HEADER ANTIVIRAL PROTEIN 30-AUG-24 9JD1 TITLE CRYSTAL STRUCTURE OF TMPRSS2 IN COMPLEX WITH FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSMEMBRANE PROTEASE SERINE 2 CATALYTIC CHAIN; COMPND 3 CHAIN: D; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: WE CHOOSE THE ECTODOMAIN OF TRANSMEMBRANE PROTEASE COMPND 6 SERINE 2 (RESIDUES: 109-492) FOR EXPRESSION. RESIDUES 250-255 COMPND 7 RESPONSIBLE FOR AUTOCLEAVAGE ARE SUBSTITUTED WITH DDDDK. THE COMPND 8 RECOMBINANT PROTEIN WAS CLEAVED INTO TWO CHAINS (A AND C) IN THE COMPND 9 PURIFICATION.; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: LIGHT CHAIN OF FAB; COMPND 12 CHAIN: A; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: HEAVY CHAIN OF FAB; COMPND 16 CHAIN: B; COMPND 17 ENGINEERED: YES; COMPND 18 OTHER_DETAILS: THE RECOMBINANT PROTEIN ENCOMPASSES A C-TERMINAL COMPND 19 LINKER ("GS") FOLLOWED BY A 6 X HIS TAG.; COMPND 20 MOL_ID: 4; COMPND 21 MOLECULE: TRANSMEMBRANE PROTEASE SERINE 2 NON-CATALYTIC CHAIN; COMPND 22 CHAIN: C; COMPND 23 ENGINEERED: YES; COMPND 24 MUTATION: YES; COMPND 25 OTHER_DETAILS: WE CHOOSE THE ECTODOMAIN OF TRANSMEMBRANE PROTEASE COMPND 26 SERINE 2 (RESIDUES: 109-492) FOR EXPRESSION. RESIDUES 250-255 COMPND 27 RESPONSIBLE FOR AUTOCLEAVAGE ARE SUBSTITUTED WITH DDDDK. THE COMPND 28 RECOMBINANT PROTEIN WAS CLEAVED INTO TWO CHAINS (A AND C) IN THE COMPND 29 PURIFICATION. 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_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_COMMON: HUMAN; SOURCE 21 ORGANISM_TAXID: 9606; SOURCE 22 GENE: TMPRSS2, PRSS10; SOURCE 23 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS COMPLEX, ANTIBODY, HOST PROTEASE, ANTIVIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR H.WANG,X.LIU,Z.ZHAO,Y.DUAN,H.YANG REVDAT 1 30-JUL-25 9JD1 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. 1.90 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.43 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 126953 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.191 REMARK 3 R VALUE (WORKING SET) : 0.190 REMARK 3 FREE R VALUE : 0.223 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.990 REMARK 3 FREE R VALUE TEST SET COUNT : 3798 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 31.4300 - 5.6800 1.00 4540 145 0.1875 0.1793 REMARK 3 2 5.6800 - 4.5100 1.00 4585 135 0.1457 0.1878 REMARK 3 3 4.5100 - 3.9500 1.00 4568 142 0.1384 0.1802 REMARK 3 4 3.9400 - 3.5800 1.00 4530 138 0.1596 0.1951 REMARK 3 5 3.5800 - 3.3300 1.00 4583 140 0.1677 0.1815 REMARK 3 6 3.3300 - 3.1300 1.00 4548 141 0.1848 0.1901 REMARK 3 7 3.1300 - 2.9800 1.00 4612 140 0.1948 0.2224 REMARK 3 8 2.9800 - 2.8500 1.00 4538 143 0.1999 0.2363 REMARK 3 9 2.8500 - 2.7400 1.00 4565 141 0.2017 0.2394 REMARK 3 10 2.7400 - 2.6400 1.00 4590 140 0.2079 0.2678 REMARK 3 11 2.6400 - 2.5600 1.00 4520 139 0.2008 0.2667 REMARK 3 12 2.5600 - 2.4900 1.00 4632 141 0.2112 0.2456 REMARK 3 13 2.4900 - 2.4200 1.00 4511 139 0.2096 0.2265 REMARK 3 14 2.4200 - 2.3600 1.00 4616 148 0.2083 0.2914 REMARK 3 15 2.3600 - 2.3100 1.00 4532 141 0.2112 0.2723 REMARK 3 16 2.3100 - 2.2600 1.00 4589 139 0.2176 0.2893 REMARK 3 17 2.2600 - 2.2100 1.00 4536 143 0.2108 0.2566 REMARK 3 18 2.2100 - 2.1700 1.00 4553 135 0.2261 0.2990 REMARK 3 19 2.1700 - 2.1300 1.00 4561 145 0.2330 0.2730 REMARK 3 20 2.1300 - 2.1000 1.00 4548 140 0.2264 0.3079 REMARK 3 21 2.1000 - 2.0600 1.00 4628 143 0.2405 0.2761 REMARK 3 22 2.0600 - 2.0300 1.00 4546 137 0.2430 0.2529 REMARK 3 23 2.0300 - 2.0000 1.00 4523 141 0.2597 0.3087 REMARK 3 24 2.0000 - 1.9700 1.00 4619 145 0.2687 0.3003 REMARK 3 25 1.9700 - 1.9500 1.00 4594 140 0.2840 0.2906 REMARK 3 26 1.9500 - 1.9200 1.00 4497 140 0.3007 0.3310 REMARK 3 27 1.9200 - 1.9000 0.98 4491 137 0.3604 0.3965 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) : 0.230 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.800 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 : 0.005 6442 REMARK 3 ANGLE : 0.802 8772 REMARK 3 CHIRALITY : 0.056 970 REMARK 3 PLANARITY : 0.007 1128 REMARK 3 DIHEDRAL : 16.103 2322 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 9JD1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 03-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1300050984. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-JUN-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 : SSRF REMARK 200 BEAMLINE : BL19U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97852 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66877 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 31.430 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 12.80 REMARK 200 R MERGE (I) : 0.11900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.5500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.83600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.61 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MES PH 5.6, 8.6% (W/V) REMARK 280 POLYETHYLENE GLYCOL 4,000, 17.1% (V/V) POLYETHYLENE GLYCOL 600, REMARK 280 EVAPORATION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 23.08200 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 100.76650 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.58800 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 100.76650 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.08200 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.58800 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 8040 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 35800 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, C, 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 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -23.08200 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 44.58800 REMARK 350 BIOMT3 2 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 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 CYS A 217 REMARK 465 SER B 146 REMARK 465 THR B 147 REMARK 465 SER B 148 REMARK 465 LYS B 230 REMARK 465 SER B 231 REMARK 465 CYS B 232 REMARK 465 GLY B 233 REMARK 465 SER B 234 REMARK 465 HIS B 235 REMARK 465 HIS B 236 REMARK 465 HIS B 237 REMARK 465 HIS B 238 REMARK 465 HIS B 239 REMARK 465 HIS B 240 REMARK 465 MET C 109 REMARK 465 GLY C 110 REMARK 465 SER C 111 REMARK 465 LYS C 112 REMARK 465 CYS C 113 REMARK 465 SER C 114 REMARK 465 ASN C 115 REMARK 465 SER C 116 REMARK 465 GLY C 117 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 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 GLU D 260 CG CD OE1 OE2 REMARK 470 ASN D 304 CG OD1 ND2 REMARK 470 TYR D 322 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU D 406 CG CD OE1 OE2 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 LEU A 157 CG CD1 CD2 REMARK 470 ARG B 109 CG CD NE CZ NH1 NH2 REMARK 470 SER B 143 OG REMARK 470 LYS B 145 CG CD CE NZ REMARK 470 ILE C 118 CG1 CG2 CD1 REMARK 470 ASP C 121 CG OD1 OD2 REMARK 470 SER C 122 OG REMARK 470 SER C 123 OG REMARK 470 SER C 130 OG REMARK 470 GLN C 164 CG CD OE1 NE2 REMARK 470 ARG C 165 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 166 CG CD CE NZ REMARK 470 SER C 206 OG REMARK 470 LEU C 248 CG CD1 CD2 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 ASN D 358 -161.46 -160.09 REMARK 500 VAL D 415 -79.27 -121.28 REMARK 500 ASN D 433 -33.54 76.65 REMARK 500 ASP A 52 -44.53 69.50 REMARK 500 ASN A 53 14.68 -146.10 REMARK 500 ALA A 87 175.73 177.86 REMARK 500 SER A 93 -155.06 -143.64 REMARK 500 ASP A 95 -153.51 -112.92 REMARK 500 SER A 97 -11.52 -142.69 REMARK 500 TYR B 114 -0.68 -140.85 REMARK 500 LYS C 191 -122.53 52.44 REMARK 500 TYR C 195 -72.80 -108.26 REMARK 500 ASN C 247 -168.07 -119.95 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 598 DISTANCE = 7.88 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 C 301 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN C 131 O REMARK 620 2 ASP C 134 OD1 97.8 REMARK 620 3 VAL C 136 O 173.5 77.5 REMARK 620 4 ASP C 144 OD2 94.2 164.5 91.3 REMARK 620 5 GLU C 145 OE2 88.1 79.8 95.3 90.8 REMARK 620 N 1 2 3 4 DBREF 9JD1 D 256 492 UNP O15393 TMPS2_HUMAN 256 492 DBREF 9JD1 A 1 217 PDB 9JD1 9JD1 1 217 DBREF 9JD1 B 1 240 PDB 9JD1 9JD1 1 240 DBREF 9JD1 C 109 254 UNP O15393 TMPS2_HUMAN 109 254 SEQADV 9JD1 GLU D 493 UNP O15393 EXPRESSION TAG SEQADV 9JD1 PHE D 494 UNP O15393 EXPRESSION TAG SEQADV 9JD1 VAL D 495 UNP O15393 EXPRESSION TAG SEQADV 9JD1 GLU D 496 UNP O15393 EXPRESSION TAG SEQADV 9JD1 HIS D 497 UNP O15393 EXPRESSION TAG SEQADV 9JD1 HIS D 498 UNP O15393 EXPRESSION TAG SEQADV 9JD1 HIS D 499 UNP O15393 EXPRESSION TAG SEQADV 9JD1 HIS D 500 UNP O15393 EXPRESSION TAG SEQADV 9JD1 HIS D 501 UNP O15393 EXPRESSION TAG SEQADV 9JD1 HIS D 502 UNP O15393 EXPRESSION TAG SEQADV 9JD1 HIS D 503 UNP O15393 EXPRESSION TAG SEQADV 9JD1 HIS D 504 UNP O15393 EXPRESSION TAG SEQADV 9JD1 ASP C 250 UNP O15393 SER 250 ENGINEERED MUTATION SEQADV 9JD1 ASP C 251 UNP O15393 SER 251 ENGINEERED MUTATION SEQADV 9JD1 ASP C 252 UNP O15393 ARG 252 ENGINEERED MUTATION SEQADV 9JD1 ASP C 253 UNP O15393 GLN 253 ENGINEERED MUTATION SEQADV 9JD1 LYS C 254 UNP O15393 SER 254 ENGINEERED MUTATION 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 A 217 ASN PHE MET LEU THR GLN PRO HIS SER MET SER GLU SER SEQRES 2 A 217 PRO GLY LYS THR VAL THR ILE SER CYS THR ARG SER SER SEQRES 3 A 217 GLY SER ILE ALA SER ASN TYR VAL GLN TRP TYR GLN GLN SEQRES 4 A 217 ARG PRO GLY SER SER PRO THR THR VAL ILE TYR ASP ASP SEQRES 5 A 217 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 A 217 SER ILE ASP SER SER SER ASN SER ALA SER LEU THR ILE SEQRES 7 A 217 SER GLY LEU LYS THR GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 A 217 GLN SER TYR ASP SER SER ASN VAL ILE PHE GLY GLY GLY SEQRES 9 A 217 THR LYS LEU THR VAL LEU ARG THR VAL ALA ALA PRO SER SEQRES 10 A 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 A 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 A 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 A 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 A 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 A 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 A 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 A 217 THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 B 240 GLN VAL GLN LEU GLN GLU SER GLY GLY ASP LEU VAL GLN SEQRES 2 B 240 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 240 PHE THR PHE SER SER SER ALA MET THR TRP VAL ARG GLN SEQRES 4 B 240 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SER SEQRES 5 B 240 ARG ASN GLY GLY SER THR ASN TYR ALA ASP SER VAL LYS SEQRES 6 B 240 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 B 240 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 B 240 ALA VAL TYR TYR CYS ALA ARG GLU GLY TYR ASP PHE TRP SEQRES 9 B 240 SER GLY ARG GLU ARG ARG TYR TYR TYR TYR GLY MET ASP SEQRES 10 B 240 VAL TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 11 B 240 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 12 B 240 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 13 B 240 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 14 B 240 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 15 B 240 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 16 B 240 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 17 B 240 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 18 B 240 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS GLY SER SEQRES 19 B 240 HIS HIS HIS HIS 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 HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET MAN E 4 11 HET MAN E 5 11 HET MES A 301 12 HET GOL A 302 6 HET GOL B 301 6 HET CA C 301 1 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID HETNAM GOL GLYCEROL HETNAM CA CALCIUM ION 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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 NAG 2(C8 H15 N O6) FORMUL 5 BMA C6 H12 O6 FORMUL 5 MAN 2(C6 H12 O6) FORMUL 6 MES C6 H13 N O4 S FORMUL 7 GOL 2(C3 H8 O3) FORMUL 9 CA CA 2+ FORMUL 10 HOH *667(H2 O) HELIX 1 AA1 ALA D 294 GLU D 299 5 6 HELIX 2 AA2 ASN D 304 TRP D 306 5 3 HELIX 3 AA3 ARG D 316 MET D 320 5 5 HELIX 4 AA4 GLU D 406 ASN D 411 1 6 HELIX 5 AA5 VAL D 477 GLU D 493 1 17 HELIX 6 AA6 SER A 28 ASN A 32 5 5 HELIX 7 AA7 LYS A 82 GLU A 86 5 5 HELIX 8 AA8 SER A 124 LYS A 129 1 6 HELIX 9 AA9 LYS A 186 GLU A 190 1 5 HELIX 10 AB1 THR B 28 SER B 32 5 5 HELIX 11 AB2 ASN B 74 LYS B 76 5 3 HELIX 12 AB3 ARG B 87 THR B 91 5 5 HELIX 13 AB4 SER B 172 ALA B 174 5 3 HELIX 14 AB5 SER B 203 LEU B 205 5 3 HELIX 15 AB6 LYS B 217 ASN B 220 5 4 HELIX 16 AB7 ASN C 128 TRP C 132 5 5 HELIX 17 AB8 GLY C 142 ASN C 146 5 5 HELIX 18 AB9 ASN C 177 GLY C 189 1 13 HELIX 19 AC1 ASP C 220 LYS C 223 5 4 SHEET 1 AA1 8 GLU D 260 SER D 261 0 SHEET 2 AA1 8 ASN D 398 ILE D 405 -1 O ALA D 399 N GLU D 260 SHEET 3 AA1 8 MET D 424 GLY D 428 -1 O GLY D 428 N LEU D 403 SHEET 4 AA1 8 GLY D 472 ASN D 476 -1 O TYR D 474 N ILE D 425 SHEET 5 AA1 8 ILE D 452 TRP D 461 -1 N TRP D 461 O VAL D 473 SHEET 6 AA1 8 PRO D 444 LYS D 449 -1 N THR D 447 O TRP D 454 SHEET 7 AA1 8 LEU D 378 GLY D 383 -1 N TRP D 380 O VAL D 446 SHEET 8 AA1 8 ASN D 398 ILE D 405 -1 O VAL D 402 N CYS D 379 SHEET 1 AA2 7 GLN D 270 VAL D 275 0 SHEET 2 AA2 7 VAL D 278 ILE D 285 -1 O CYS D 281 N LEU D 273 SHEET 3 AA2 7 TRP D 290 THR D 293 -1 O VAL D 292 N SER D 284 SHEET 4 AA2 7 ALA D 347 LEU D 351 -1 O ALA D 347 N THR D 293 SHEET 5 AA2 7 TYR D 326 SER D 333 -1 N GLU D 329 O LYS D 350 SHEET 6 AA2 7 TRP D 308 ALA D 312 -1 N ALA D 310 O TYR D 326 SHEET 7 AA2 7 GLN D 270 VAL D 275 -1 N HIS D 274 O THR D 309 SHEET 1 AA3 4 LEU A 4 THR A 5 0 SHEET 2 AA3 4 VAL A 18 ARG A 24 -1 O THR A 23 N THR A 5 SHEET 3 AA3 4 SER A 73 ILE A 78 -1 O LEU A 76 N ILE A 20 SHEET 4 AA3 4 PHE A 63 ASP A 68 -1 N ASP A 68 O SER A 73 SHEET 1 AA4 5 SER A 9 GLU A 12 0 SHEET 2 AA4 5 THR A 105 VAL A 109 1 O THR A 108 N MET A 10 SHEET 3 AA4 5 ALA A 87 TYR A 94 -1 N ALA A 87 O LEU A 107 SHEET 4 AA4 5 GLN A 35 GLN A 39 -1 N GLN A 35 O GLN A 92 SHEET 5 AA4 5 THR A 46 ILE A 49 -1 O THR A 46 N GLN A 38 SHEET 1 AA5 4 SER A 9 GLU A 12 0 SHEET 2 AA5 4 THR A 105 VAL A 109 1 O THR A 108 N MET A 10 SHEET 3 AA5 4 ALA A 87 TYR A 94 -1 N ALA A 87 O LEU A 107 SHEET 4 AA5 4 VAL A 99 PHE A 101 -1 O ILE A 100 N SER A 93 SHEET 1 AA6 4 SER A 117 PHE A 121 0 SHEET 2 AA6 4 THR A 132 PHE A 142 -1 O LEU A 138 N PHE A 119 SHEET 3 AA6 4 TYR A 176 SER A 185 -1 O LEU A 184 N ALA A 133 SHEET 4 AA6 4 SER A 162 VAL A 166 -1 N SER A 165 O SER A 179 SHEET 1 AA7 4 ALA A 156 LEU A 157 0 SHEET 2 AA7 4 LYS A 148 VAL A 153 -1 N VAL A 153 O ALA A 156 SHEET 3 AA7 4 VAL A 194 THR A 200 -1 O ALA A 196 N LYS A 152 SHEET 4 AA7 4 VAL A 208 ASN A 213 -1 O LYS A 210 N CYS A 197 SHEET 1 AA8 4 GLN B 3 SER B 7 0 SHEET 2 AA8 4 LEU B 18 SER B 25 -1 O ALA B 23 N GLN B 5 SHEET 3 AA8 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AA8 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA9 6 LEU B 11 VAL B 12 0 SHEET 2 AA9 6 THR B 123 VAL B 127 1 O THR B 126 N VAL B 12 SHEET 3 AA9 6 ALA B 92 GLU B 99 -1 N TYR B 94 O THR B 123 SHEET 4 AA9 6 ALA B 33 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA9 6 LEU B 45 ILE B 51 -1 O SER B 49 N TRP B 36 SHEET 6 AA9 6 THR B 58 TYR B 60 -1 O ASN B 59 N ASP B 50 SHEET 1 AB1 2 TYR B 101 SER B 105 0 SHEET 2 AB1 2 ARG B 110 GLY B 115 -1 O ARG B 110 N SER B 105 SHEET 1 AB2 4 SER B 136 LEU B 140 0 SHEET 2 AB2 4 THR B 151 TYR B 161 -1 O GLY B 155 N LEU B 140 SHEET 3 AB2 4 TYR B 192 PRO B 201 -1 O LEU B 194 N VAL B 158 SHEET 4 AB2 4 VAL B 179 THR B 181 -1 N HIS B 180 O VAL B 197 SHEET 1 AB3 4 SER B 136 LEU B 140 0 SHEET 2 AB3 4 THR B 151 TYR B 161 -1 O GLY B 155 N LEU B 140 SHEET 3 AB3 4 TYR B 192 PRO B 201 -1 O LEU B 194 N VAL B 158 SHEET 4 AB3 4 VAL B 185 LEU B 186 -1 N VAL B 185 O SER B 193 SHEET 1 AB4 3 THR B 167 TRP B 170 0 SHEET 2 AB4 3 TYR B 210 HIS B 216 -1 O ASN B 213 N SER B 169 SHEET 3 AB4 3 THR B 221 VAL B 227 -1 O VAL B 223 N VAL B 214 SHEET 1 AB5 3 VAL C 149 TYR C 152 0 SHEET 2 AB5 3 ILE C 157 SER C 162 -1 O ILE C 157 N TYR C 152 SHEET 3 AB5 3 SER C 167 PRO C 170 -1 O SER C 167 N SER C 162 SHEET 1 AB6 2 SER C 196 ILE C 200 0 SHEET 2 AB6 2 VAL C 236 ARG C 240 -1 O VAL C 236 N ILE C 200 SHEET 1 AB7 2 PHE C 209 LEU C 212 0 SHEET 2 AB7 2 LEU C 225 SER C 228 -1 O TYR C 226 N LYS C 211 SSBOND 1 CYS D 281 CYS D 297 1555 1555 2.03 SSBOND 2 CYS D 365 CYS C 244 1555 1555 2.04 SSBOND 3 CYS D 410 CYS D 426 1555 1555 2.03 SSBOND 4 CYS D 437 CYS D 465 1555 1555 2.04 SSBOND 5 CYS A 22 CYS A 91 1555 1555 2.05 SSBOND 6 CYS A 137 CYS A 197 1555 1555 2.03 SSBOND 7 CYS B 22 CYS B 96 1555 1555 2.05 SSBOND 8 CYS B 156 CYS B 212 1555 1555 2.03 SSBOND 9 CYS C 120 CYS C 139 1555 1555 2.03 SSBOND 10 CYS C 133 CYS C 148 1555 1555 2.02 SSBOND 11 CYS C 172 CYS C 231 1555 1555 2.03 SSBOND 12 CYS C 185 CYS C 241 1555 1555 2.04 LINK ND2 ASN C 213 C1 NAG E 1 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44 LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.43 LINK O6 BMA E 3 C1 MAN E 5 1555 1555 1.44 LINK O ASN C 131 CA CA C 301 1555 1555 2.30 LINK OD1 ASP C 134 CA CA C 301 1555 1555 2.39 LINK O VAL C 136 CA CA C 301 1555 1555 2.23 LINK OD2 ASP C 144 CA CA C 301 1555 1555 2.39 LINK OE2 GLU C 145 CA CA C 301 1555 1555 2.36 CISPEP 1 LYS D 300 PRO D 301 0 2.20 CISPEP 2 TYR A 143 PRO A 144 0 3.77 CISPEP 3 PHE B 162 PRO B 163 0 -4.75 CISPEP 4 GLU B 164 PRO B 165 0 -1.74 CRYST1 46.164 89.176 201.533 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.021662 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011214 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004962 0.00000