HEADER MEMBRANE PROTEIN 14-MAR-25 9NRC TITLE TMPRSS6 IN COMPLEX WITH REGN7999 FAB AND REGN8023 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSMEMBRANE PROTEASE SERINE 6; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MATRIPTASE-2; COMPND 5 EC: 3.4.21.-; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: REGN7999 FAB LIGHT CHAIN; COMPND 10 CHAIN: L; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: REGN7999 FAB HEAVY CHAIN; COMPND 14 CHAIN: H; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: REGN8023 FAB LIGHT CHAIN; COMPND 18 CHAIN: B; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: REGN8023 FAB HEAVY CHAIN; COMPND 22 CHAIN: C; COMPND 23 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: TMPRSS6, UNQ354/PRO618; SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 23 MOL_ID: 5; SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS SERINE PROTEASE, MATRIPTASE, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR K.SAOTOME,M.C.FRANKLIN REVDAT 1 09-JUL-25 9NRC 0 JRNL AUTH H.E.LOB,N.SINGH,K.MOHAMMADI,L.IVANOVA,B.CROWELL,H.J.KIM, JRNL AUTH 2 L.KRAVETS,N.M.DAS,Y.RAY,J.H.KIM,S.ROTTEY, JRNL AUTH 3 E.LABRIOLA-TOMPKINS,H.E.HASSAN,L.FARRELLY,H.F.CHIN,M.PREDA, JRNL AUTH 4 L.SPENCER NOAKES,K.SAOTOME,M.FRANKLIN,M.W.RETTER, JRNL AUTH 5 E.KARAYUSUF,J.J.FLANAGAN,W.OLSON,K.C.NANNURU,V.IDONE, JRNL AUTH 6 M.E.BURCZYNSKI,O.A.HARARI,L.PERLEE,G.VAN LANCKER,A.J.MURPHY, JRNL AUTH 7 A.N.ECONOMIDES,S.J.HATSELL JRNL TITL A TMPRSS6-INHIBITING MAB IMPROVES DISEASE IN A JRNL TITL 2 BETA-THALASSEMIA MOUSE MODEL AND REDUCES IRON IN HEALTHY JRNL TITL 3 HUMANS. JRNL REF JCI INSIGHT V. 10 2025 JRNL REFN ISSN 2379-3708 JRNL PMID 40548380 JRNL DOI 10.1172/JCI.INSIGHT.191813 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.LIEBSCHNER,P.V.AFONINE,M.L.BAKER,G.BUNKOCZI,V.B.CHEN, REMARK 1 AUTH 2 T.I.CROLL,B.HINTZE,L.W.HUNG,S.JAIN,A.J.MCCOY,N.W.MORIARTY, REMARK 1 AUTH 3 R.D.OEFFNER,B.K.POON,M.G.PRISANT,R.J.READ,J.S.RICHARDSON, REMARK 1 AUTH 4 D.C.RICHARDSON,M.D.SAMMITO,O.V.SOBOLEV,D.H.STOCKWELL, REMARK 1 AUTH 5 T.C.TERWILLIGER,A.G.URZHUMTSEV,L.L.VIDEAU,C.J.WILLIAMS, REMARK 1 AUTH 6 P.D.ADAMS REMARK 1 TITL MACROMOLECULAR STRUCTURE DETERMINATION USING X-RAYS, REMARK 1 TITL 2 NEUTRONS AND ELECTRONS: RECENT DEVELOPMENTS IN PHENIX REMARK 1 REF ACTA CRYSTALLOGR D STRUCT 2019 REMARK 1 REF 2 BIOL REMARK 1 REFN REMARK 1 PMID 31588918 REMARK 1 DOI 10.1107/S2059798319011471 REMARK 2 REMARK 2 RESOLUTION. 3.29 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.290 REMARK 3 NUMBER OF PARTICLES : 105142 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9NRC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1000294042. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : TMPRSS6 IN COMPLEX WITH REMARK 245 REGN7999 FAB AND REGN8023 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, H, B, C, E, 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 GLY A 77 REMARK 465 TYR A 78 REMARK 465 LYS A 79 REMARK 465 ALA A 80 REMARK 465 GLU A 81 REMARK 465 PRO A 573 REMARK 465 SER A 574 REMARK 465 SER A 575 REMARK 465 ARG A 576 REMARK 465 ILE A 577 REMARK 465 VAL A 578 REMARK 465 GLY A 579 REMARK 465 GLY A 580 REMARK 465 LYS A 755 REMARK 465 ASP A 756 REMARK 465 GLU A 812 REMARK 465 GLN A 813 REMARK 465 LYS A 814 REMARK 465 LEU A 815 REMARK 465 ILE A 816 REMARK 465 SER A 817 REMARK 465 GLU A 818 REMARK 465 GLU A 819 REMARK 465 ASP A 820 REMARK 465 LEU A 821 REMARK 465 GLY A 822 REMARK 465 GLY A 823 REMARK 465 GLU A 824 REMARK 465 GLN A 825 REMARK 465 LYS A 826 REMARK 465 LEU A 827 REMARK 465 ILE A 828 REMARK 465 SER A 829 REMARK 465 GLU A 830 REMARK 465 GLU A 831 REMARK 465 ASP A 832 REMARK 465 LEU A 833 REMARK 465 HIS A 834 REMARK 465 HIS A 835 REMARK 465 HIS A 836 REMARK 465 HIS A 837 REMARK 465 HIS A 838 REMARK 465 HIS A 839 REMARK 465 SER H 139 REMARK 465 ARG H 140 REMARK 465 SER H 141 REMARK 465 THR H 142 REMARK 465 SER H 143 REMARK 465 GLU H 144 REMARK 465 LYS H 225 REMARK 465 TYR H 226 REMARK 465 GLY H 227 REMARK 465 PRO H 228 REMARK 465 PRO H 229 REMARK 465 CYS H 230 REMARK 465 PRO H 231 REMARK 465 PRO H 232 REMARK 465 CYS H 233 REMARK 465 PRO H 234 REMARK 465 ALA H 235 REMARK 465 PRO H 236 REMARK 465 GLU H 237 REMARK 465 PHE H 238 REMARK 465 LEU H 239 REMARK 465 GLY H 240 REMARK 465 SER C 136 REMARK 465 ARG C 137 REMARK 465 SER C 138 REMARK 465 THR C 139 REMARK 465 SER C 140 REMARK 465 GLU C 141 REMARK 465 LYS C 222 REMARK 465 TYR C 223 REMARK 465 GLY C 224 REMARK 465 PRO C 225 REMARK 465 PRO C 226 REMARK 465 CYS C 227 REMARK 465 PRO C 228 REMARK 465 PRO C 229 REMARK 465 CYS C 230 REMARK 465 PRO C 231 REMARK 465 ALA C 232 REMARK 465 PRO C 233 REMARK 465 GLU C 234 REMARK 465 PHE C 235 REMARK 465 LEU C 236 REMARK 465 GLY C 237 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 VAL A 82 CG1 CG2 REMARK 470 MET A 83 CG SD CE REMARK 470 VAL A 84 CG1 CG2 REMARK 470 SER A 85 OG REMARK 470 GLN A 86 CG CD OE1 NE2 REMARK 470 VAL A 87 CG1 CG2 REMARK 470 TYR A 88 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER A 89 OG REMARK 470 SER A 91 OG REMARK 470 LEU A 92 CG CD1 CD2 REMARK 470 ARG A 93 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 94 CG1 CG2 REMARK 470 LEU A 95 CG CD1 CD2 REMARK 470 ASN A 96 CG OD1 ND2 REMARK 470 ARG A 97 CG CD NE CZ NH1 NH2 REMARK 470 HIS A 98 CG ND1 CD2 CE1 NE2 REMARK 470 PHE A 99 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER A 100 OG REMARK 470 GLN A 101 CG CD OE1 NE2 REMARK 470 ASP A 102 CG OD1 OD2 REMARK 470 LEU A 103 CG CD1 CD2 REMARK 470 THR A 104 OG1 CG2 REMARK 470 ARG A 105 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 106 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 107 CG CD OE1 OE2 REMARK 470 SER A 108 OG REMARK 470 SER A 109 OG REMARK 470 PHE A 111 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 112 CG CD NE CZ NH1 NH2 REMARK 470 SER A 113 OG REMARK 470 GLU A 114 CG CD OE1 OE2 REMARK 470 THR A 115 OG1 CG2 REMARK 470 LYS A 117 CG CD CE NZ REMARK 470 GLN A 119 CG CD OE1 NE2 REMARK 470 LYS A 120 CG CD CE NZ REMARK 470 MET A 121 CG SD CE REMARK 470 LEU A 122 CG CD1 CD2 REMARK 470 LYS A 123 CG CD CE NZ REMARK 470 GLU A 124 CG CD OE1 OE2 REMARK 470 LEU A 125 CG CD1 CD2 REMARK 470 ILE A 126 CG1 CG2 CD1 REMARK 470 THR A 127 OG1 CG2 REMARK 470 SER A 128 OG REMARK 470 THR A 129 OG1 CG2 REMARK 470 ARG A 130 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 131 CG CD1 CD2 REMARK 470 THR A 133 OG1 CG2 REMARK 470 TYR A 134 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR A 135 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER A 137 OG REMARK 470 SER A 138 OG REMARK 470 SER A 139 OG REMARK 470 VAL A 140 CG1 CG2 REMARK 470 TYR A 141 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER A 142 OG REMARK 470 PHE A 143 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU A 145 CG CD OE1 OE2 REMARK 470 PRO A 147 CG CD REMARK 470 LEU A 148 CG CD1 CD2 REMARK 470 THR A 149 OG1 CG2 REMARK 470 CYS A 150 SG REMARK 470 PHE A 151 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE A 152 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TRP A 153 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 153 CZ3 CH2 REMARK 470 PHE A 154 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE A 155 CG1 CG2 CD1 REMARK 470 LEU A 156 CG CD1 CD2 REMARK 470 GLN A 157 CG CD OE1 NE2 REMARK 470 ILE A 158 CG1 CG2 CD1 REMARK 470 PRO A 159 CG CD REMARK 470 GLU A 160 CG CD OE1 OE2 REMARK 470 HIS A 161 CG ND1 CD2 CE1 NE2 REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 163 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 164 CG CD1 CD2 REMARK 470 MET A 165 CG SD CE REMARK 470 LEU A 166 CG CD1 CD2 REMARK 470 SER A 167 OG REMARK 470 PRO A 168 CG CD REMARK 470 GLU A 169 CG CD OE1 OE2 REMARK 470 VAL A 170 CG1 CG2 REMARK 470 VAL A 171 CG1 CG2 REMARK 470 GLN A 172 CG CD OE1 NE2 REMARK 470 LEU A 174 CG CD1 CD2 REMARK 470 LEU A 175 CG CD1 CD2 REMARK 470 VAL A 176 CG1 CG2 REMARK 470 GLU A 177 CG CD OE1 OE2 REMARK 470 GLU A 178 CG CD OE1 OE2 REMARK 470 LEU A 179 CG CD1 CD2 REMARK 470 LEU A 180 CG CD1 CD2 REMARK 470 SER A 181 OG REMARK 470 THR A 182 OG1 CG2 REMARK 470 VAL A 183 CG1 CG2 REMARK 470 ASN A 184 CG OD1 ND2 REMARK 470 SER A 185 OG REMARK 470 SER A 186 OG REMARK 470 VAL A 189 CG1 CG2 REMARK 470 PRO A 190 CG CD REMARK 470 TYR A 191 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 192 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 194 CG CD OE1 OE2 REMARK 470 TYR A 195 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 196 CG CD OE1 OE2 REMARK 470 VAL A 197 CG1 CG2 REMARK 470 ASP A 198 CG OD1 OD2 REMARK 470 PRO A 199 CG CD REMARK 470 GLU A 200 CG CD OE1 OE2 REMARK 470 LEU A 202 CG CD1 CD2 REMARK 470 VAL A 203 CG1 CG2 REMARK 470 ILE A 204 CG1 CG2 CD1 REMARK 470 LEU A 205 CG CD1 CD2 REMARK 470 GLU A 206 CG CD OE1 OE2 REMARK 470 SER A 208 OG REMARK 470 SER H 75 OG REMARK 470 SER H 85 OG REMARK 470 THR H 119 CG2 REMARK 470 THR B 14 CG2 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 CYS A 292 CA - CB - SG ANGL. DEV. = 9.0 DEGREES REMARK 500 PHE L 94 N - CA - C ANGL. DEV. = 16.4 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 338 108.38 -161.99 REMARK 500 ASN A 406 -0.77 69.19 REMARK 500 LEU A 415 52.30 -93.09 REMARK 500 ASP A 456 65.76 28.37 REMARK 500 ASP A 500 15.76 -140.81 REMARK 500 ASP A 540 30.11 -93.76 REMARK 500 CYS A 566 57.47 -96.69 REMARK 500 HIS A 617 -1.16 -57.49 REMARK 500 HIS A 665 16.34 58.28 REMARK 500 ARG A 738 75.62 55.07 REMARK 500 TYR A 739 37.77 75.91 REMARK 500 ASP A 761 -175.72 73.29 REMARK 500 ASN L 30 14.99 103.80 REMARK 500 TRP L 32 65.80 -103.54 REMARK 500 ALA L 51 -10.77 72.17 REMARK 500 GLU L 81 48.04 -91.85 REMARK 500 SER L 93 160.03 100.39 REMARK 500 GLU L 143 98.61 -69.83 REMARK 500 ASN H 215 49.96 33.69 REMARK 500 LEU B 29 71.22 -106.70 REMARK 500 TYR B 38 45.03 -104.84 REMARK 500 LEU B 57 -10.35 72.39 REMARK 500 SER B 58 -37.49 -130.74 REMARK 500 ASN B 144 61.26 61.23 REMARK 500 ALA C 23 90.65 -164.95 REMARK 500 ASP C 31 -14.99 -142.80 REMARK 500 VAL C 48 -62.83 -121.50 REMARK 500 ASP C 152 60.29 60.54 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 902 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PRO A 472 O REMARK 620 2 ASP A 475 OD1 101.2 REMARK 620 3 VAL A 477 O 165.0 90.5 REMARK 620 4 ASP A 485 OD2 85.2 168.2 84.9 REMARK 620 5 GLU A 486 OE2 108.9 67.0 84.2 101.6 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 904 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 LYS A 508 O REMARK 620 2 ASP A 511 OD2 99.3 REMARK 620 3 GLN A 513 O 161.2 92.5 REMARK 620 4 ASP A 521 OD2 77.7 163.5 94.9 REMARK 620 5 GLU A 522 OE2 132.7 63.2 65.8 106.7 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 903 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PRO A 549 O REMARK 620 2 ASP A 552 OD1 89.4 REMARK 620 3 ARG A 554 O 163.0 75.6 REMARK 620 4 ASP A 556 OD2 86.0 95.0 87.3 REMARK 620 5 ASP A 562 OD2 80.4 168.4 115.2 89.9 REMARK 620 6 GLU A 563 OE2 133.1 114.9 62.3 127.4 69.5 REMARK 620 N 1 2 3 4 5 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-49728 RELATED DB: EMDB REMARK 900 TMPRSS6 IN COMPLEX WITH REGN7999 FAB AND REGN8023 FAB DBREF 9NRC A 77 811 UNP Q8IU80 TMPS6_HUMAN 77 811 DBREF 9NRC L 1 214 PDB 9NRC 9NRC 1 214 DBREF 9NRC H 1 240 PDB 9NRC 9NRC 1 240 DBREF 9NRC B 1 220 PDB 9NRC 9NRC 1 220 DBREF 9NRC C 1 237 PDB 9NRC 9NRC 1 237 SEQADV 9NRC ALA A 762 UNP Q8IU80 SER 762 ENGINEERED MUTATION SEQADV 9NRC GLU A 812 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC GLN A 813 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC LYS A 814 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC LEU A 815 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC ILE A 816 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC SER A 817 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC GLU A 818 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC GLU A 819 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC ASP A 820 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC LEU A 821 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC GLY A 822 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC GLY A 823 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC GLU A 824 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC GLN A 825 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC LYS A 826 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC LEU A 827 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC ILE A 828 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC SER A 829 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC GLU A 830 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC GLU A 831 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC ASP A 832 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC LEU A 833 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC HIS A 834 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC HIS A 835 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC HIS A 836 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC HIS A 837 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC HIS A 838 UNP Q8IU80 EXPRESSION TAG SEQADV 9NRC HIS A 839 UNP Q8IU80 EXPRESSION TAG SEQRES 1 A 763 GLY TYR LYS ALA GLU VAL MET VAL SER GLN VAL TYR SER SEQRES 2 A 763 GLY SER LEU ARG VAL LEU ASN ARG HIS PHE SER GLN ASP SEQRES 3 A 763 LEU THR ARG ARG GLU SER SER ALA PHE ARG SER GLU THR SEQRES 4 A 763 ALA LYS ALA GLN LYS MET LEU LYS GLU LEU ILE THR SER SEQRES 5 A 763 THR ARG LEU GLY THR TYR TYR ASN SER SER SER VAL TYR SEQRES 6 A 763 SER PHE GLY GLU GLY PRO LEU THR CYS PHE PHE TRP PHE SEQRES 7 A 763 ILE LEU GLN ILE PRO GLU HIS ARG ARG LEU MET LEU SER SEQRES 8 A 763 PRO GLU VAL VAL GLN ALA LEU LEU VAL GLU GLU LEU LEU SEQRES 9 A 763 SER THR VAL ASN SER SER ALA ALA VAL PRO TYR ARG ALA SEQRES 10 A 763 GLU TYR GLU VAL ASP PRO GLU GLY LEU VAL ILE LEU GLU SEQRES 11 A 763 ALA SER VAL LYS ASP ILE ALA ALA LEU ASN SER THR LEU SEQRES 12 A 763 GLY CYS TYR ARG TYR SER TYR VAL GLY GLN GLY GLN VAL SEQRES 13 A 763 LEU ARG LEU LYS GLY PRO ASP HIS LEU ALA SER SER CYS SEQRES 14 A 763 LEU TRP HIS LEU GLN GLY PRO LYS ASP LEU MET LEU LYS SEQRES 15 A 763 LEU ARG LEU GLU TRP THR LEU ALA GLU CYS ARG ASP ARG SEQRES 16 A 763 LEU ALA MET TYR ASP VAL ALA GLY PRO LEU GLU LYS ARG SEQRES 17 A 763 LEU ILE THR SER VAL TYR GLY CYS SER ARG GLN GLU PRO SEQRES 18 A 763 VAL VAL GLU VAL LEU ALA SER GLY ALA ILE MET ALA VAL SEQRES 19 A 763 VAL TRP LYS LYS GLY LEU HIS SER TYR TYR ASP PRO PHE SEQRES 20 A 763 VAL LEU SER VAL GLN PRO VAL VAL PHE GLN ALA CYS GLU SEQRES 21 A 763 VAL ASN LEU THR LEU ASP ASN ARG LEU ASP SER GLN GLY SEQRES 22 A 763 VAL LEU SER THR PRO TYR PHE PRO SER TYR TYR SER PRO SEQRES 23 A 763 GLN THR HIS CYS SER TRP HIS LEU THR VAL PRO SER LEU SEQRES 24 A 763 ASP TYR GLY LEU ALA LEU TRP PHE ASP ALA TYR ALA LEU SEQRES 25 A 763 ARG ARG GLN LYS TYR ASP LEU PRO CYS THR GLN GLY GLN SEQRES 26 A 763 TRP THR ILE GLN ASN ARG ARG LEU CYS GLY LEU ARG ILE SEQRES 27 A 763 LEU GLN PRO TYR ALA GLU ARG ILE PRO VAL VAL ALA THR SEQRES 28 A 763 ALA GLY ILE THR ILE ASN PHE THR SER GLN ILE SER LEU SEQRES 29 A 763 THR GLY PRO GLY VAL ARG VAL HIS TYR GLY LEU TYR ASN SEQRES 30 A 763 GLN SER ASP PRO CYS PRO GLY GLU PHE LEU CYS SER VAL SEQRES 31 A 763 ASN GLY LEU CYS VAL PRO ALA CYS ASP GLY VAL LYS ASP SEQRES 32 A 763 CYS PRO ASN GLY LEU ASP GLU ARG ASN CYS VAL CYS ARG SEQRES 33 A 763 ALA THR PHE GLN CYS LYS GLU ASP SER THR CYS ILE SER SEQRES 34 A 763 LEU PRO LYS VAL CYS ASP GLY GLN PRO ASP CYS LEU ASN SEQRES 35 A 763 GLY SER ASP GLU GLU GLN CYS GLN GLU GLY VAL PRO CYS SEQRES 36 A 763 GLY THR PHE THR PHE GLN CYS GLU ASP ARG SER CYS VAL SEQRES 37 A 763 LYS LYS PRO ASN PRO GLN CYS ASP GLY ARG PRO ASP CYS SEQRES 38 A 763 ARG ASP GLY SER ASP GLU GLU HIS CYS ASP CYS GLY LEU SEQRES 39 A 763 GLN GLY PRO SER SER ARG ILE VAL GLY GLY ALA VAL SER SEQRES 40 A 763 SER GLU GLY GLU TRP PRO TRP GLN ALA SER LEU GLN VAL SEQRES 41 A 763 ARG GLY ARG HIS ILE CYS GLY GLY ALA LEU ILE ALA ASP SEQRES 42 A 763 ARG TRP VAL ILE THR ALA ALA HIS CYS PHE GLN GLU ASP SEQRES 43 A 763 SER MET ALA SER THR VAL LEU TRP THR VAL PHE LEU GLY SEQRES 44 A 763 LYS VAL TRP GLN ASN SER ARG TRP PRO GLY GLU VAL SER SEQRES 45 A 763 PHE LYS VAL SER ARG LEU LEU LEU HIS PRO TYR HIS GLU SEQRES 46 A 763 GLU ASP SER HIS ASP TYR ASP VAL ALA LEU LEU GLN LEU SEQRES 47 A 763 ASP HIS PRO VAL VAL ARG SER ALA ALA VAL ARG PRO VAL SEQRES 48 A 763 CYS LEU PRO ALA ARG SER HIS PHE PHE GLU PRO GLY LEU SEQRES 49 A 763 HIS CYS TRP ILE THR GLY TRP GLY ALA LEU ARG GLU GLY SEQRES 50 A 763 GLY PRO ILE SER ASN ALA LEU GLN LYS VAL ASP VAL GLN SEQRES 51 A 763 LEU ILE PRO GLN ASP LEU CYS SER GLU VAL TYR ARG TYR SEQRES 52 A 763 GLN VAL THR PRO ARG MET LEU CYS ALA GLY TYR ARG LYS SEQRES 53 A 763 GLY LYS LYS ASP ALA CYS GLN GLY ASP ALA GLY GLY PRO SEQRES 54 A 763 LEU VAL CYS LYS ALA LEU SER GLY ARG TRP PHE LEU ALA SEQRES 55 A 763 GLY LEU VAL SER TRP GLY LEU GLY CYS GLY ARG PRO ASN SEQRES 56 A 763 TYR PHE GLY VAL TYR THR ARG ILE THR GLY VAL ILE SER SEQRES 57 A 763 TRP ILE GLN GLN VAL VAL THR GLU GLN LYS LEU ILE SER SEQRES 58 A 763 GLU GLU ASP LEU GLY GLY GLU GLN LYS LEU ILE SER GLU SEQRES 59 A 763 GLU ASP LEU HIS HIS HIS HIS HIS HIS SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL ILE ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLN ASP PHE ASN SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 214 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN THR SEQRES 8 L 214 ASP SER PHE PRO PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 L 214 ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 H 240 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 240 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 240 PHE THR PHE SER SER TYR ALA MET THR TRP VAL ARG GLN SEQRES 4 H 240 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE SER SEQRES 5 H 240 GLY SER ASP THR SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 240 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 240 LEU PHE LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 240 ALA VAL TYR TYR CYS ALA LYS HIS GLN ASP TYR ASP PHE SEQRES 9 H 240 SER TYR TYR TYR SER ALA MET ASP VAL TRP GLY GLN GLY SEQRES 10 H 240 THR THR VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 240 SER VAL PHE PRO LEU ALA PRO CYS SER ARG SER THR SER SEQRES 12 H 240 GLU SER THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 240 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 240 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 240 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 240 PRO SER SER SER LEU GLY THR LYS THR TYR THR CYS ASN SEQRES 17 H 240 VAL ASP HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18 H 240 VAL GLU SER LYS TYR GLY PRO PRO CYS PRO PRO CYS PRO SEQRES 19 H 240 ALA PRO GLU PHE LEU GLY SEQRES 1 B 220 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 B 220 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 B 220 GLN SER LEU LEU ASP SER ASP ASP GLY ASN THR TYR LEU SEQRES 4 B 220 ASP TRP TYR LEU ARG LYS PRO GLY GLN SER PRO GLN LEU SEQRES 5 B 220 LEU ILE TYR THR LEU SER TYR ARG ALA SER GLY VAL PRO SEQRES 6 B 220 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 B 220 LEU LYS ILE SER ARG VAL GLU ALA ASP ASP VAL GLY VAL SEQRES 8 B 220 TYR TYR CYS MET GLN ARG ILE GLU PHE PRO LEU THR PHE SEQRES 9 B 220 GLY GLY GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA SEQRES 10 B 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 B 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 B 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 B 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 B 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 B 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 B 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 B 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 237 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 C 237 PRO GLY GLY SER LEU ARG ILE SER CYS ALA ALA SER GLY SEQRES 3 C 237 PHE ILE PHE VAL ASP TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 C 237 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE SER SEQRES 5 C 237 TRP ASN SER GLY SER ILE GLY TYR ALA ASP SER VAL LYS SEQRES 6 C 237 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS LYS SER SEQRES 7 C 237 LEU TYR LEU GLN MET SER GLY LEU ARG PRO GLU ASP THR SEQRES 8 C 237 ALA LEU TYR TYR CYS VAL LYS SER GLY PHE TYR TYR VAL SEQRES 9 C 237 ARG SER TYR PHE ASP ASN TRP GLY GLN GLY THR LEU VAL SEQRES 10 C 237 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 C 237 PRO LEU ALA PRO CYS SER ARG SER THR SER GLU SER THR SEQRES 12 C 237 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 C 237 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 C 237 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 C 237 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 C 237 SER LEU GLY THR LYS THR TYR THR CYS ASN VAL ASP HIS SEQRES 17 C 237 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SER SEQRES 18 C 237 LYS TYR GLY PRO PRO CYS PRO PRO CYS PRO ALA PRO GLU SEQRES 19 C 237 PHE LEU GLY HET NAG E 1 14 HET NAG E 2 14 HET NAG D 1 14 HET NAG D 2 14 HET NAG F 1 14 HET NAG F 2 14 HET NAG A 901 14 HET CA A 902 1 HET CA A 903 1 HET CA A 904 1 HET NAG A 905 14 HET NAG A 906 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FORMUL 6 NAG 9(C8 H15 N O6) FORMUL 10 CA 3(CA 2+) HELIX 1 AA1 SER A 100 ARG A 105 5 6 HELIX 2 AA2 SER A 108 THR A 129 1 22 HELIX 3 AA3 ARG A 130 THR A 133 5 4 HELIX 4 AA4 HIS A 161 LEU A 166 5 6 HELIX 5 AA5 SER A 167 SER A 185 1 19 HELIX 6 AA6 ASP A 198 LEU A 202 5 5 HELIX 7 AA7 SER A 208 THR A 218 1 11 HELIX 8 AA8 LEU A 281 LYS A 283 5 3 HELIX 9 AA9 SER A 505 VAL A 509 5 5 HELIX 10 AB1 ALA A 615 PHE A 619 5 5 HELIX 11 AB2 ASP A 622 SER A 626 5 5 HELIX 12 AB3 PRO A 729 ARG A 738 1 10 HELIX 13 AB4 ILE A 799 GLY A 801 5 3 HELIX 14 AB5 VAL A 802 THR A 811 1 10 HELIX 15 AB6 GLN L 79 PHE L 83 5 5 HELIX 16 AB7 SER L 121 LYS L 126 1 6 HELIX 17 AB8 LYS L 183 LYS L 188 1 6 HELIX 18 AB9 THR H 28 TYR H 32 5 5 HELIX 19 AC1 SER H 167 ALA H 169 5 3 HELIX 20 AC2 SER H 198 LEU H 200 5 3 HELIX 21 AC3 ASP B 128 LYS B 132 5 5 HELIX 22 AC4 LYS B 189 GLU B 193 1 5 SHEET 1 AA1 4 TYR A 135 GLY A 144 0 SHEET 2 AA1 4 PRO A 147 PRO A 159 -1 O PHE A 151 N TYR A 141 SHEET 3 AA1 4 MET A 83 HIS A 98 -1 N VAL A 84 O ILE A 158 SHEET 4 AA1 4 VAL A 203 ALA A 207 -1 O VAL A 203 N SER A 91 SHEET 1 AA2 5 CYS A 221 TYR A 226 0 SHEET 2 AA2 5 SER A 244 GLN A 250 1 O HIS A 248 N ARG A 223 SHEET 3 AA2 5 ILE A 307 LYS A 313 -1 O TRP A 312 N CYS A 245 SHEET 4 AA2 5 ARG A 271 TYR A 275 -1 N TYR A 275 O ALA A 309 SHEET 5 AA2 5 LEU A 285 TYR A 290 -1 O VAL A 289 N LEU A 272 SHEET 1 AA3 4 LEU A 233 ARG A 234 0 SHEET 2 AA3 4 PHE A 323 VAL A 330 -1 O VAL A 327 N LEU A 233 SHEET 3 AA3 4 MET A 256 TRP A 263 -1 N LYS A 258 O GLN A 328 SHEET 4 AA3 4 VAL A 298 ALA A 303 -1 O VAL A 301 N LEU A 259 SHEET 1 AA4 6 VAL A 337 THR A 340 0 SHEET 2 AA4 6 HIS A 365 THR A 371 1 O HIS A 369 N LEU A 339 SHEET 3 AA4 6 GLY A 429 THR A 435 -1 O PHE A 434 N CYS A 366 SHEET 4 AA4 6 GLN A 401 ILE A 404 -1 N GLN A 401 O THR A 435 SHEET 5 AA4 6 ARG A 407 GLY A 411 -1 O ARG A 407 N ILE A 404 SHEET 6 AA4 6 LEU A 388 ARG A 389 -1 N ARG A 389 O CYS A 410 SHEET 1 AA5 4 SER A 347 SER A 352 0 SHEET 2 AA5 4 ARG A 446 ASN A 453 -1 O VAL A 447 N LEU A 351 SHEET 3 AA5 4 TYR A 377 PHE A 383 -1 N GLY A 378 O TYR A 452 SHEET 4 AA5 4 TYR A 418 ILE A 422 -1 O ILE A 422 N LEU A 379 SHEET 1 AA6 2 PHE A 462 CYS A 464 0 SHEET 2 AA6 2 LEU A 469 VAL A 471 -1 O VAL A 471 N PHE A 462 SHEET 1 AA7 2 PHE A 495 GLN A 496 0 SHEET 2 AA7 2 CYS A 503 ILE A 504 -1 O ILE A 504 N PHE A 495 SHEET 1 AA8 7 GLN A 591 VAL A 596 0 SHEET 2 AA8 7 ARG A 599 LEU A 606 -1 O CYS A 602 N LEU A 594 SHEET 3 AA8 7 TRP A 611 THR A 614 -1 O ILE A 613 N ALA A 605 SHEET 4 AA8 7 ALA A 670 LEU A 674 -1 O LEU A 672 N VAL A 612 SHEET 5 AA8 7 VAL A 647 LEU A 656 -1 N SER A 652 O GLN A 673 SHEET 6 AA8 7 THR A 631 LEU A 634 -1 N LEU A 634 O VAL A 647 SHEET 7 AA8 7 GLN A 591 VAL A 596 -1 N GLN A 595 O THR A 631 SHEET 1 AA9 6 HIS A 701 THR A 705 0 SHEET 2 AA9 6 LYS A 722 ILE A 728 -1 O VAL A 723 N ILE A 704 SHEET 3 AA9 6 MET A 745 GLY A 749 -1 O GLY A 749 N GLN A 726 SHEET 4 AA9 6 GLY A 794 THR A 797 -1 O GLY A 794 N ALA A 748 SHEET 5 AA9 6 TRP A 775 GLY A 784 -1 N TRP A 783 O VAL A 795 SHEET 6 AA9 6 PRO A 765 LYS A 769 -1 N CYS A 768 O PHE A 776 SHEET 1 AB1 4 THR L 5 SER L 7 0 SHEET 2 AB1 4 VAL L 19 ARG L 24 -1 O ARG L 24 N THR L 5 SHEET 3 AB1 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AB1 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB2 6 SER L 10 ALA L 13 0 SHEET 2 AB2 6 THR L 102 ILE L 106 1 O ASP L 105 N LEU L 11 SHEET 3 AB2 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB2 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AB2 6 LEU L 46 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AB2 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AB3 4 SER L 10 ALA L 13 0 SHEET 2 AB3 4 THR L 102 ILE L 106 1 O ASP L 105 N LEU L 11 SHEET 3 AB3 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB3 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB4 4 SER L 114 PHE L 118 0 SHEET 2 AB4 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB4 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB4 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB5 3 LYS L 145 VAL L 150 0 SHEET 2 AB5 3 TYR L 192 THR L 197 -1 O THR L 197 N LYS L 145 SHEET 3 AB5 3 SER L 208 PHE L 209 -1 O PHE L 209 N TYR L 192 SHEET 1 AB6 4 GLN H 3 SER H 7 0 SHEET 2 AB6 4 SER H 17 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AB6 4 THR H 78 ASN H 84 -1 O MET H 83 N LEU H 18 SHEET 4 AB6 4 THR H 69 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AB7 6 LEU H 11 VAL H 12 0 SHEET 2 AB7 6 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AB7 6 ALA H 92 HIS H 99 -1 N ALA H 92 O VAL H 120 SHEET 4 AB7 6 MET H 34 GLN H 39 -1 N GLN H 39 O VAL H 93 SHEET 5 AB7 6 LEU H 45 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AB7 6 THR H 58 TYR H 60 -1 O TYR H 59 N ALA H 50 SHEET 1 AB8 4 LEU H 11 VAL H 12 0 SHEET 2 AB8 4 THR H 118 VAL H 122 1 O THR H 121 N VAL H 12 SHEET 3 AB8 4 ALA H 92 HIS H 99 -1 N ALA H 92 O VAL H 120 SHEET 4 AB8 4 MET H 111 VAL H 113 -1 O VAL H 113 N LYS H 98 SHEET 1 AB9 4 SER H 131 LEU H 135 0 SHEET 2 AB9 4 THR H 146 TYR H 156 -1 O LEU H 152 N PHE H 133 SHEET 3 AB9 4 TYR H 187 PRO H 196 -1 O VAL H 193 N LEU H 149 SHEET 4 AB9 4 VAL H 174 THR H 176 -1 N HIS H 175 O VAL H 192 SHEET 1 AC1 4 SER H 131 LEU H 135 0 SHEET 2 AC1 4 THR H 146 TYR H 156 -1 O LEU H 152 N PHE H 133 SHEET 3 AC1 4 TYR H 187 PRO H 196 -1 O VAL H 193 N LEU H 149 SHEET 4 AC1 4 VAL H 180 LEU H 181 -1 N VAL H 180 O SER H 188 SHEET 1 AC2 3 THR H 162 TRP H 165 0 SHEET 2 AC2 3 TYR H 205 HIS H 211 -1 O ASP H 210 N THR H 162 SHEET 3 AC2 3 THR H 216 VAL H 222 -1 O LYS H 220 N CYS H 207 SHEET 1 AC3 4 THR B 5 SER B 7 0 SHEET 2 AC3 4 ALA B 19 ARG B 24 -1 O SER B 22 N SER B 7 SHEET 3 AC3 4 ASP B 76 ILE B 81 -1 O PHE B 77 N CYS B 23 SHEET 4 AC3 4 PHE B 68 SER B 73 -1 N SER B 69 O LYS B 80 SHEET 1 AC4 2 SER B 10 VAL B 13 0 SHEET 2 AC4 2 LYS B 109 ILE B 112 1 O GLU B 111 N VAL B 13 SHEET 1 AC5 4 TYR B 59 ARG B 60 0 SHEET 2 AC5 4 GLN B 51 TYR B 55 -1 N TYR B 55 O TYR B 59 SHEET 3 AC5 4 LEU B 39 ARG B 44 -1 N LEU B 43 O GLN B 51 SHEET 4 AC5 4 VAL B 91 GLN B 96 -1 O VAL B 91 N ARG B 44 SHEET 1 AC6 4 SER B 120 PHE B 124 0 SHEET 2 AC6 4 THR B 135 PHE B 145 -1 O LEU B 141 N PHE B 122 SHEET 3 AC6 4 TYR B 179 SER B 188 -1 O LEU B 181 N LEU B 142 SHEET 4 AC6 4 SER B 165 VAL B 169 -1 N GLN B 166 O THR B 184 SHEET 1 AC7 3 ALA B 150 VAL B 156 0 SHEET 2 AC7 3 VAL B 197 HIS B 204 -1 O GLU B 201 N GLN B 153 SHEET 3 AC7 3 THR B 212 ASN B 216 -1 O LYS B 213 N CYS B 200 SHEET 1 AC8 2 GLN C 3 LEU C 4 0 SHEET 2 AC8 2 ALA C 24 SER C 25 -1 O SER C 25 N GLN C 3 SHEET 1 AC9 6 GLY C 10 VAL C 12 0 SHEET 2 AC9 6 THR C 115 VAL C 119 1 O THR C 118 N GLY C 10 SHEET 3 AC9 6 ALA C 92 SER C 99 -1 N TYR C 94 O THR C 115 SHEET 4 AC9 6 MET C 34 GLN C 39 -1 N HIS C 35 O VAL C 97 SHEET 5 AC9 6 LEU C 45 ILE C 51 -1 O SER C 49 N TRP C 36 SHEET 6 AC9 6 GLY C 59 TYR C 60 -1 O GLY C 59 N GLY C 50 SHEET 1 AD1 4 GLY C 10 VAL C 12 0 SHEET 2 AD1 4 THR C 115 VAL C 119 1 O THR C 118 N GLY C 10 SHEET 3 AD1 4 ALA C 92 SER C 99 -1 N TYR C 94 O THR C 115 SHEET 4 AD1 4 PHE C 108 TRP C 111 -1 O ASN C 110 N LYS C 98 SHEET 1 AD2 3 SER C 17 SER C 21 0 SHEET 2 AD2 3 SER C 78 SER C 84 -1 O MET C 83 N LEU C 18 SHEET 3 AD2 3 PHE C 68 ASP C 73 -1 N SER C 71 O TYR C 80 SHEET 1 AD3 4 SER C 128 LEU C 132 0 SHEET 2 AD3 4 THR C 143 TYR C 153 -1 O GLY C 147 N LEU C 132 SHEET 3 AD3 4 TYR C 184 PRO C 193 -1 O VAL C 190 N LEU C 146 SHEET 4 AD3 4 VAL C 171 THR C 173 -1 N HIS C 172 O VAL C 189 SHEET 1 AD4 4 SER C 128 LEU C 132 0 SHEET 2 AD4 4 THR C 143 TYR C 153 -1 O GLY C 147 N LEU C 132 SHEET 3 AD4 4 TYR C 184 PRO C 193 -1 O VAL C 190 N LEU C 146 SHEET 4 AD4 4 VAL C 177 LEU C 178 -1 N VAL C 177 O SER C 185 SHEET 1 AD5 3 THR C 159 TRP C 162 0 SHEET 2 AD5 3 TYR C 202 HIS C 208 -1 O ASN C 205 N SER C 161 SHEET 3 AD5 3 THR C 213 VAL C 219 -1 O LYS C 217 N CYS C 204 SSBOND 1 CYS A 221 CYS A 245 1555 1555 2.03 SSBOND 2 CYS A 268 CYS A 292 1555 1555 2.04 SSBOND 3 CYS A 335 CYS A 366 1555 1555 2.03 SSBOND 4 CYS A 397 CYS A 410 1555 1555 2.03 SSBOND 5 CYS A 458 CYS A 470 1555 1555 2.03 SSBOND 6 CYS A 464 CYS A 480 1555 1555 2.04 SSBOND 7 CYS A 474 CYS A 489 1555 1555 2.03 SSBOND 8 CYS A 491 CYS A 503 1555 1555 2.03 SSBOND 9 CYS A 497 CYS A 516 1555 1555 2.04 SSBOND 10 CYS A 510 CYS A 525 1555 1555 2.03 SSBOND 11 CYS A 531 CYS A 543 1555 1555 2.03 SSBOND 12 CYS A 538 CYS A 557 1555 1555 2.04 SSBOND 13 CYS A 551 CYS A 566 1555 1555 2.03 SSBOND 14 CYS A 568 CYS A 688 1555 1555 2.03 SSBOND 15 CYS A 602 CYS A 618 1555 1555 2.04 SSBOND 16 CYS A 702 CYS A 768 1555 1555 2.03 SSBOND 17 CYS A 733 CYS A 747 1555 1555 2.03 SSBOND 18 CYS A 758 CYS A 787 1555 1555 2.02 SSBOND 19 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 20 CYS L 134 CYS L 194 1555 1555 2.04 SSBOND 21 CYS L 214 CYS H 138 1555 1555 2.03 SSBOND 22 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 23 CYS H 151 CYS H 207 1555 1555 2.04 SSBOND 24 CYS B 23 CYS B 94 1555 1555 2.04 SSBOND 25 CYS B 140 CYS B 200 1555 1555 2.03 SSBOND 26 CYS B 220 CYS C 135 1555 1555 2.03 SSBOND 27 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 28 CYS C 148 CYS C 204 1555 1555 2.03 LINK ND2 ASN A 136 C1 NAG A 901 1555 1555 1.44 LINK ND2 ASN A 216 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN A 338 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 433 C1 NAG F 1 1555 1555 1.44 LINK ND2 ASN A 453 C1 NAG A 905 1555 1555 1.44 LINK ND2 ASN A 518 C1 NAG A 906 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O PRO A 472 CA CA A 902 1555 1555 2.59 LINK OD1 ASP A 475 CA CA A 902 1555 1555 2.39 LINK O VAL A 477 CA CA A 902 1555 1555 2.32 LINK OD2 ASP A 485 CA CA A 902 1555 1555 2.47 LINK OE2 GLU A 486 CA CA A 902 1555 1555 2.48 LINK O LYS A 508 CA CA A 904 1555 1555 2.22 LINK OD2 ASP A 511 CA CA A 904 1555 1555 2.31 LINK O GLN A 513 CA CA A 904 1555 1555 2.22 LINK OD2 ASP A 521 CA CA A 904 1555 1555 2.74 LINK OE2 GLU A 522 CA CA A 904 1555 1555 2.79 LINK O PRO A 549 CA CA A 903 1555 1555 2.29 LINK OD1 ASP A 552 CA CA A 903 1555 1555 2.29 LINK O ARG A 554 CA CA A 903 1555 1555 2.78 LINK OD2 ASP A 556 CA CA A 903 1555 1555 2.30 LINK OD2 ASP A 562 CA CA A 903 1555 1555 2.55 LINK OE2 GLU A 563 CA CA A 903 1555 1555 2.26 CISPEP 1 PHE A 356 PRO A 357 0 0.54 CISPEP 2 SER L 7 PRO L 8 0 19.39 CISPEP 3 TYR L 140 PRO L 141 0 0.25 CISPEP 4 PHE H 157 PRO H 158 0 -2.16 CISPEP 5 GLU H 159 PRO H 160 0 -1.67 CISPEP 6 SER B 7 PRO B 8 0 -6.09 CISPEP 7 PHE B 100 PRO B 101 0 27.34 CISPEP 8 TYR B 146 PRO B 147 0 0.85 CISPEP 9 PHE C 154 PRO C 155 0 -5.26 CISPEP 10 GLU C 156 PRO C 157 0 -2.79 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000