HEADER MEMBRANE PROTEIN 15-JUL-23 8THE TITLE CRYO-EM STRUCTURE OF PSEUDOMONAS AERUGINOSA TONB-DEPENDENT TRANSPORTER TITLE 2 PHUR IN COMPLEX WITH SYNTHETIC ANTIBODY AND HEME COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEME/HEMOGLOBIN UPTAKE OUTER MEMBRANE RECEPTOR PHUR; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SYNTHETIC ANTIBODY HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SYNTHETIC ANTIBODY LIGHT CHAIN; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA; SOURCE 3 ORGANISM_TAXID: 287; SOURCE 4 ATCC: 47085; SOURCE 5 GENE: PHUR, PA4710; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS BETA BARREL, OUTER MEMBRANE PROTEIN, HEME BINDING PROTEIN, HEME KEYWDS 2 TRANSPORT, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR P.KNEJSKI,S.K.ERRAMILLI,A.A.KOSSIAKOFF JRNL AUTH P.KNEJSKI,S.K.ERRAMILLI,A.A.KOSSIAKOFF JRNL TITL CHAPERONE-ASSISTED CRYO-EM STRUCTURE OF P. AERUGINOSA PHUR JRNL TITL 2 REVEALS MOLECULAR BASIS FOR HEME BINDING JRNL REF STRUCTURE 2024 JRNL REFN ISSN 0969-2126 JRNL DOI 10.1016/J.STR.2024.01.007 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : RELION, RELION, COOT, PHENIX, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC 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) : 2.500 REMARK 3 NUMBER OF PARTICLES : 292512 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 8THE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000275949. 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 : HEME BOUND P. AERUGINOSA PHUR REMARK 245 WITH BOUND SYNTHETIC ANTIBODY REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 5.00 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 : 5031 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 900.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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) : 60.00 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 -12 REMARK 465 LYS A -11 REMARK 465 TYR A -10 REMARK 465 LEU A -9 REMARK 465 LEU A -8 REMARK 465 PRO A -7 REMARK 465 THR A -6 REMARK 465 ALA A -5 REMARK 465 ALA A -4 REMARK 465 ALA A -3 REMARK 465 GLY A -2 REMARK 465 LEU A -1 REMARK 465 LEU A 0 REMARK 465 LEU A 1 REMARK 465 LEU A 2 REMARK 465 ALA A 3 REMARK 465 ALA A 4 REMARK 465 GLN A 5 REMARK 465 PRO A 6 REMARK 465 ALA A 7 REMARK 465 MET A 8 REMARK 465 ALA A 9 REMARK 465 MET A 10 REMARK 465 GLY A 11 REMARK 465 HIS A 12 REMARK 465 HIS A 13 REMARK 465 HIS A 14 REMARK 465 HIS A 15 REMARK 465 HIS A 16 REMARK 465 HIS A 17 REMARK 465 GLY A 18 REMARK 465 GLU A 19 REMARK 465 ASN A 20 REMARK 465 LEU A 21 REMARK 465 TYR A 22 REMARK 465 PHE A 23 REMARK 465 GLN A 24 REMARK 465 GLY A 25 REMARK 465 GLY A 26 REMARK 465 ASN A 27 REMARK 465 ALA A 28 REMARK 465 VAL A 29 REMARK 465 PRO A 30 REMARK 465 LEU A 31 REMARK 465 THR A 32 REMARK 465 PRO A 33 REMARK 465 THR A 34 REMARK 465 THR A 35 REMARK 465 ILE A 36 REMARK 465 THR A 37 REMARK 465 ALA A 38 REMARK 465 THR A 39 REMARK 465 ARG A 40 REMARK 465 THR A 41 REMARK 465 GLU A 42 REMARK 465 GLN A 43 REMARK 465 ALA A 44 REMARK 465 VAL A 45 REMARK 465 ASP A 46 REMARK 465 ASP A 579 REMARK 465 SER A 580 REMARK 465 THR A 581 REMARK 465 GLY A 582 REMARK 465 GLY A 583 REMARK 465 ASN A 584 REMARK 465 GLU H 1 REMARK 465 SER H 129 REMARK 465 SER H 130 REMARK 465 ALA H 131 REMARK 465 SER H 132 REMARK 465 THR H 133 REMARK 465 LYS H 134 REMARK 465 GLY H 135 REMARK 465 PRO H 136 REMARK 465 SER H 137 REMARK 465 VAL H 138 REMARK 465 PHE H 139 REMARK 465 PRO H 140 REMARK 465 LEU H 141 REMARK 465 ALA H 142 REMARK 465 PRO H 143 REMARK 465 SER H 144 REMARK 465 SER H 145 REMARK 465 LYS H 146 REMARK 465 SER H 147 REMARK 465 THR H 148 REMARK 465 SER H 149 REMARK 465 GLY H 150 REMARK 465 GLY H 151 REMARK 465 THR H 152 REMARK 465 ALA H 153 REMARK 465 ALA H 154 REMARK 465 LEU H 155 REMARK 465 GLY H 156 REMARK 465 CYS H 157 REMARK 465 LEU H 158 REMARK 465 VAL H 159 REMARK 465 LYS H 160 REMARK 465 ASP H 161 REMARK 465 TYR H 162 REMARK 465 PHE H 163 REMARK 465 PRO H 164 REMARK 465 GLU H 165 REMARK 465 PRO H 166 REMARK 465 VAL H 167 REMARK 465 THR H 168 REMARK 465 VAL H 169 REMARK 465 SER H 170 REMARK 465 TRP H 171 REMARK 465 ASN H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 ALA H 175 REMARK 465 LEU H 176 REMARK 465 THR H 177 REMARK 465 SER H 178 REMARK 465 GLY H 179 REMARK 465 VAL H 180 REMARK 465 HIS H 181 REMARK 465 THR H 182 REMARK 465 PHE H 183 REMARK 465 PRO H 184 REMARK 465 ALA H 185 REMARK 465 VAL H 186 REMARK 465 LEU H 187 REMARK 465 GLN H 188 REMARK 465 SER H 189 REMARK 465 SER H 190 REMARK 465 GLY H 191 REMARK 465 LEU H 192 REMARK 465 TYR H 193 REMARK 465 SER H 194 REMARK 465 LEU H 195 REMARK 465 SER H 196 REMARK 465 SER H 197 REMARK 465 VAL H 198 REMARK 465 VAL H 199 REMARK 465 THR H 200 REMARK 465 VAL H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 SER H 204 REMARK 465 SER H 205 REMARK 465 LEU H 206 REMARK 465 GLY H 207 REMARK 465 THR H 208 REMARK 465 GLN H 209 REMARK 465 THR H 210 REMARK 465 TYR H 211 REMARK 465 ILE H 212 REMARK 465 CYS H 213 REMARK 465 ASN H 214 REMARK 465 VAL H 215 REMARK 465 ASN H 216 REMARK 465 HIS H 217 REMARK 465 LYS H 218 REMARK 465 PRO H 219 REMARK 465 SER H 220 REMARK 465 ASN H 221 REMARK 465 THR H 222 REMARK 465 LYS H 223 REMARK 465 VAL H 224 REMARK 465 ASP H 225 REMARK 465 LYS H 226 REMARK 465 LYS H 227 REMARK 465 VAL H 228 REMARK 465 GLU H 229 REMARK 465 PRO H 230 REMARK 465 LYS H 231 REMARK 465 SER H 232 REMARK 465 CYS H 233 REMARK 465 ASP H 234 REMARK 465 LYS H 235 REMARK 465 THR H 236 REMARK 465 HIS H 237 REMARK 465 THR H 238 REMARK 465 SER L 1 REMARK 465 ARG L 109 REMARK 465 THR L 110 REMARK 465 VAL L 111 REMARK 465 ALA L 112 REMARK 465 ALA L 113 REMARK 465 PRO L 114 REMARK 465 SER L 115 REMARK 465 VAL L 116 REMARK 465 PHE L 117 REMARK 465 ILE L 118 REMARK 465 PHE L 119 REMARK 465 PRO L 120 REMARK 465 PRO L 121 REMARK 465 SER L 122 REMARK 465 ASP L 123 REMARK 465 SER L 124 REMARK 465 GLN L 125 REMARK 465 LEU L 126 REMARK 465 LYS L 127 REMARK 465 SER L 128 REMARK 465 GLY L 129 REMARK 465 THR L 130 REMARK 465 ALA L 131 REMARK 465 SER L 132 REMARK 465 VAL L 133 REMARK 465 VAL L 134 REMARK 465 CYS L 135 REMARK 465 LEU L 136 REMARK 465 LEU L 137 REMARK 465 ASN L 138 REMARK 465 ASN L 139 REMARK 465 PHE L 140 REMARK 465 TYR L 141 REMARK 465 PRO L 142 REMARK 465 ARG L 143 REMARK 465 GLU L 144 REMARK 465 ALA L 145 REMARK 465 LYS L 146 REMARK 465 VAL L 147 REMARK 465 GLN L 148 REMARK 465 TRP L 149 REMARK 465 LYS L 150 REMARK 465 VAL L 151 REMARK 465 ASP L 152 REMARK 465 ASN L 153 REMARK 465 ALA L 154 REMARK 465 LEU L 155 REMARK 465 GLN L 156 REMARK 465 SER L 157 REMARK 465 GLY L 158 REMARK 465 ASN L 159 REMARK 465 SER L 160 REMARK 465 GLN L 161 REMARK 465 GLU L 162 REMARK 465 SER L 163 REMARK 465 VAL L 164 REMARK 465 THR L 165 REMARK 465 GLU L 166 REMARK 465 GLN L 167 REMARK 465 ASP L 168 REMARK 465 SER L 169 REMARK 465 LYS L 170 REMARK 465 ASP L 171 REMARK 465 SER L 172 REMARK 465 THR L 173 REMARK 465 TYR L 174 REMARK 465 SER L 175 REMARK 465 LEU L 176 REMARK 465 SER L 177 REMARK 465 SER L 178 REMARK 465 THR L 179 REMARK 465 LEU L 180 REMARK 465 THR L 181 REMARK 465 LEU L 182 REMARK 465 SER L 183 REMARK 465 LYS L 184 REMARK 465 ALA L 185 REMARK 465 ASP L 186 REMARK 465 TYR L 187 REMARK 465 GLU L 188 REMARK 465 LYS L 189 REMARK 465 HIS L 190 REMARK 465 LYS L 191 REMARK 465 VAL L 192 REMARK 465 TYR L 193 REMARK 465 ALA L 194 REMARK 465 CYS L 195 REMARK 465 GLU L 196 REMARK 465 VAL L 197 REMARK 465 THR L 198 REMARK 465 HIS L 199 REMARK 465 GLN L 200 REMARK 465 GLY L 201 REMARK 465 LEU L 202 REMARK 465 SER L 203 REMARK 465 SER L 204 REMARK 465 PRO L 205 REMARK 465 VAL L 206 REMARK 465 THR L 207 REMARK 465 LYS L 208 REMARK 465 SER L 209 REMARK 465 PHE L 210 REMARK 465 ASN L 211 REMARK 465 ARG L 212 REMARK 465 GLY L 213 REMARK 465 GLU L 214 REMARK 465 CYS L 215 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OE1 GLN L 91 O HOH L 301 2.08 REMARK 500 OE1 GLU H 4 O HOH H 301 2.16 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 PRO A 49 46.40 -81.36 REMARK 500 ASN A 126 50.82 -140.94 REMARK 500 ASP A 199 -121.76 60.77 REMARK 500 ILE A 347 -59.35 68.43 REMARK 500 ASP A 424 65.67 39.30 REMARK 500 ASN A 441 -121.73 59.91 REMARK 500 GLN A 498 -3.22 67.32 REMARK 500 ALA A 742 71.77 -151.73 REMARK 500 PHE H 32 31.49 -99.29 REMARK 500 THR H 77 -6.77 72.04 REMARK 500 ALA H 95 -179.32 -171.29 REMARK 500 ALA L 52 -6.78 72.25 REMARK 500 ALA L 85 -169.26 -161.73 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 73 0.17 SIDE CHAIN 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 HEM A 801 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TYR A 529 OH REMARK 620 2 HEM A 801 NA 94.4 REMARK 620 3 HEM A 801 NB 79.9 90.7 REMARK 620 4 HEM A 801 NC 89.3 176.3 89.3 REMARK 620 5 HEM A 801 ND 103.2 89.3 176.8 90.4 REMARK 620 N 1 2 3 4 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-41255 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF PSEUDOMONAS AERUGINOSA TONB-DEPENDENT REMARK 900 TRANSPORTER PHUR IN COMPLEX WITH SYNTHETIC ANTIBODY AND HEME DBREF 8THE A 26 764 UNP Q9HV88 Q9HV88_PSEAE 26 764 DBREF 8THE H 1 238 PDB 8THE 8THE 1 238 DBREF 8THE L 1 215 PDB 8THE 8THE 1 215 SEQADV 8THE MET A -12 UNP Q9HV88 INITIATING METHIONINE SEQADV 8THE LYS A -11 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE TYR A -10 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE LEU A -9 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE LEU A -8 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE PRO A -7 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE THR A -6 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE ALA A -5 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE ALA A -4 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE ALA A -3 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE GLY A -2 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE LEU A -1 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE LEU A 0 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE LEU A 1 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE LEU A 2 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE ALA A 3 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE ALA A 4 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE GLN A 5 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE PRO A 6 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE ALA A 7 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE MET A 8 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE ALA A 9 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE MET A 10 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE GLY A 11 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE HIS A 12 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE HIS A 13 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE HIS A 14 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE HIS A 15 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE HIS A 16 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE HIS A 17 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE GLY A 18 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE GLU A 19 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE ASN A 20 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE LEU A 21 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE TYR A 22 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE PHE A 23 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE GLN A 24 UNP Q9HV88 EXPRESSION TAG SEQADV 8THE GLY A 25 UNP Q9HV88 EXPRESSION TAG SEQRES 1 A 777 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 A 777 LEU LEU ALA ALA GLN PRO ALA MET ALA MET GLY HIS HIS SEQRES 3 A 777 HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE GLN GLY GLY SEQRES 4 A 777 ASN ALA VAL PRO LEU THR PRO THR THR ILE THR ALA THR SEQRES 5 A 777 ARG THR GLU GLN ALA VAL ASP SER VAL PRO SER THR VAL SEQRES 6 A 777 SER VAL GLN THR ARG GLU GLN LEU ASP ARG GLN ASN VAL SEQRES 7 A 777 ASN ASN ILE LYS GLU LEU VAL ARG TYR GLU PRO GLY VAL SEQRES 8 A 777 SER VAL GLY GLY ALA GLY GLN ARG ALA GLY ILE THR GLY SEQRES 9 A 777 TYR ASN ILE ARG GLY ILE ASP GLY ASN ARG ILE LEU THR SEQRES 10 A 777 GLN ILE ASP GLY VAL GLU LEU PRO ASN ASP PHE PHE SER SEQRES 11 A 777 GLY PRO TYR ALA GLN THR HIS ARG ASN TYR VAL ASP PRO SEQRES 12 A 777 ASP ILE VAL LYS ARG VAL GLU ILE LEU ARG GLY PRO ALA SEQRES 13 A 777 SER ALA LEU TYR GLY SER ASN ALA ILE GLY GLY ALA VAL SEQRES 14 A 777 SER TYR PHE THR LEU ASP PRO SER ASP ILE ILE LYS ASP SEQRES 15 A 777 GLY LYS ASP VAL GLY ALA ARG LEU LYS ALA GLY TYR GLU SEQRES 16 A 777 SER ALA SER HIS SER TRP LEU THR SER ALA THR VAL ALA SEQRES 17 A 777 GLY ARG ALA ASP ASP PHE ASP GLY LEU LEU HIS TYR GLY SEQRES 18 A 777 TYR ARG GLN GLY HIS GLU THR GLU SER ASN GLY GLY HIS SEQRES 19 A 777 GLY GLY THR GLY LEU SER ARG SER GLU ALA ASN PRO GLU SEQRES 20 A 777 ASP ALA ASP SER TYR SER LEU LEU GLY LYS LEU GLY TRP SEQRES 21 A 777 ASN TYR ALA GLU GLY SER ARG PHE GLY LEU VAL PHE GLU SEQRES 22 A 777 LYS TYR LYS SER ASP VAL ASP THR ASP GLN LYS SER ALA SEQRES 23 A 777 TYR GLY GLY PRO TYR ASP LYS GLY LYS PRO ALA ILE PRO SEQRES 24 A 777 PRO SER MET LEU PRO GLY GLY MET TYR GLN TRP ARG LYS SEQRES 25 A 777 GLY ASN ASP THR LEU THR ARG GLU ARG TYR GLY LEU GLU SEQRES 26 A 777 HIS HIS PHE LEU LEU ASP SER GLN VAL ALA ASP ARG ILE SEQRES 27 A 777 GLN TRP SER LEU ASN TYR GLN LEU ALA LYS THR ASP GLN SEQRES 28 A 777 ALA THR ARG GLU PHE TYR TYR PRO ILE THR ARG LYS VAL SEQRES 29 A 777 LEU ARG THR ARG ASP THR THR TYR LYS GLU ARG LEU TRP SEQRES 30 A 777 VAL PHE ASP SER GLN LEU ASP LYS SER PHE ALA ILE GLY SEQRES 31 A 777 GLU THR GLU HIS LEU LEU SER TYR GLY ILE ASN LEU LYS SEQRES 32 A 777 HIS GLN LYS VAL THR GLY MET ARG SER GLY THR GLY THR SEQRES 33 A 777 ASN LEU ASP THR GLY ALA ASP SER PRO ARG ASP ALA LEU SEQRES 34 A 777 GLU ARG SER SER ASP PHE PRO ASP PRO THR VAL LYS THR SEQRES 35 A 777 TYR ALA LEU PHE ALA GLN ASP SER ILE SER TRP ASN ASP SEQRES 36 A 777 TRP THR PHE THR PRO GLY LEU ARG TYR ASP TYR THR ARG SEQRES 37 A 777 MET GLU PRO HIS ILE THR ASP GLU PHE LEU ARG THR MET SEQRES 38 A 777 LYS GLN SER GLN ASN THR ALA VAL ASP GLU SER ASP LYS SEQRES 39 A 777 LYS TRP HIS ARG VAL SER PRO LYS PHE GLY VAL THR TYR SEQRES 40 A 777 ASP PHE ALA GLN HIS TYR THR TRP TYR GLY GLN TYR ALA SEQRES 41 A 777 GLN GLY PHE ARG THR PRO THR ALA LYS ALA LEU TYR GLY SEQRES 42 A 777 ARG PHE GLU ASN LEU GLN ALA GLY TYR HIS ILE GLU PRO SEQRES 43 A 777 ASN PRO ASN LEU LYS PRO GLU LYS SER GLN SER PHE GLU SEQRES 44 A 777 THR GLY LEU ARG GLY LYS PHE ASP GLU GLY SER PHE GLY SEQRES 45 A 777 VAL ALA VAL PHE TYR ASN LYS TYR ARG ASP PHE ILE ASP SEQRES 46 A 777 GLU ASP ALA LEU ASN THR ASP SER THR GLY GLY ASN GLY SEQRES 47 A 777 GLN THR PHE GLN SER ASN ASN ILE GLU ARG ALA VAL ILE SEQRES 48 A 777 LYS GLY VAL GLU LEU LYS GLY ARG LEU GLU LEU GLY ALA SEQRES 49 A 777 PHE GLY ALA PRO GLN GLY LEU TYR THR GLN GLY SER VAL SEQRES 50 A 777 ALA TYR ALA TYR GLY ARG ASN LYS ASP ASN GLY GLU PRO SEQRES 51 A 777 ILE ASN SER VAL ASN PRO LEU THR GLY VAL PHE GLY LEU SEQRES 52 A 777 GLY TYR ASP GLU ALA ASP GLY ASN TYR GLY GLY LEU LEU SEQRES 53 A 777 SER TRP THR LEU VAL LYS ARG LYS ASP ARG VAL ASP ASP SEQRES 54 A 777 SER THR PHE HIS THR PRO ASP GLY THR ALA SER GLN PHE SEQRES 55 A 777 LYS THR PRO GLY PHE GLY VAL LEU ASP LEU SER ALA TYR SEQRES 56 A 777 TYR ARG LEU SER LYS ASP LEU THR LEU ASN ALA GLY LEU SEQRES 57 A 777 TYR ASN LEU THR ASP LYS LYS TYR TRP LEU TRP ASP ASP SEQRES 58 A 777 VAL ARG GLY TYR ASP SER VAL GLY GLU ALA SER ALA LEU SEQRES 59 A 777 ALA PRO ALA ASN ILE ASP ARG LEU SER GLN PRO GLY ARG SEQRES 60 A 777 ASN PHE ALA VAL ASN LEU VAL TRP ASP ILE SEQRES 1 H 238 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 H 238 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 H 238 ALA SER GLY PHE ASN PHE TYR TYR TYR SER ILE HIS TRP SEQRES 4 H 238 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 H 238 SER ILE SER PRO TYR TYR GLY SER THR TYR TYR ALA ASP SEQRES 6 H 238 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 H 238 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 H 238 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG SER MET ASN SEQRES 9 H 238 TRP TYR TYR SER SER PRO TYR GLY MET SER GLN GLY MET SEQRES 10 H 238 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 11 H 238 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 H 238 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 H 238 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 H 238 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 H 238 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 H 238 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 H 238 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 H 238 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 19 H 238 LYS THR HIS THR SEQRES 1 L 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 L 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 L 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 L 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 215 GLY SER SER SER PRO LEU THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS HET HEM A 801 43 HET CTQ A 802 138 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 4 HEM C34 H32 FE N4 O4 FORMUL 5 CTQ FORMUL 6 HOH *81(H2 O) HELIX 1 AA1 ARG A 57 GLN A 63 1 7 HELIX 2 AA2 ASN A 67 VAL A 72 1 6 HELIX 3 AA3 ASP A 98 ASN A 100 5 3 HELIX 4 AA4 ASP A 129 ASP A 131 5 3 HELIX 5 AA5 ASP A 162 ILE A 167 1 6 HELIX 6 AA6 THR A 224 ARG A 228 5 5 HELIX 7 AA7 LYS A 271 TYR A 274 5 4 HELIX 8 AA8 SER A 411 ALA A 415 5 5 HELIX 9 AA9 THR A 461 SER A 471 1 11 HELIX 10 AB1 THR A 514 GLY A 520 1 7 HELIX 11 AB2 GLY A 610 PHE A 612 5 3 HELIX 12 AB3 LEU A 725 GLY A 731 1 7 HELIX 13 AB4 GLU A 737 ALA A 742 1 6 HELIX 14 AB5 ASP H 65 LYS H 68 5 4 HELIX 15 AB6 ARG H 90 THR H 94 5 5 HELIX 16 AB7 SER H 109 MET H 113 5 5 HELIX 17 AB8 GLN L 80 PHE L 84 5 5 SHEET 1 AA1 5 VAL A 52 THR A 56 0 SHEET 2 AA1 5 VAL A 133 ARG A 140 -1 O ILE A 138 N SER A 53 SHEET 3 AA1 5 GLY A 154 THR A 160 -1 O PHE A 159 N LYS A 134 SHEET 4 AA1 5 ILE A 102 ILE A 106 1 N LEU A 103 O VAL A 156 SHEET 5 AA1 5 VAL A 109 GLU A 110 -1 O VAL A 109 N ILE A 106 SHEET 1 AA2 2 VAL A 78 VAL A 80 0 SHEET 2 AA2 2 TYR A 92 ILE A 94 -1 O ASN A 93 N SER A 79 SHEET 1 AA3 2 PHE A 115 PHE A 116 0 SHEET 2 AA3 2 GLN A 122 THR A 123 -1 O THR A 123 N PHE A 115 SHEET 1 AA426 VAL A 173 GLU A 182 0 SHEET 2 AA426 SER A 187 ALA A 198 -1 O ALA A 195 N GLY A 174 SHEET 3 AA426 PHE A 201 HIS A 213 -1 O TYR A 207 N ALA A 192 SHEET 4 AA426 GLU A 234 ALA A 250 -1 O SER A 238 N ARG A 210 SHEET 5 AA426 SER A 253 ASP A 269 -1 O ASP A 265 N ASP A 237 SHEET 6 AA426 TYR A 295 LEU A 316 -1 O LEU A 304 N SER A 264 SHEET 7 AA426 ARG A 324 TYR A 344 -1 O ARG A 341 N LYS A 299 SHEET 8 AA426 VAL A 351 ILE A 376 -1 O ARG A 355 N THR A 340 SHEET 9 AA426 THR A 379 ASN A 404 -1 O TYR A 385 N LEU A 370 SHEET 10 AA426 LEU A 416 SER A 419 -1 O LEU A 416 N GLY A 400 SHEET 11 AA426 THR A 426 TRP A 440 -1 O GLN A 435 N SER A 384 SHEET 12 AA426 TRP A 443 GLU A 457 -1 O TYR A 451 N LEU A 432 SHEET 13 AA426 LYS A 481 PHE A 496 -1 O GLY A 491 N THR A 446 SHEET 14 AA426 TYR A 500 ARG A 511 -1 O TYR A 506 N PHE A 490 SHEET 15 AA426 PHE A 522 ASN A 524 0 SHEET 16 AA426 TYR A 529 GLU A 532 -1 O ILE A 531 N PHE A 522 SHEET 17 AA426 GLU A 540 PHE A 553 -1 O GLU A 546 N GLN A 505 SHEET 18 AA426 GLY A 556 LEU A 576 -1 O ARG A 568 N LYS A 541 SHEET 19 AA426 GLN A 586 GLU A 608 -1 O ALA A 596 N TYR A 567 SHEET 20 AA426 LEU A 618 ASN A 631 -1 O VAL A 624 N LEU A 603 SHEET 21 AA426 GLU A 636 PRO A 637 -1 O GLU A 636 N ASN A 631 SHEET 22 AA426 THR A 645 ASP A 653 -1 O GLY A 651 N TYR A 619 SHEET 23 AA426 TYR A 659 VAL A 668 -1 O LEU A 667 N GLY A 646 SHEET 24 AA426 PHE A 694 ARG A 704 -1 O ASP A 698 N SER A 664 SHEET 25 AA426 LEU A 709 TYR A 716 -1 O LEU A 715 N LEU A 699 SHEET 26 AA426 ASN A 755 TRP A 762 -1 O ASN A 755 N TYR A 716 SHEET 1 AA5 2 TYR A 278 ASP A 279 0 SHEET 2 AA5 2 LYS A 282 PRO A 283 -1 O LYS A 282 N ASP A 279 SHEET 1 AA6 4 VAL H 5 SER H 10 0 SHEET 2 AA6 4 LEU H 21 GLY H 29 -1 O SER H 28 N GLN H 6 SHEET 3 AA6 4 THR H 81 MET H 86 -1 O ALA H 82 N CYS H 25 SHEET 4 AA6 4 PHE H 71 ALA H 75 -1 N THR H 72 O GLN H 85 SHEET 1 AA7 6 ILE H 37 GLN H 42 0 SHEET 2 AA7 6 LEU H 48 SER H 55 -1 O ILE H 54 N ILE H 37 SHEET 3 AA7 6 SER H 60 TYR H 63 -1 O SER H 60 N SER H 55 SHEET 4 AA7 6 ALA H 95 SER H 102 -1 O TYR H 98 N VAL H 40 SHEET 5 AA7 6 MET H 117 TRP H 120 -1 O TYR H 119 N ARG H 101 SHEET 6 AA7 6 THR H 124 VAL H 126 -1 O VAL H 126 N ALA H 95 SHEET 1 AA8 4 MET L 5 SER L 8 0 SHEET 2 AA8 4 VAL L 20 ALA L 26 -1 O ARG L 25 N THR L 6 SHEET 3 AA8 4 ASP L 71 ILE L 76 -1 O PHE L 72 N CYS L 24 SHEET 4 AA8 4 PHE L 63 SER L 68 -1 N SER L 68 O ASP L 71 SHEET 1 AA9 7 SER L 11 ALA L 14 0 SHEET 2 AA9 7 VAL L 34 GLN L 39 0 SHEET 3 AA9 7 LYS L 46 TYR L 50 -1 O ILE L 49 N TRP L 36 SHEET 4 AA9 7 SER L 54 LEU L 55 -1 O SER L 54 N TYR L 50 SHEET 5 AA9 7 THR L 86 GLN L 91 -1 O GLN L 90 N ALA L 35 SHEET 6 AA9 7 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 7 AA9 7 THR L 103 ILE L 107 -1 O THR L 103 N TYR L 87 SSBOND 1 CYS H 25 CYS H 99 1555 1555 2.03 SSBOND 2 CYS L 24 CYS L 89 1555 1555 2.03 LINK OH TYR A 529 FE HEM A 801 1555 1555 1.92 CISPEP 1 GLY A 276 PRO A 277 0 0.36 CISPEP 2 SER L 8 PRO L 9 0 -9.21 CISPEP 3 SER L 95 PRO L 96 0 1.06 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