THR PHE ASN ASP SEQRES 9 B 249 LEU VAL LYS PRO VAL CYS LEU PRO ASN PRO GLY MET MET SEQRES 10 B 249 LEU GLN PRO GLU GLN LEU CYS TRP ILE SER GLY TRP GLY SEQRES 11 B 249 ALA THR GLU GLU LYS GLY LYS THR SER GLU VAL LEU ASN SEQRES 12 B 249 ALA ALA LYS VAL LEU LEU ILE GLU THR GLN ARG CYS ASN SEQRES 13 B 249 SER ARG TYR VAL TYR ASP ASN LEU ILE THR PRO ALA MET SEQRES 14 B 249 ILE CYS ALA GLY PHE LEU GLN GLY ASN VAL ASP SER CYS SEQRES 15 B 249 GLN GLY ASP SER GLY GLY PRO LEU VAL THR SER LYS ASN SEQRES 16 B 249 ASN ILE TRP TRP LEU ILE GLY ASP THR SER TRP GLY SER SEQRES 17 B 249 GLY CYS ALA LYS ALA TYR ARG PRO GLY VAL TYR GLY ASN SEQRES 18 B 249 VAL MET VAL PHE THR ASP TRP ILE TYR ARG GLN MET ARG SEQRES 19 B 249 ALA ASP GLY GLU PHE VAL GLU HIS HIS HIS HIS HIS HIS SEQRES 20 B 249 HIS HIS SEQRES 1 C 146 MET GLY SER LYS CYS SER ASN SER GLY ILE GLU CYS ASP SEQRES 2 C 146 SER SER GLY THR CYS ILE ASN PRO SER ASN TRP CYS ASP SEQRES 3 C 146 GLY VAL SER HIS CYS PRO GLY GLY GLU ASP GLU ASN ARG SEQRES 4 C 146 CYS VAL ARG LEU TYR GLY PRO ASN PHE ILE LEU GLN VAL SEQRES 5 C 146 TYR SER SER GLN ARG LYS SER TRP HIS PRO VAL CYS GLN SEQRES 6 C 146 ASP ASP TRP ASN GLU ASN TYR GLY ARG ALA ALA CYS ARG SEQRES 7 C 146 ASP MET GLY TYR LYS ASN ASN PHE TYR SER SER GLN GLY SEQRES 8 C 146 ILE VAL ASP ASP SER GLY SER THR SER PHE MET LYS LEU SEQRES 9 C 146 ASN THR SER ALA GLY ASN VAL ASP ILE TYR LYS LYS LEU SEQRES 10 C 146 TYR HIS SER ASP ALA CYS SER SER LYS ALA VAL VAL SER SEQRES 11 C 146 LEU ARG CYS ILE ALA CYS GLY VAL ASN LEU ASN ASP ASP SEQRES 12 C 146 ASP ASP LYS SEQRES 1 D 249 ILE VAL GLY GLY GLU SER ALA LEU PRO GLY ALA TRP PRO SEQRES 2 D 249 TRP GLN VAL SER LEU HIS VAL GLN ASN VAL HIS VAL CYS SEQRES 3 D 249 GLY GLY SER ILE ILE THR PRO GLU TRP ILE VAL THR ALA SEQRES 4 D 249 ALA HIS CYS VAL GLU LYS PRO LEU ASN ASN PRO TRP HIS SEQRES 5 D 249 TRP THR ALA PHE ALA GLY ILE LEU ARG GLN SER PHE MET SEQRES 6 D 249 PHE TYR GLY ALA GLY TYR GLN VAL GLU LYS VAL ILE SER SEQRES 7 D 249 HIS PRO ASN TYR ASP SER LYS THR LYS ASN ASN ASP ILE SEQRES 8 D 249 ALA LEU MET LYS LEU GLN LYS PRO LEU THR PHE ASN ASP SEQRES 9 D 249 LEU VAL LYS PRO VAL CYS LEU PRO ASN PRO GLY MET MET SEQRES 10 D 249 LEU GLN PRO GLU GLN LEU CYS TRP ILE SER GLY TRP GLY SEQRES 11 D 249 ALA THR GLU GLU LYS GLY LYS THR SER GLU VAL LEU ASN SEQRES 12 D 249 ALA ALA LYS VAL LEU LEU ILE GLU THR GLN ARG CYS ASN SEQRES 13 D 249 SER ARG TYR VAL TYR ASP ASN LEU ILE THR PRO ALA MET SEQRES 14 D 249 ILE CYS ALA GLY PHE LEU GLN GLY ASN VAL ASP SER CYS SEQRES 15 D 249 GLN GLY ASP SER GLY GLY PRO LEU VAL THR SER LYS ASN SEQRES 16 D 249 ASN ILE TRP TRP LEU ILE GLY ASP THR SER TRP GLY SER SEQRES 17 D 249 GLY CYS ALA LYS ALA TYR ARG PRO GLY VAL TYR GLY ASN SEQRES 18 D 249 VAL MET VAL PHE THR ASP TRP ILE TYR ARG GLN MET ARG SEQRES 19 D 249 ALA ASP GLY GLU PHE VAL GLU HIS HIS HIS HIS HIS HIS SEQRES 20 D 249 HIS HIS SEQRES 1 E 131 ALA VAL GLN LEU GLN ALA SER GLY GLY GLY PHE VAL GLN SEQRES 2 E 131 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 131 LYS VAL VAL GLU GLN GLY LEU MET GLY TRP PHE ARG GLN SEQRES 4 E 131 ALA PRO GLY LYS GLU ARG GLU PHE VAL SER ALA ILE GLN SEQRES 5 E 131 TYR ASP THR LYS LEU GLU TYR TYR ALA ASP SER VAL LYS SEQRES 6 E 131 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 E 131 VAL TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 E 131 ALA THR TYR TYR CYS ALA THR PRO GLN MET TRP VAL GLN SEQRES 9 E 131 ARG ASP ARG ASP ASP ARG TRP TYR TRP GLY GLN GLY THR SEQRES 10 E 131 GLN VAL THR VAL SER SER GLY SER HIS HIS HIS HIS HIS SEQRES 11 E 131 HIS SEQRES 1 F 131 ALA VAL GLN LEU GLN ALA SER GLY GLY GLY PHE VAL GLN SEQRES 2 F 131 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 131 LYS VAL VAL GLU GLN GLY LEU MET GLY TRP PHE ARG GLN SEQRES 4 F 131 ALA PRO GLY LYS GLU ARG GLU PHE VAL SER ALA ILE GLN SEQRES 5 F 131 TYR ASP THR LYS LEU GLU TYR TYR ALA ASP SER VAL LYS SEQRES 6 F 131 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 F 131 VAL TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 F 131 ALA THR TYR TYR CYS ALA THR PRO GLN MET TRP VAL GLN SEQRES 9 F 131 ARG ASP ARG ASP ASP ARG TRP TYR TRP GLY GLN GLY THR SEQRES 10 F 131 GLN VAL THR VAL SER SER GLY SER HIS HIS HIS HIS HIS SEQRES 11 F 131 HIS HET CA A 301 1 HET NAG A 302 14 HET GOL B 601 6 HET CA C 301 1 HET NAG C 302 14 HET GOL D 601 6 HET GOL E 201 6 HET GOL F 501 6 HETNAM CA CALCIUM ION HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM GOL GLYCEROL HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 7 CA 2(CA 2+) FORMUL 8 NAG 2(C8 H15 N O6) FORMUL 9 GOL 4(C3 H8 O3) FORMUL 15 HOH *599(H2 O) HELIX 1 AA1 PRO A 129 TRP A 132 5 4 HELIX 2 AA2 GLY A 142 ASN A 146 5 5 HELIX 3 AA3 ASN A 177 MET A 188 1 12 HELIX 4 AA4 ASP A 220 LYS A 223 5 4 HELIX 5 AA5 ALA B 294 VAL B 298 5 5 HELIX 6 AA6 ASN B 304 TRP B 306 5 3 HELIX 7 AA7 ARG B 316 MET B 320 5 5 HELIX 8 AA8 GLU B 406 ASN B 411 1 6 HELIX 9 AA9 VAL B 477 GLU B 493 1 17 HELIX 10 AB1 PRO C 129 TRP C 132 5 4 HELIX 11 AB2 GLY C 142 ASN C 146 5 5 HELIX 12 AB3 ASN C 177 MET C 188 1 12 HELIX 13 AB4 ASP C 220 LYS C 223 5 4 HELIX 14 AB5 ALA D 294 VAL D 298 5 5 HELIX 15 AB6 ASN D 304 TRP D 306 5 3 HELIX 16 AB7 ARG D 316 MET D 320 5 5 HELIX 17 AB8 GLU D 406 ASN D 411 1 6 HELIX 18 AB9 VAL D 477 GLU D 493 1 17 HELIX 19 AC1 LYS E 27 GLN E 31 5 5 HELIX 20 AC2 ARG E 87 THR E 91 5 5 HELIX 21 AC3 THR E 98 VAL E 103 1 6 HELIX 22 AC4 LYS F 27 GLN F 31 5 5 HELIX 23 AC5 ARG F 87 THR F 91 5 5 HELIX 24 AC6 THR F 98 VAL F 103 1 6 SHEET 1 AA1 8 ILE A 118 GLU A 119 0 SHEET 2 AA1 8 THR A 125 ILE A 127 -1 O ILE A 127 N ILE A 118 SHEET 3 AA1 8 LEU F 57 TYR F 60 -1 O GLU F 58 N CYS A 126 SHEET 4 AA1 8 GLU F 46 GLN F 52 -1 N GLN F 52 O LEU F 57 SHEET 5 AA1 8 LEU F 33 GLN F 39 -1 N TRP F 36 O SER F 49 SHEET 6 AA1 8 ALA F 92 ALA F 97 -1 O TYR F 95 N PHE F 37 SHEET 7 AA1 8 THR F 117 VAL F 121 -1 O THR F 117 N TYR F 94 SHEET 8 AA1 8 GLY F 10 VAL F 12 1 N GLY F 10 O THR F 120 SHEET 1 AA2 3 VAL A 149 TYR A 152 0 SHEET 2 AA2 3 ILE A 157 SER A 162 -1 O GLN A 159 N ARG A 150 SHEET 3 AA2 3 SER A 167 PRO A 170 -1 O SER A 167 N SER A 162 SHEET 1 AA3 2 SER A 196 ILE A 200 0 SHEET 2 AA3 2 VAL A 236 ARG A 240 -1 O SER A 238 N GLN A 198 SHEET 1 AA4 2 PHE A 209 LEU A 212 0 SHEET 2 AA4 2 LEU A 225 SER A 228 -1 O SER A 228 N PHE A 209 SHEET 1 AA5 8 GLU B 260 SER B 261 0 SHEET 2 AA5 8 ASN B 398 ILE B 405 -1 O ALA B 399 N GLU B 260 SHEET 3 AA5 8 MET B 424 GLY B 428 -1 O CYS B 426 N ILE B 405 SHEET 4 AA5 8 GLY B 472 ASN B 476 -1 O TYR B 474 N ILE B 425 SHEET 5 AA5 8 ILE B 452 TRP B 461 -1 N ASP B 458 O GLY B 475 SHEET 6 AA5 8 PRO B 444 LYS B 449 -1 N THR B 447 O TRP B 454 SHEET 7 AA5 8 LEU B 378 GLY B 383 -1 N TRP B 380 O VAL B 446 SHEET 8 AA5 8 ASN B 398 ILE B 405 -1 O VAL B 402 N CYS B 379 SHEET 1 AA6 7 GLN B 270 VAL B 275 0 SHEET 2 AA6 7 VAL B 278 ILE B 285 -1 O CYS B 281 N LEU B 273 SHEET 3 AA6 7 TRP B 290 THR B 293 -1 O VAL B 292 N SER B 284 SHEET 4 AA6 7 ALA B 347 LEU B 351 -1 O ALA B 347 N THR B 293 SHEET 5 AA6 7 TYR B 326 SER B 333 -1 N GLU B 329 O LYS B 350 SHEET 6 AA6 7 TRP B 308 ALA B 312 -1 N ALA B 310 O TYR B 326 SHEET 7 AA6 7 GLN B 270 VAL B 275 -1 N HIS B 274 O THR B 309 SHEET 1 AA7 8 ILE C 118 GLU C 119 0 SHEET 2 AA7 8 THR C 125 ILE C 127 -1 O ILE C 127 N ILE C 118 SHEET 3 AA7 8 LEU E 57 TYR E 60 -1 O GLU E 58 N CYS C 126 SHEET 4 AA7 8 GLU E 46 GLN E 52 -1 N GLN E 52 O LEU E 57 SHEET 5 AA7 8 LEU E 33 GLN E 39 -1 N ARG E 38 O GLU E 46 SHEET 6 AA7 8 ALA E 92 ALA E 97 -1 O TYR E 95 N PHE E 37 SHEET 7 AA7 8 THR E 117 VAL E 121 -1 O THR E 117 N TYR E 94 SHEET 8 AA7 8 GLY E 10 VAL E 12 1 N GLY E 10 O THR E 120 SHEET 1 AA8 3 VAL C 149 TYR C 152 0 SHEET 2 AA8 3 ILE C 157 SER C 162 -1 O ILE C 157 N TYR C 152 SHEET 3 AA8 3 SER C 167 PRO C 170 -1 O SER C 167 N SER C 162 SHEET 1 AA9 2 SER C 196 ILE C 200 0 SHEET 2 AA9 2 VAL C 236 ARG C 240 -1 O ARG C 240 N SER C 196 SHEET 1 AB1 2 PHE C 209 LEU C 212 0 SHEET 2 AB1 2 LEU C 225 SER C 228 -1 O TYR C 226 N LYS C 211 SHEET 1 AB2 8 GLU D 260 SER D 261 0 SHEET 2 AB2 8 ASN D 398 ILE D 405 -1 O ALA D 399 N GLU D 260 SHEET 3 AB2 8 MET D 424 GLY D 428 -1 O CYS D 426 N ILE D 405 SHEET 4 AB2 8 GLY D 472 ASN D 476 -1 O TYR D 474 N ILE D 425 SHEET 5 AB2 8 ILE D 452 TRP D 461 -1 N ASP D 458 O GLY D 475 SHEET 6 AB2 8 PRO D 444 LYS D 449 -1 N THR D 447 O TRP D 454 SHEET 7 AB2 8 LEU D 378 GLY D 383 -1 N TRP D 380 O VAL D 446 SHEET 8 AB2 8 ASN D 398 ILE D 405 -1 O VAL D 402 N CYS D 379 SHEET 1 AB3 7 GLN D 270 VAL D 275 0 SHEET 2 AB3 7 VAL D 278 ILE D 285 -1 O CYS D 281 N LEU D 273 SHEET 3 AB3 7 TRP D 290 THR D 293 -1 O VAL D 292 N SER D 284 SHEET 4 AB3 7 ALA D 347 LEU D 351 -1 O ALA D 347 N THR D 293 SHEET 5 AB3 7 TYR D 326 SER D 333 -1 N GLU D 329 O LYS D 350 SHEET 6 AB3 7 TRP D 308 ALA D 312 -1 N ALA D 310 O TYR D 326 SHEET 7 AB3 7 GLN D 270 VAL D 275 -1 N HIS D 274 O THR D 309 SHEET 1 AB4 4 GLN E 3 SER E 7 0 SHEET 2 AB4 4 LEU E 18 SER E 25 -1 O SER E 25 N GLN E 3 SHEET 3 AB4 4 THR E 78 MET E 83 -1 O MET E 83 N LEU E 18 SHEET 4 AB4 4 PHE E 68 ASP E 73 -1 N THR E 69 O GLN E 82 SHEET 1 AB5 4 GLN F 3 SER F 7 0 SHEET 2 AB5 4 LEU F 18 SER F 25 -1 O SER F 25 N GLN F 3 SHEET 3 AB5 4 THR F 78 MET F 83 -1 O MET F 83 N LEU F 18 SHEET 4 AB5 4 PHE F 68 ASP F 73 -1 N THR F 69 O GLN F 82 SSBOND 1 CYS A 113 CYS A 126 1555 1555 2.04 SSBOND 2 CYS A 120 CYS A 139 1555 1555 2.03 SSBOND 3 CYS A 133 CYS A 148 1555 1555 2.04 SSBOND 4 CYS A 172 CYS A 231 1555 1555 2.03 SSBOND 5 CYS A 185 CYS A 241 1555 1555 2.03 SSBOND 6 CYS A 244 CYS B 365 1555 1555 2.03 SSBOND 7 CYS B 281 CYS B 297 1555 1555 2.05 SSBOND 8 CYS B 410 CYS B 426 1555 1555 2.04 SSBOND 9 CYS B 437 CYS B 465 1555 1555 2.03 SSBOND 10 CYS C 113 CYS C 126 1555 1555 2.03 SSBOND 11 CYS C 120 CYS C 139 1555 1555 2.03 SSBOND 12 CYS C 133 CYS C 148 1555 1555 2.02 SSBOND 13 CYS C 172 CYS C 231 1555 1555 2.03 SSBOND 14 CYS C 185 CYS C 241 1555 1555 2.04 SSBOND 15 CYS C 244 CYS D 365 1555 1555 2.03 SSBOND 16 CYS D 281 CYS D 297 1555 1555 2.05 SSBOND 17 CYS D 410 CYS D 426 1555 1555 2.03 SSBOND 18 CYS D 437 CYS D 465 1555 1555 2.03 SSBOND 19 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 20 CYS F 22 CYS F 96 1555 1555 2.03 LINK ND2 ASN A 213 C1 NAG A 302 1555 1555 1.44 LINK ND2 ASN C 213 C1 NAG C 302 1555 1555 1.45 LINK O ASN A 131 CA CA A 301 1555 1555 2.27 LINK OD1 ASP A 134 CA CA A 301 1555 1555 2.34 LINK O VAL A 136 CA CA A 301 1555 1555 2.20 LINK OD2 ASP A 144 CA CA A 301 1555 1555 2.28 LINK OE2 GLU A 145 CA CA A 301 1555 1555 2.26 LINK O ASN C 131 CA CA C 301 1555 1555 2.26 LINK OD1 ASP C 134 CA CA C 301 1555 1555 2.32 LINK O VAL C 136 CA CA C 301 1555 1555 2.15 LINK OD2 ASP C 144 CA CA C 301 1555 1555 2.29 LINK OE2 GLU C 145 CA CA C 301 1555 1555 2.32 CISPEP 1 LYS B 300 PRO B 301 0 1.30 CISPEP 2 LYS D 300 PRO D 301 0 1.43 CRYST1 67.616 69.827 82.192 104.97 112.85 102.10 P 1 2 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 0.014789 0.003172 0.008019 0.00000 SCALE2 0.000000 0.014647 0.005963 0.00000 SCALE3 0.000000 0.000000 0.014255 0.00000