HEADER MEMBRANE PROTEIN 29-JUL-23 8TMP TITLE CRYO-EM STRUCTURE OF MAGNESIUM DEPLETED CORA IN COMPLEX WITH TITLE 2 CONFORMATION-SPECIFIC SYNTHETIC ANTIBODY C18, STATE MGD-1B COMPND MOL_ID: 1; COMPND 2 MOLECULE: SAB C18 LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SAB C18 HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: COBALT/MAGNESIUM TRANSPORT PROTEIN CORA; COMPND 11 CHAIN: A, B, C, D, E; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA; SOURCE 13 ORGANISM_TAXID: 2336; SOURCE 14 GENE: CORA; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG'; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 866768 KEYWDS ION CHANNEL, MAGNESIUM CHANNEL, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.K.ERRAMILLI,E.PEROZO,A.A.KOSSIAKOFF REVDAT 1 12-FEB-25 8TMP 0 JRNL AUTH S.K.ERRAMILLI,K.NOSOL,K.PIETRZAK-LICHWA,T.LI,P.DUTKA,J.HOU, JRNL AUTH 2 M.ZHAO,E.PEROZO,A.A.KOSSIAKOFF JRNL TITL STRUCTURAL BASIS FOR CORA CHANNEL GATING USING JRNL TITL 2 CONFORMATION-SPECIFIC SYNTHETIC ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : RELION, EPU, RELION, COOT, PHENIX, REMARK 3 CRYOSPARC, RELION, 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) : 3.200 REMARK 3 NUMBER OF PARTICLES : 59130 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 8TMP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-23. REMARK 100 THE DEPOSITION ID IS D_1000276016. 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 : MAGNESIUM-FREE CORA IN COMPLEX REMARK 245 WITH CONFORMATION-SPECIFIC SAB REMARK 245 C18 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 : 12478 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) : 1000.00 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) : 6000.00 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: HEPTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, A, B, C, D, 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 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 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 GLU H 1 REMARK 465 ILE H 2 REMARK 465 SER H 3 REMARK 465 ALA H 130 REMARK 465 SER H 131 REMARK 465 THR H 132 REMARK 465 LYS H 133 REMARK 465 GLY H 134 REMARK 465 PRO H 135 REMARK 465 SER H 136 REMARK 465 VAL H 137 REMARK 465 PHE H 138 REMARK 465 PRO H 139 REMARK 465 LEU H 140 REMARK 465 ALA H 141 REMARK 465 PRO H 142 REMARK 465 SER H 143 REMARK 465 SER H 144 REMARK 465 LYS H 145 REMARK 465 SER H 146 REMARK 465 THR H 147 REMARK 465 SER H 148 REMARK 465 GLY H 149 REMARK 465 GLY H 150 REMARK 465 THR H 151 REMARK 465 ALA H 152 REMARK 465 ALA H 153 REMARK 465 LEU H 154 REMARK 465 GLY H 155 REMARK 465 CYS H 156 REMARK 465 LEU H 157 REMARK 465 VAL H 158 REMARK 465 LYS H 159 REMARK 465 ASP H 160 REMARK 465 MET A -21 REMARK 465 GLY A -20 REMARK 465 SER A -19 REMARK 465 SER A -18 REMARK 465 HIS A -17 REMARK 465 HIS A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 HIS A -13 REMARK 465 HIS A -12 REMARK 465 SER A -11 REMARK 465 SER A -10 REMARK 465 GLY A -9 REMARK 465 ARG A -8 REMARK 465 GLU A -7 REMARK 465 ASN A -6 REMARK 465 LEU A -5 REMARK 465 TYR A -4 REMARK 465 PHE A -3 REMARK 465 GLN A -2 REMARK 465 GLY A -1 REMARK 465 HIS A 0 REMARK 465 MET A 1 REMARK 465 GLU A 2 REMARK 465 GLU A 3 REMARK 465 LYS A 4 REMARK 465 ARG A 5 REMARK 465 LEU A 6 REMARK 465 SER A 7 REMARK 465 ALA A 8 REMARK 465 LYS A 9 REMARK 465 LYS A 10 REMARK 465 GLY A 11 REMARK 465 LEU A 12 REMARK 465 PRO A 13 REMARK 465 PRO A 14 REMARK 465 GLY A 15 REMARK 465 LEU A 351 REMARK 465 MET B -21 REMARK 465 GLY B -20 REMARK 465 SER B -19 REMARK 465 SER B -18 REMARK 465 HIS B -17 REMARK 465 HIS B -16 REMARK 465 HIS B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 SER B -11 REMARK 465 SER B -10 REMARK 465 GLY B -9 REMARK 465 ARG B -8 REMARK 465 GLU B -7 REMARK 465 ASN B -6 REMARK 465 LEU B -5 REMARK 465 TYR B -4 REMARK 465 PHE B -3 REMARK 465 GLN B -2 REMARK 465 GLY B -1 REMARK 465 HIS B 0 REMARK 465 MET C -21 REMARK 465 GLY C -20 REMARK 465 SER C -19 REMARK 465 SER C -18 REMARK 465 HIS C -17 REMARK 465 HIS C -16 REMARK 465 HIS C -15 REMARK 465 HIS C -14 REMARK 465 HIS C -13 REMARK 465 HIS C -12 REMARK 465 SER C -11 REMARK 465 SER C -10 REMARK 465 GLY C -9 REMARK 465 ARG C -8 REMARK 465 GLU C -7 REMARK 465 ASN C -6 REMARK 465 LEU C -5 REMARK 465 TYR C -4 REMARK 465 PHE C -3 REMARK 465 GLN C -2 REMARK 465 GLY C -1 REMARK 465 HIS C 0 REMARK 465 MET C 1 REMARK 465 GLU C 2 REMARK 465 GLU C 3 REMARK 465 LYS C 4 REMARK 465 ARG C 5 REMARK 465 LEU C 6 REMARK 465 SER C 7 REMARK 465 ALA C 8 REMARK 465 LYS C 9 REMARK 465 LYS C 10 REMARK 465 GLY C 11 REMARK 465 LEU C 12 REMARK 465 PRO C 13 REMARK 465 PRO C 14 REMARK 465 GLY C 15 REMARK 465 MET D -21 REMARK 465 GLY D -20 REMARK 465 SER D -19 REMARK 465 SER D -18 REMARK 465 HIS D -17 REMARK 465 HIS D -16 REMARK 465 HIS D -15 REMARK 465 HIS D -14 REMARK 465 HIS D -13 REMARK 465 HIS D -12 REMARK 465 SER D -11 REMARK 465 SER D -10 REMARK 465 GLY D -9 REMARK 465 ARG D -8 REMARK 465 GLU D -7 REMARK 465 ASN D -6 REMARK 465 LEU D -5 REMARK 465 TYR D -4 REMARK 465 PHE D -3 REMARK 465 GLN D -2 REMARK 465 GLY D -1 REMARK 465 HIS D 0 REMARK 465 MET D 1 REMARK 465 LEU D 351 REMARK 465 MET E -21 REMARK 465 GLY E -20 REMARK 465 SER E -19 REMARK 465 SER E -18 REMARK 465 HIS E -17 REMARK 465 HIS E -16 REMARK 465 HIS E -15 REMARK 465 HIS E -14 REMARK 465 HIS E -13 REMARK 465 HIS E -12 REMARK 465 SER E -11 REMARK 465 SER E -10 REMARK 465 GLY E -9 REMARK 465 ARG E -8 REMARK 465 GLU E -7 REMARK 465 ASN E -6 REMARK 465 LEU E -5 REMARK 465 TYR E -4 REMARK 465 PHE E -3 REMARK 465 GLN E -2 REMARK 465 GLY E -1 REMARK 465 HIS E 0 REMARK 465 LEU E 351 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 O LYS C 111 OH TYR C 181 2.19 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 ALA L 33 57.90 -94.17 REMARK 500 ALA L 52 -8.02 71.55 REMARK 500 SER L 53 -36.44 -131.48 REMARK 500 GLU A 28 147.78 -170.43 REMARK 500 GLU A 244 154.14 69.10 REMARK 500 LEU B 119 -6.50 71.71 REMARK 500 ASP B 238 -53.29 167.87 REMARK 500 VAL B 239 73.63 52.59 REMARK 500 TRP B 325 28.62 49.20 REMARK 500 GLU C 25 -169.41 -127.52 REMARK 500 GLU C 48 4.29 -66.63 REMARK 500 SER C 49 38.23 -98.58 REMARK 500 SER C 56 15.20 59.44 REMARK 500 PRO C 59 131.81 -38.54 REMARK 500 HIS C 83 77.15 53.41 REMARK 500 PRO C 84 -17.24 -45.44 REMARK 500 ASN C 104 -6.60 73.27 REMARK 500 ALA C 166 -3.47 68.04 REMARK 500 LYS C 245 -7.06 73.48 REMARK 500 PHE C 315 -157.41 40.31 REMARK 500 PRO C 319 45.00 -81.65 REMARK 500 ARG C 322 -156.68 60.02 REMARK 500 TRP C 325 -173.54 57.65 REMARK 500 LYS D 10 -167.46 59.74 REMARK 500 LYS D 133 -99.62 53.84 REMARK 500 LYS D 163 30.31 -96.82 REMARK 500 VAL D 239 70.59 42.75 REMARK 500 GLU D 246 25.09 46.21 REMARK 500 ASN D 314 76.47 -100.74 REMARK 500 PRO D 319 44.67 -80.93 REMARK 500 LYS D 346 -6.27 71.00 REMARK 500 LYS D 349 -8.19 76.68 REMARK 500 GLU E 2 -173.34 61.45 REMARK 500 GLU E 3 52.68 -91.61 REMARK 500 PRO E 52 3.74 -65.42 REMARK 500 LYS E 133 -127.84 50.72 REMARK 500 ASN E 134 54.88 -97.40 REMARK 500 PHE E 345 -61.26 -90.73 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-41397 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF MAGNESIUM DEPLETED CORA IN COMPLEX WITH REMARK 900 CONFORMATION-SPECIFIC SYNTHETIC ANTIBODY C18, STATE MGD-1B DBREF 8TMP L 1 160 PDB 8TMP 8TMP 1 160 DBREF 8TMP H 1 160 PDB 8TMP 8TMP 1 160 DBREF 8TMP A 1 351 UNP Q9WZ31 CORA_THEMA 1 351 DBREF 8TMP B 1 351 UNP Q9WZ31 CORA_THEMA 1 351 DBREF 8TMP C 1 351 UNP Q9WZ31 CORA_THEMA 1 351 DBREF 8TMP D 1 351 UNP Q9WZ31 CORA_THEMA 1 351 DBREF 8TMP E 1 351 UNP Q9WZ31 CORA_THEMA 1 351 SEQADV 8TMP MET A -21 UNP Q9WZ31 INITIATING METHIONINE SEQADV 8TMP GLY A -20 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER A -19 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER A -18 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS A -17 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS A -16 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS A -15 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS A -14 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS A -13 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS A -12 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER A -11 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER A -10 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLY A -9 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP ARG A -8 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLU A -7 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP ASN A -6 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP LEU A -5 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP TYR A -4 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP PHE A -3 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLN A -2 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLY A -1 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS A 0 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP MET B -21 UNP Q9WZ31 INITIATING METHIONINE SEQADV 8TMP GLY B -20 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER B -19 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER B -18 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS B -17 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS B -16 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS B -15 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS B -14 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS B -13 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS B -12 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER B -11 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER B -10 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLY B -9 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP ARG B -8 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLU B -7 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP ASN B -6 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP LEU B -5 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP TYR B -4 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP PHE B -3 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLN B -2 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLY B -1 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS B 0 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP MET C -21 UNP Q9WZ31 INITIATING METHIONINE SEQADV 8TMP GLY C -20 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER C -19 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER C -18 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS C -17 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS C -16 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS C -15 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS C -14 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS C -13 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS C -12 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER C -11 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER C -10 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLY C -9 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP ARG C -8 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLU C -7 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP ASN C -6 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP LEU C -5 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP TYR C -4 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP PHE C -3 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLN C -2 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLY C -1 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS C 0 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP MET D -21 UNP Q9WZ31 INITIATING METHIONINE SEQADV 8TMP GLY D -20 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER D -19 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER D -18 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS D -17 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS D -16 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS D -15 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS D -14 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS D -13 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS D -12 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER D -11 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER D -10 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLY D -9 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP ARG D -8 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLU D -7 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP ASN D -6 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP LEU D -5 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP TYR D -4 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP PHE D -3 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLN D -2 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLY D -1 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS D 0 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP MET E -21 UNP Q9WZ31 INITIATING METHIONINE SEQADV 8TMP GLY E -20 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER E -19 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER E -18 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS E -17 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS E -16 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS E -15 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS E -14 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS E -13 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS E -12 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER E -11 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP SER E -10 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLY E -9 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP ARG E -8 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLU E -7 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP ASN E -6 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP LEU E -5 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP TYR E -4 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP PHE E -3 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLN E -2 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP GLY E -1 UNP Q9WZ31 EXPRESSION TAG SEQADV 8TMP HIS E 0 UNP Q9WZ31 EXPRESSION TAG SEQRES 1 L 160 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 L 160 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 L 160 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 L 160 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 L 160 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 L 160 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 160 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 160 SER SER SER SER LEU ILE THR PHE GLY GLN GLY THR LYS SEQRES 9 L 160 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 160 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 L 160 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 160 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 160 SER GLY ASN SER SEQRES 1 H 160 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 H 160 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 H 160 ALA SER GLY PHE ASN VAL SER TYR TYR SER ILE HIS TRP SEQRES 4 H 160 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 H 160 SER ILE SER SER SER SER GLY SER THR SER TYR ALA ASP SEQRES 6 H 160 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 H 160 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 H 160 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG SER TYR TRP SEQRES 9 H 160 TYR TYR ILE TRP SER TYR SER TYR GLY ASN ALA MET ASP SEQRES 10 H 160 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 11 H 160 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 12 H 160 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 13 H 160 LEU VAL LYS ASP SEQRES 1 A 373 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 373 ARG GLU ASN LEU TYR PHE GLN GLY HIS MET GLU GLU LYS SEQRES 3 A 373 ARG LEU SER ALA LYS LYS GLY LEU PRO PRO GLY THR LEU SEQRES 4 A 373 VAL TYR THR GLY LYS TYR ARG GLU ASP PHE GLU ILE GLU SEQRES 5 A 373 VAL MET ASN TYR SER ILE GLU GLU PHE ARG GLU PHE LYS SEQRES 6 A 373 THR THR ASP VAL GLU SER VAL LEU PRO PHE ARG ASP SER SEQRES 7 A 373 SER THR PRO THR TRP ILE ASN ILE THR GLY ILE HIS ARG SEQRES 8 A 373 THR ASP VAL VAL GLN ARG VAL GLY GLU PHE PHE GLY ILE SEQRES 9 A 373 HIS PRO LEU VAL LEU GLU ASP ILE LEU ASN VAL HIS GLN SEQRES 10 A 373 ARG PRO LYS VAL GLU PHE PHE GLU ASN TYR VAL PHE ILE SEQRES 11 A 373 VAL LEU LYS MET PHE THR TYR ASP LYS ASN LEU HIS GLU SEQRES 12 A 373 LEU GLU SER GLU GLN VAL SER LEU ILE LEU THR LYS ASN SEQRES 13 A 373 CYS VAL LEU MET PHE GLN GLU LYS ILE GLY ASP VAL PHE SEQRES 14 A 373 ASP PRO VAL ARG GLU ARG ILE ARG TYR ASN ARG GLY ILE SEQRES 15 A 373 ILE ARG LYS LYS ARG ALA ASP TYR LEU LEU TYR SER LEU SEQRES 16 A 373 ILE ASP ALA LEU VAL ASP ASP TYR PHE VAL LEU LEU GLU SEQRES 17 A 373 LYS ILE ASP ASP GLU ILE ASP VAL LEU GLU GLU GLU VAL SEQRES 18 A 373 LEU GLU ARG PRO GLU LYS GLU THR VAL GLN ARG THR HIS SEQRES 19 A 373 GLN LEU LYS ARG ASN LEU VAL GLU LEU ARG LYS THR ILE SEQRES 20 A 373 TRP PRO LEU ARG GLU VAL LEU SER SER LEU TYR ARG ASP SEQRES 21 A 373 VAL PRO PRO LEU ILE GLU LYS GLU THR VAL PRO TYR PHE SEQRES 22 A 373 ARG ASP VAL TYR ASP HIS THR ILE GLN ILE ALA ASP THR SEQRES 23 A 373 VAL GLU THR PHE ARG ASP ILE VAL SER GLY LEU LEU ASP SEQRES 24 A 373 VAL TYR LEU SER SER VAL SER ASN LYS THR ASN GLU VAL SEQRES 25 A 373 MET LYS VAL LEU THR ILE ILE ALA THR ILE PHE MET PRO SEQRES 26 A 373 LEU THR PHE ILE ALA GLY ILE TYR GLY MET ASN PHE GLU SEQRES 27 A 373 TYR MET PRO GLU LEU ARG TRP LYS TRP GLY TYR PRO VAL SEQRES 28 A 373 VAL LEU ALA VAL MET GLY VAL ILE ALA VAL ILE MET VAL SEQRES 29 A 373 VAL TYR PHE LYS LYS LYS LYS TRP LEU SEQRES 1 B 373 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 B 373 ARG GLU ASN LEU TYR PHE GLN GLY HIS MET GLU GLU LYS SEQRES 3 B 373 ARG LEU SER ALA LYS LYS GLY LEU PRO PRO GLY THR LEU SEQRES 4 B 373 VAL TYR THR GLY LYS TYR ARG GLU ASP PHE GLU ILE GLU SEQRES 5 B 373 VAL MET ASN TYR SER ILE GLU GLU PHE ARG GLU PHE LYS SEQRES 6 B 373 THR THR ASP VAL GLU SER VAL LEU PRO PHE ARG ASP SER SEQRES 7 B 373 SER THR PRO THR TRP ILE ASN ILE THR GLY ILE HIS ARG SEQRES 8 B 373 THR ASP VAL VAL GLN ARG VAL GLY GLU PHE PHE GLY ILE SEQRES 9 B 373 HIS PRO LEU VAL LEU GLU ASP ILE LEU ASN VAL HIS GLN SEQRES 10 B 373 ARG PRO LYS VAL GLU PHE PHE GLU ASN TYR VAL PHE ILE SEQRES 11 B 373 VAL LEU LYS MET PHE THR TYR ASP LYS ASN LEU HIS GLU SEQRES 12 B 373 LEU GLU SER GLU GLN VAL SER LEU ILE LEU THR LYS ASN SEQRES 13 B 373 CYS VAL LEU MET PHE GLN GLU LYS ILE GLY ASP VAL PHE SEQRES 14 B 373 ASP PRO VAL ARG GLU ARG ILE ARG TYR ASN ARG GLY ILE SEQRES 15 B 373 ILE ARG LYS LYS ARG ALA ASP TYR LEU LEU TYR SER LEU SEQRES 16 B 373 ILE ASP ALA LEU VAL ASP ASP TYR PHE VAL LEU LEU GLU SEQRES 17 B 373 LYS ILE ASP ASP GLU ILE ASP VAL LEU GLU GLU GLU VAL SEQRES 18 B 373 LEU GLU ARG PRO GLU LYS GLU THR VAL GLN ARG THR HIS SEQRES 19 B 373 GLN LEU LYS ARG ASN LEU VAL GLU LEU ARG LYS THR ILE SEQRES 20 B 373 TRP PRO LEU ARG GLU VAL LEU SER SER LEU TYR ARG ASP SEQRES 21 B 373 VAL PRO PRO LEU ILE GLU LYS GLU THR VAL PRO TYR PHE SEQRES 22 B 373 ARG ASP VAL TYR ASP HIS THR ILE GLN ILE ALA ASP THR SEQRES 23 B 373 VAL GLU THR PHE ARG ASP ILE VAL SER GLY LEU LEU ASP SEQRES 24 B 373 VAL TYR LEU SER SER VAL SER ASN LYS THR ASN GLU VAL SEQRES 25 B 373 MET LYS VAL LEU THR ILE ILE ALA THR ILE PHE MET PRO SEQRES 26 B 373 LEU THR PHE ILE ALA GLY ILE TYR GLY MET ASN PHE GLU SEQRES 27 B 373 TYR MET PRO GLU LEU ARG TRP LYS TRP GLY TYR PRO VAL SEQRES 28 B 373 VAL LEU ALA VAL MET GLY VAL ILE ALA VAL ILE MET VAL SEQRES 29 B 373 VAL TYR PHE LYS LYS LYS LYS TRP LEU SEQRES 1 C 373 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 C 373 ARG GLU ASN LEU TYR PHE GLN GLY HIS MET GLU GLU LYS SEQRES 3 C 373 ARG LEU SER ALA LYS LYS GLY LEU PRO PRO GLY THR LEU SEQRES 4 C 373 VAL TYR THR GLY LYS TYR ARG GLU ASP PHE GLU ILE GLU SEQRES 5 C 373 VAL MET ASN TYR SER ILE GLU GLU PHE ARG GLU PHE LYS SEQRES 6 C 373 THR THR ASP VAL GLU SER VAL LEU PRO PHE ARG ASP SER SEQRES 7 C 373 SER THR PRO THR TRP ILE ASN ILE THR GLY ILE HIS ARG SEQRES 8 C 373 THR ASP VAL VAL GLN ARG VAL GLY GLU PHE PHE GLY ILE SEQRES 9 C 373 HIS PRO LEU VAL LEU GLU ASP ILE LEU ASN VAL HIS GLN SEQRES 10 C 373 ARG PRO LYS VAL GLU PHE PHE GLU ASN TYR VAL PHE ILE SEQRES 11 C 373 VAL LEU LYS MET PHE THR TYR ASP LYS ASN LEU HIS GLU SEQRES 12 C 373 LEU GLU SER GLU GLN VAL SER LEU ILE LEU THR LYS ASN SEQRES 13 C 373 CYS VAL LEU MET PHE GLN GLU LYS ILE GLY ASP VAL PHE SEQRES 14 C 373 ASP PRO VAL ARG GLU ARG ILE ARG TYR ASN ARG GLY ILE SEQRES 15 C 373 ILE ARG LYS LYS ARG ALA ASP TYR LEU LEU TYR SER LEU SEQRES 16 C 373 ILE ASP ALA LEU VAL ASP ASP TYR PHE VAL LEU LEU GLU SEQRES 17 C 373 LYS ILE ASP ASP GLU ILE ASP VAL LEU GLU GLU GLU VAL SEQRES 18 C 373 LEU GLU ARG PRO GLU LYS GLU THR VAL GLN ARG THR HIS SEQRES 19 C 373 GLN LEU LYS ARG ASN LEU VAL GLU LEU ARG LYS THR ILE SEQRES 20 C 373 TRP PRO LEU ARG GLU VAL LEU SER SER LEU TYR ARG ASP SEQRES 21 C 373 VAL PRO PRO LEU ILE GLU LYS GLU THR VAL PRO TYR PHE SEQRES 22 C 373 ARG ASP VAL TYR ASP HIS THR ILE GLN ILE ALA ASP THR SEQRES 23 C 373 VAL GLU THR PHE ARG ASP ILE VAL SER GLY LEU LEU ASP SEQRES 24 C 373 VAL TYR LEU SER SER VAL SER ASN LYS THR ASN GLU VAL SEQRES 25 C 373 MET LYS VAL LEU THR ILE ILE ALA THR ILE PHE MET PRO SEQRES 26 C 373 LEU THR PHE ILE ALA GLY ILE TYR GLY MET ASN PHE GLU SEQRES 27 C 373 TYR MET PRO GLU LEU ARG TRP LYS TRP GLY TYR PRO VAL SEQRES 28 C 373 VAL LEU ALA VAL MET GLY VAL ILE ALA VAL ILE MET VAL SEQRES 29 C 373 VAL TYR PHE LYS LYS LYS LYS TRP LEU SEQRES 1 D 373 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 D 373 ARG GLU ASN LEU TYR PHE GLN GLY HIS MET GLU GLU LYS SEQRES 3 D 373 ARG LEU SER ALA LYS LYS GLY LEU PRO PRO GLY THR LEU SEQRES 4 D 373 VAL TYR THR GLY LYS TYR ARG GLU ASP PHE GLU ILE GLU SEQRES 5 D 373 VAL MET ASN TYR SER ILE GLU GLU PHE ARG GLU PHE LYS SEQRES 6 D 373 THR THR ASP VAL GLU SER VAL LEU PRO PHE ARG ASP SER SEQRES 7 D 373 SER THR PRO THR TRP ILE ASN ILE THR GLY ILE HIS ARG SEQRES 8 D 373 THR ASP VAL VAL GLN ARG VAL GLY GLU PHE PHE GLY ILE SEQRES 9 D 373 HIS PRO LEU VAL LEU GLU ASP ILE LEU ASN VAL HIS GLN SEQRES 10 D 373 ARG PRO LYS VAL GLU PHE PHE GLU ASN TYR VAL PHE ILE SEQRES 11 D 373 VAL LEU LYS MET PHE THR TYR ASP LYS ASN LEU HIS GLU SEQRES 12 D 373 LEU GLU SER GLU GLN VAL SER LEU ILE LEU THR LYS ASN SEQRES 13 D 373 CYS VAL LEU MET PHE GLN GLU LYS ILE GLY ASP VAL PHE SEQRES 14 D 373 ASP PRO VAL ARG GLU ARG ILE ARG TYR ASN ARG GLY ILE SEQRES 15 D 373 ILE ARG LYS LYS ARG ALA ASP TYR LEU LEU TYR SER LEU SEQRES 16 D 373 ILE ASP ALA LEU VAL ASP ASP TYR PHE VAL LEU LEU GLU SEQRES 17 D 373 LYS ILE ASP ASP GLU ILE ASP VAL LEU GLU GLU GLU VAL SEQRES 18 D 373 LEU GLU ARG PRO GLU LYS GLU THR VAL GLN ARG THR HIS SEQRES 19 D 373 GLN LEU LYS ARG ASN LEU VAL GLU LEU ARG LYS THR ILE SEQRES 20 D 373 TRP PRO LEU ARG GLU VAL LEU SER SER LEU TYR ARG ASP SEQRES 21 D 373 VAL PRO PRO LEU ILE GLU LYS GLU THR VAL PRO TYR PHE SEQRES 22 D 373 ARG ASP VAL TYR ASP HIS THR ILE GLN ILE ALA ASP THR SEQRES 23 D 373 VAL GLU THR PHE ARG ASP ILE VAL SER GLY LEU LEU ASP SEQRES 24 D 373 VAL TYR LEU SER SER VAL SER ASN LYS THR ASN GLU VAL SEQRES 25 D 373 MET LYS VAL LEU THR ILE ILE ALA THR ILE PHE MET PRO SEQRES 26 D 373 LEU THR PHE ILE ALA GLY ILE TYR GLY MET ASN PHE GLU SEQRES 27 D 373 TYR MET PRO GLU LEU ARG TRP LYS TRP GLY TYR PRO VAL SEQRES 28 D 373 VAL LEU ALA VAL MET GLY VAL ILE ALA VAL ILE MET VAL SEQRES 29 D 373 VAL TYR PHE LYS LYS LYS LYS TRP LEU SEQRES 1 E 373 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 E 373 ARG GLU ASN LEU TYR PHE GLN GLY HIS MET GLU GLU LYS SEQRES 3 E 373 ARG LEU SER ALA LYS LYS GLY LEU PRO PRO GLY THR LEU SEQRES 4 E 373 VAL TYR THR GLY LYS TYR ARG GLU ASP PHE GLU ILE GLU SEQRES 5 E 373 VAL MET ASN TYR SER ILE GLU GLU PHE ARG GLU PHE LYS SEQRES 6 E 373 THR THR ASP VAL GLU SER VAL LEU PRO PHE ARG ASP SER SEQRES 7 E 373 SER THR PRO THR TRP ILE ASN ILE THR GLY ILE HIS ARG SEQRES 8 E 373 THR ASP VAL VAL GLN ARG VAL GLY GLU PHE PHE GLY ILE SEQRES 9 E 373 HIS PRO LEU VAL LEU GLU ASP ILE LEU ASN VAL HIS GLN SEQRES 10 E 373 ARG PRO LYS VAL GLU PHE PHE GLU ASN TYR VAL PHE ILE SEQRES 11 E 373 VAL LEU LYS MET PHE THR TYR ASP LYS ASN LEU HIS GLU SEQRES 12 E 373 LEU GLU SER GLU GLN VAL SER LEU ILE LEU THR LYS ASN SEQRES 13 E 373 CYS VAL LEU MET PHE GLN GLU LYS ILE GLY ASP VAL PHE SEQRES 14 E 373 ASP PRO VAL ARG GLU ARG ILE ARG TYR ASN ARG GLY ILE SEQRES 15 E 373 ILE ARG LYS LYS ARG ALA ASP TYR LEU LEU TYR SER LEU SEQRES 16 E 373 ILE ASP ALA LEU VAL ASP ASP TYR PHE VAL LEU LEU GLU SEQRES 17 E 373 LYS ILE ASP ASP GLU ILE ASP VAL LEU GLU GLU GLU VAL SEQRES 18 E 373 LEU GLU ARG PRO GLU LYS GLU THR VAL GLN ARG THR HIS SEQRES 19 E 373 GLN LEU LYS ARG ASN LEU VAL GLU LEU ARG LYS THR ILE SEQRES 20 E 373 TRP PRO LEU ARG GLU VAL LEU SER SER LEU TYR ARG ASP SEQRES 21 E 373 VAL PRO PRO LEU ILE GLU LYS GLU THR VAL PRO TYR PHE SEQRES 22 E 373 ARG ASP VAL TYR ASP HIS THR ILE GLN ILE ALA ASP THR SEQRES 23 E 373 VAL GLU THR PHE ARG ASP ILE VAL SER GLY LEU LEU ASP SEQRES 24 E 373 VAL TYR LEU SER SER VAL SER ASN LYS THR ASN GLU VAL SEQRES 25 E 373 MET LYS VAL LEU THR ILE ILE ALA THR ILE PHE MET PRO SEQRES 26 E 373 LEU THR PHE ILE ALA GLY ILE TYR GLY MET ASN PHE GLU SEQRES 27 E 373 TYR MET PRO GLU LEU ARG TRP LYS TRP GLY TYR PRO VAL SEQRES 28 E 373 VAL LEU ALA VAL MET GLY VAL ILE ALA VAL ILE MET VAL SEQRES 29 E 373 VAL TYR PHE LYS LYS LYS LYS TRP LEU HET MG A 401 1 HET MG D 401 1 HETNAM MG MAGNESIUM ION FORMUL 8 MG 2(MG 2+) HELIX 1 AA1 ASN H 31 TYR H 34 5 4 HELIX 2 AA2 ASP A 46 LEU A 51 1 6 HELIX 3 AA3 PRO A 52 SER A 56 5 5 HELIX 4 AA4 ARG A 69 GLY A 81 1 13 HELIX 5 AA5 HIS A 83 ASN A 92 1 10 HELIX 6 AA6 PHE A 147 ASN A 157 1 11 HELIX 7 AA7 ARG A 165 ARG A 202 1 38 HELIX 8 AA8 GLU A 204 ARG A 237 1 34 HELIX 9 AA9 GLU A 244 GLU A 246 5 3 HELIX 10 AB1 THR A 247 SER A 281 1 35 HELIX 11 AB2 VAL A 283 THR A 299 1 17 HELIX 12 AB3 PHE A 301 GLY A 312 1 12 HELIX 13 AB4 TRP A 325 LYS A 348 1 24 HELIX 14 AB5 ASP B 46 ARG B 54 5 9 HELIX 15 AB6 ARG B 69 PHE B 80 1 12 HELIX 16 AB7 HIS B 83 ASN B 92 1 10 HELIX 17 AB8 LYS B 117 HIS B 120 5 4 HELIX 18 AB9 PHE B 147 ASN B 157 1 11 HELIX 19 AC1 ILE B 160 LYS B 164 5 5 HELIX 20 AC2 ARG B 165 ARG B 202 1 38 HELIX 21 AC3 GLU B 204 ARG B 237 1 34 HELIX 22 AC4 THR B 247 TYR B 311 1 65 HELIX 23 AC5 GLY B 326 LYS B 348 1 23 HELIX 24 AC6 ARG C 69 PHE C 80 1 12 HELIX 25 AC7 HIS C 83 LEU C 85 5 3 HELIX 26 AC8 VAL C 86 ASN C 92 1 7 HELIX 27 AC9 PHE C 147 TYR C 156 1 10 HELIX 28 AD1 ILE C 160 LYS C 164 5 5 HELIX 29 AD2 ALA C 166 ARG C 202 1 37 HELIX 30 AD3 GLU C 206 ASP C 238 1 33 HELIX 31 AD4 THR C 247 TYR C 311 1 65 HELIX 32 AD5 GLY C 326 LYS C 349 1 24 HELIX 33 AD6 VAL D 47 ARG D 54 5 8 HELIX 34 AD7 ARG D 69 PHE D 80 1 12 HELIX 35 AD8 HIS D 83 ASN D 92 1 10 HELIX 36 AD9 PHE D 147 ASN D 157 1 11 HELIX 37 AE1 ARG D 165 ARG D 202 1 38 HELIX 38 AE2 GLU D 204 VAL D 239 1 36 HELIX 39 AE3 THR D 247 GLY D 312 1 66 HELIX 40 AE4 TRP D 325 PHE D 345 1 21 HELIX 41 AE5 ASP E 46 SER E 56 5 11 HELIX 42 AE6 ARG E 69 GLY E 81 1 13 HELIX 43 AE7 HIS E 83 ASN E 92 1 10 HELIX 44 AE8 PHE E 147 TYR E 156 1 10 HELIX 45 AE9 ARG E 165 ARG E 202 1 38 HELIX 46 AF1 GLU E 204 ARG E 237 1 34 HELIX 47 AF2 THR E 247 MET E 313 1 67 HELIX 48 AF3 TRP E 325 LYS E 346 1 22 SHEET 1 AA1 4 MET L 5 SER L 8 0 SHEET 2 AA1 4 VAL L 20 ALA L 26 -1 O THR L 23 N SER L 8 SHEET 3 AA1 4 ASP L 71 ILE L 76 -1 O PHE L 72 N CYS L 24 SHEET 4 AA1 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AA2 6 SER L 11 SER L 13 0 SHEET 2 AA2 6 THR L 103 GLU L 106 1 O GLU L 106 N LEU L 12 SHEET 3 AA2 6 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA2 6 VAL L 34 GLN L 39 -1 N GLN L 39 O THR L 86 SHEET 5 AA2 6 LYS L 46 TYR L 50 -1 O LYS L 46 N GLN L 38 SHEET 6 AA2 6 SER L 54 LEU L 55 -1 O SER L 54 N TYR L 50 SHEET 1 AA3 4 SER L 11 SER L 13 0 SHEET 2 AA3 4 THR L 103 GLU L 106 1 O GLU L 106 N LEU L 12 SHEET 3 AA3 4 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA3 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AA4 4 GLN H 6 SER H 10 0 SHEET 2 AA4 4 LEU H 21 SER H 28 -1 O SER H 28 N GLN H 6 SHEET 3 AA4 4 THR H 81 MET H 86 -1 O LEU H 84 N LEU H 23 SHEET 4 AA4 4 PHE H 71 ASP H 76 -1 N THR H 72 O GLN H 85 SHEET 1 AA5 6 LEU H 14 VAL H 15 0 SHEET 2 AA5 6 THR H 123 VAL H 127 1 O THR H 126 N VAL H 15 SHEET 3 AA5 6 ALA H 95 TYR H 106 -1 N ALA H 95 O VAL H 125 SHEET 4 AA5 6 SER H 36 GLN H 42 -1 N VAL H 40 O TYR H 98 SHEET 5 AA5 6 LEU H 48 SER H 55 -1 O GLU H 49 N ARG H 41 SHEET 6 AA5 6 SER H 60 TYR H 63 -1 O SER H 62 N SER H 53 SHEET 1 AA6 4 LEU H 14 VAL H 15 0 SHEET 2 AA6 4 THR H 123 VAL H 127 1 O THR H 126 N VAL H 15 SHEET 3 AA6 4 ALA H 95 TYR H 106 -1 N ALA H 95 O VAL H 125 SHEET 4 AA6 4 TYR H 112 TRP H 119 -1 O GLY H 113 N TYR H 105 SHEET 1 AA7 7 PHE A 39 THR A 44 0 SHEET 2 AA7 7 ILE A 29 TYR A 34 -1 N ASN A 33 O ARG A 40 SHEET 3 AA7 7 THR A 60 ILE A 64 -1 O ASN A 63 N GLU A 30 SHEET 4 AA7 7 CYS A 135 PHE A 139 1 O MET A 138 N ILE A 64 SHEET 5 AA7 7 GLU A 121 THR A 132 -1 N ILE A 130 O LEU A 137 SHEET 6 AA7 7 VAL A 106 ASP A 116 -1 N LEU A 110 O VAL A 127 SHEET 7 AA7 7 LYS A 98 PHE A 101 -1 N GLU A 100 O PHE A 107 SHEET 1 AA8 7 PHE B 39 THR B 44 0 SHEET 2 AA8 7 GLU B 28 TYR B 34 -1 N ILE B 29 O THR B 44 SHEET 3 AA8 7 THR B 60 THR B 65 -1 O ASN B 63 N GLU B 30 SHEET 4 AA8 7 CYS B 135 PHE B 139 1 O MET B 138 N ILE B 62 SHEET 5 AA8 7 GLU B 121 LEU B 131 -1 N ILE B 130 O LEU B 137 SHEET 6 AA8 7 VAL B 106 ASP B 116 -1 N MET B 112 O GLU B 125 SHEET 7 AA8 7 LYS B 98 PHE B 101 -1 N LYS B 98 O VAL B 109 SHEET 1 AA9 7 PHE C 39 THR C 44 0 SHEET 2 AA9 7 GLU C 28 TYR C 34 -1 N ILE C 29 O THR C 44 SHEET 3 AA9 7 THR C 60 THR C 65 -1 O TRP C 61 N MET C 32 SHEET 4 AA9 7 CYS C 135 GLN C 140 1 O MET C 138 N ILE C 64 SHEET 5 AA9 7 LEU C 122 THR C 132 -1 N SER C 128 O PHE C 139 SHEET 6 AA9 7 TYR C 105 TYR C 115 -1 N LEU C 110 O VAL C 127 SHEET 7 AA9 7 LYS C 98 VAL C 99 -1 N LYS C 98 O VAL C 109 SHEET 1 AB1 7 PHE D 42 THR D 44 0 SHEET 2 AB1 7 GLU D 28 VAL D 31 -1 N VAL D 31 O PHE D 42 SHEET 3 AB1 7 THR D 60 THR D 65 -1 O ASN D 63 N GLU D 30 SHEET 4 AB1 7 CYS D 135 PHE D 139 1 O VAL D 136 N THR D 60 SHEET 5 AB1 7 GLU D 121 THR D 132 -1 N THR D 132 O CYS D 135 SHEET 6 AB1 7 TYR D 105 ASP D 116 -1 N ILE D 108 O LEU D 129 SHEET 7 AB1 7 VAL D 99 PHE D 101 -1 N GLU D 100 O PHE D 107 SHEET 1 AB2 7 PHE E 39 THR E 44 0 SHEET 2 AB2 7 GLU E 28 TYR E 34 -1 N VAL E 31 O PHE E 42 SHEET 3 AB2 7 THR E 60 THR E 65 -1 O ASN E 63 N GLU E 30 SHEET 4 AB2 7 CYS E 135 GLN E 140 1 O MET E 138 N ILE E 62 SHEET 5 AB2 7 LEU E 122 THR E 132 -1 N ILE E 130 O LEU E 137 SHEET 6 AB2 7 TYR E 105 TYR E 115 -1 N LEU E 110 O VAL E 127 SHEET 7 AB2 7 LYS E 98 PHE E 101 -1 N LYS E 98 O VAL E 109 SSBOND 1 CYS L 24 CYS L 89 1555 1555 2.04 SSBOND 2 CYS H 25 CYS H 99 1555 1555 2.03 LINK OD2 ASP D 175 MG MG D 401 1555 1555 2.96 CISPEP 1 SER L 8 PRO L 9 0 -2.54 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