HEADER MEMBRANE PROTEIN 19-DEC-23 8XIQ TITLE STRUCTURE OF L796778-SSTR3 G PROTEIN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: SOMATOSTATIN RECEPTOR TYPE 3; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SS-3-R,SS3-R,SS3R,SST3,SSR-28; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: G-ALPHA I; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 12 BETA-1; COMPND 13 CHAIN: C; COMPND 14 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: NANOBODY NB35; COMPND 18 CHAIN: D; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 22 GAMMA-2; COMPND 23 CHAIN: G; COMPND 24 SYNONYM: G GAMMA-I; COMPND 25 ENGINEERED: YES; COMPND 26 MOL_ID: 6; COMPND 27 MOLECULE: NIT-FC0-NLE-A1D5B; COMPND 28 CHAIN: F; COMPND 29 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: SSTR3; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111; 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: TRICHOPLUSIA NI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 GENE: GNB1; SOURCE 19 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 23 ORGANISM_TAXID: 9844; SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 26 MOL_ID: 5; SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 28 ORGANISM_COMMON: HUMAN; SOURCE 29 ORGANISM_TAXID: 9606; SOURCE 30 GENE: GNG2; SOURCE 31 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 33 MOL_ID: 6; SOURCE 34 SYNTHETIC: YES; SOURCE 35 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 36 ORGANISM_TAXID: 32630 KEYWDS GPCR, SSTR3, L796778, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Y.WANG,Y.XU,H.E.XU,Y.ZHUANG JRNL AUTH Y.WANG,Y.XU,X.HE,W.FAN,K.WU,W.HU,X.CHENG,S.SUN,H.E.XU, JRNL AUTH 2 Y.ZHUANG JRNL TITL SELECTIVE LIGAND RECOGNITION AND ACTIVATION OF SOMATOSTATIN JRNL TITL 2 RECEPTORS SSTR1 AND SSTR3 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.71 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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) : 2.710 REMARK 3 NUMBER OF PARTICLES : 425379 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8XIQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC. REMARK 100 THE DEPOSITION ID IS D_1300043583. 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 : STRUCTURE OF L796778-SSTR3 G REMARK 245 PROTEIN COMPLEX 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 : FEI TITAN REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 5000.00 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) : 50.00 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, G, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ASP A 2 REMARK 465 MET A 3 REMARK 465 LEU A 4 REMARK 465 HIS A 5 REMARK 465 PRO A 6 REMARK 465 SER A 7 REMARK 465 SER A 8 REMARK 465 VAL A 9 REMARK 465 SER A 10 REMARK 465 THR A 11 REMARK 465 THR A 12 REMARK 465 SER A 13 REMARK 465 GLU A 14 REMARK 465 PRO A 15 REMARK 465 GLU A 16 REMARK 465 ASN A 17 REMARK 465 ALA A 18 REMARK 465 SER A 19 REMARK 465 SER A 20 REMARK 465 ALA A 21 REMARK 465 TRP A 22 REMARK 465 PRO A 23 REMARK 465 PRO A 24 REMARK 465 ASP A 25 REMARK 465 ALA A 26 REMARK 465 THR A 27 REMARK 465 LEU A 28 REMARK 465 GLY A 29 REMARK 465 ASN A 30 REMARK 465 VAL A 31 REMARK 465 SER A 32 REMARK 465 ALA A 33 REMARK 465 GLY A 34 REMARK 465 PRO A 35 REMARK 465 SER A 36 REMARK 465 PRO A 37 REMARK 465 ALA A 38 REMARK 465 GLY A 39 REMARK 465 LEU A 329 REMARK 465 ARG A 330 REMARK 465 PRO A 331 REMARK 465 SER A 332 REMARK 465 ARG A 333 REMARK 465 ARG A 334 REMARK 465 VAL A 335 REMARK 465 ARG A 336 REMARK 465 SER A 337 REMARK 465 GLN A 338 REMARK 465 GLU A 339 REMARK 465 PRO A 340 REMARK 465 THR A 341 REMARK 465 VAL A 342 REMARK 465 GLY A 343 REMARK 465 PRO A 344 REMARK 465 PRO A 345 REMARK 465 GLU A 346 REMARK 465 LYS A 347 REMARK 465 THR A 348 REMARK 465 GLU A 349 REMARK 465 GLU A 350 REMARK 465 GLU A 351 REMARK 465 ASP A 352 REMARK 465 GLU A 353 REMARK 465 GLU A 354 REMARK 465 GLU A 355 REMARK 465 GLU A 356 REMARK 465 ASP A 357 REMARK 465 GLY A 358 REMARK 465 GLU A 359 REMARK 465 GLU A 360 REMARK 465 SER A 361 REMARK 465 ARG A 362 REMARK 465 GLU A 363 REMARK 465 GLY A 364 REMARK 465 GLY A 365 REMARK 465 LYS A 366 REMARK 465 GLY A 367 REMARK 465 LYS A 368 REMARK 465 GLU A 369 REMARK 465 MET B 1 REMARK 465 GLY B 2 REMARK 465 CYS B 3 REMARK 465 TYR B 56 REMARK 465 HIS B 57 REMARK 465 VAL B 58 REMARK 465 ASN B 59 REMARK 465 GLY B 60 REMARK 465 TYR B 61 REMARK 465 SER B 62 REMARK 465 GLU B 63 REMARK 465 GLU B 64 REMARK 465 GLU B 65 REMARK 465 CYS B 66 REMARK 465 LYS B 67 REMARK 465 GLN B 68 REMARK 465 TYR B 69 REMARK 465 LYS B 70 REMARK 465 ALA B 71 REMARK 465 VAL B 72 REMARK 465 VAL B 73 REMARK 465 TYR B 74 REMARK 465 SER B 75 REMARK 465 ASN B 76 REMARK 465 THR B 77 REMARK 465 ILE B 78 REMARK 465 GLN B 79 REMARK 465 SER B 80 REMARK 465 ILE B 81 REMARK 465 ILE B 82 REMARK 465 ALA B 83 REMARK 465 ILE B 84 REMARK 465 ILE B 85 REMARK 465 ARG B 86 REMARK 465 ALA B 87 REMARK 465 MET B 88 REMARK 465 GLY B 89 REMARK 465 ARG B 90 REMARK 465 LEU B 91 REMARK 465 LYS B 92 REMARK 465 ILE B 93 REMARK 465 ASP B 94 REMARK 465 PHE B 95 REMARK 465 GLY B 96 REMARK 465 ASP B 97 REMARK 465 SER B 98 REMARK 465 ALA B 99 REMARK 465 ARG B 100 REMARK 465 ALA B 101 REMARK 465 ASP B 102 REMARK 465 ASP B 103 REMARK 465 ALA B 104 REMARK 465 ARG B 105 REMARK 465 GLN B 106 REMARK 465 LEU B 107 REMARK 465 PHE B 108 REMARK 465 VAL B 109 REMARK 465 LEU B 110 REMARK 465 ALA B 111 REMARK 465 GLY B 112 REMARK 465 ALA B 113 REMARK 465 ALA B 114 REMARK 465 GLU B 115 REMARK 465 GLU B 116 REMARK 465 GLY B 117 REMARK 465 PHE B 118 REMARK 465 MET B 119 REMARK 465 THR B 120 REMARK 465 ALA B 121 REMARK 465 GLU B 122 REMARK 465 LEU B 123 REMARK 465 ALA B 124 REMARK 465 GLY B 125 REMARK 465 VAL B 126 REMARK 465 ILE B 127 REMARK 465 LYS B 128 REMARK 465 ARG B 129 REMARK 465 LEU B 130 REMARK 465 TRP B 131 REMARK 465 LYS B 132 REMARK 465 ASP B 133 REMARK 465 SER B 134 REMARK 465 GLY B 135 REMARK 465 VAL B 136 REMARK 465 GLN B 137 REMARK 465 ALA B 138 REMARK 465 CYS B 139 REMARK 465 PHE B 140 REMARK 465 ASN B 141 REMARK 465 ARG B 142 REMARK 465 SER B 143 REMARK 465 ARG B 144 REMARK 465 GLU B 145 REMARK 465 TYR B 146 REMARK 465 GLN B 147 REMARK 465 LEU B 148 REMARK 465 ASN B 149 REMARK 465 ASP B 150 REMARK 465 SER B 151 REMARK 465 ALA B 152 REMARK 465 ALA B 153 REMARK 465 TYR B 154 REMARK 465 TYR B 155 REMARK 465 LEU B 156 REMARK 465 ASN B 157 REMARK 465 ASP B 158 REMARK 465 LEU B 159 REMARK 465 ASP B 160 REMARK 465 ARG B 161 REMARK 465 ILE B 162 REMARK 465 ALA B 163 REMARK 465 GLN B 164 REMARK 465 PRO B 165 REMARK 465 ASN B 166 REMARK 465 TYR B 167 REMARK 465 ILE B 168 REMARK 465 PRO B 169 REMARK 465 THR B 170 REMARK 465 GLN B 171 REMARK 465 GLN B 172 REMARK 465 ASP B 173 REMARK 465 VAL B 174 REMARK 465 LEU B 175 REMARK 465 ARG B 176 REMARK 465 THR B 177 REMARK 465 MET C 3 REMARK 465 LEU C 4 REMARK 465 LEU C 5 REMARK 465 GLN C 6 REMARK 465 SER C 7 REMARK 465 GLU C 8 REMARK 465 LEU C 9 REMARK 465 ASP C 10 REMARK 465 GLY C 346 REMARK 465 SER C 347 REMARK 465 SER C 348 REMARK 465 GLY C 349 REMARK 465 GLY C 350 REMARK 465 GLY C 351 REMARK 465 GLY C 352 REMARK 465 SER C 353 REMARK 465 GLY C 354 REMARK 465 GLY C 355 REMARK 465 GLY C 356 REMARK 465 GLY C 357 REMARK 465 SER C 358 REMARK 465 SER C 359 REMARK 465 GLY C 360 REMARK 465 VAL C 361 REMARK 465 SER C 362 REMARK 465 GLY C 363 REMARK 465 TRP C 364 REMARK 465 ARG C 365 REMARK 465 LEU C 366 REMARK 465 PHE C 367 REMARK 465 LYS C 368 REMARK 465 LYS C 369 REMARK 465 ILE C 370 REMARK 465 SER C 371 REMARK 465 MET D -19 REMARK 465 LYS D -18 REMARK 465 TYR D -17 REMARK 465 LEU D -16 REMARK 465 LEU D -15 REMARK 465 PRO D -14 REMARK 465 THR D -13 REMARK 465 ALA D -12 REMARK 465 ALA D -11 REMARK 465 ALA D -10 REMARK 465 GLY D -9 REMARK 465 LEU D -8 REMARK 465 LEU D -7 REMARK 465 LEU D -6 REMARK 465 LEU D -5 REMARK 465 ALA D -4 REMARK 465 ALA D -3 REMARK 465 GLN D -2 REMARK 465 PRO D -1 REMARK 465 ALA D 0 REMARK 465 MET D 1 REMARK 465 ALA D 2 REMARK 465 VAL D 128 REMARK 465 SER D 129 REMARK 465 SER D 130 REMARK 465 HIS D 131 REMARK 465 HIS D 132 REMARK 465 HIS D 133 REMARK 465 HIS D 134 REMARK 465 HIS D 135 REMARK 465 HIS D 136 REMARK 465 MET G 1 REMARK 465 ALA G 2 REMARK 465 SER G 3 REMARK 465 ASN G 4 REMARK 465 ASN G 5 REMARK 465 THR G 6 REMARK 465 ALA G 7 REMARK 465 GLU G 63 REMARK 465 LYS G 64 REMARK 465 LYS G 65 REMARK 465 PHE G 66 REMARK 465 PHE G 67 REMARK 465 CYS G 68 REMARK 465 ALA G 69 REMARK 465 ILE G 70 REMARK 465 LEU G 71 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 THR C 34 OG1 CG2 REMARK 470 SER C 36 OG REMARK 470 GLU C 135 CG CD OE1 OE2 REMARK 470 ASP C 158 CG OD1 OD2 REMARK 470 GLU C 177 CG CD OE1 OE2 REMARK 470 ARG C 202 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 220 CG CD OE1 OE2 REMARK 470 GLU G 17 CG CD OE1 OE2 REMARK 470 ASP G 26 CG OD1 OD2 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 OH TYR B 285 OD2 ASP B 310 2.08 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 SER A 189 116.43 -166.61 REMARK 500 PRO A 196 -175.63 -67.33 REMARK 500 ARG A 247 70.36 59.92 REMARK 500 LYS B 260 61.07 60.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38387 RELATED DB: EMDB REMARK 900 STRUCTURE OF L796778-SSTR3 G PROTEIN COMPLEX DBREF 8XIQ A 1 369 UNP P32745 SSR3_HUMAN 1 369 DBREF 8XIQ B 1 361 PDB 8XIQ 8XIQ 1 361 DBREF 8XIQ C 7 345 UNP P62873 GBB1_HUMAN 2 340 DBREF 8XIQ D -19 136 PDB 8XIQ 8XIQ -19 136 DBREF 8XIQ G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8XIQ F 1 4 PDB 8XIQ 8XIQ 1 4 SEQADV 8XIQ MET C 3 UNP P62873 INITIATING METHIONINE SEQADV 8XIQ LEU C 4 UNP P62873 EXPRESSION TAG SEQADV 8XIQ LEU C 5 UNP P62873 EXPRESSION TAG SEQADV 8XIQ GLN C 6 UNP P62873 EXPRESSION TAG SEQADV 8XIQ GLY C 346 UNP P62873 EXPRESSION TAG SEQADV 8XIQ SER C 347 UNP P62873 EXPRESSION TAG SEQADV 8XIQ SER C 348 UNP P62873 EXPRESSION TAG SEQADV 8XIQ GLY C 349 UNP P62873 EXPRESSION TAG SEQADV 8XIQ GLY C 350 UNP P62873 EXPRESSION TAG SEQADV 8XIQ GLY C 351 UNP P62873 EXPRESSION TAG SEQADV 8XIQ GLY C 352 UNP P62873 EXPRESSION TAG SEQADV 8XIQ SER C 353 UNP P62873 EXPRESSION TAG SEQADV 8XIQ GLY C 354 UNP P62873 EXPRESSION TAG SEQADV 8XIQ GLY C 355 UNP P62873 EXPRESSION TAG SEQADV 8XIQ GLY C 356 UNP P62873 EXPRESSION TAG SEQADV 8XIQ GLY C 357 UNP P62873 EXPRESSION TAG SEQADV 8XIQ SER C 358 UNP P62873 EXPRESSION TAG SEQADV 8XIQ SER C 359 UNP P62873 EXPRESSION TAG SEQADV 8XIQ GLY C 360 UNP P62873 EXPRESSION TAG SEQADV 8XIQ VAL C 361 UNP P62873 EXPRESSION TAG SEQADV 8XIQ SER C 362 UNP P62873 EXPRESSION TAG SEQADV 8XIQ GLY C 363 UNP P62873 EXPRESSION TAG SEQADV 8XIQ TRP C 364 UNP P62873 EXPRESSION TAG SEQADV 8XIQ ARG C 365 UNP P62873 EXPRESSION TAG SEQADV 8XIQ LEU C 366 UNP P62873 EXPRESSION TAG SEQADV 8XIQ PHE C 367 UNP P62873 EXPRESSION TAG SEQADV 8XIQ LYS C 368 UNP P62873 EXPRESSION TAG SEQADV 8XIQ LYS C 369 UNP P62873 EXPRESSION TAG SEQADV 8XIQ ILE C 370 UNP P62873 EXPRESSION TAG SEQADV 8XIQ SER C 371 UNP P62873 EXPRESSION TAG SEQRES 1 A 369 MET ASP MET LEU HIS PRO SER SER VAL SER THR THR SER SEQRES 2 A 369 GLU PRO GLU ASN ALA SER SER ALA TRP PRO PRO ASP ALA SEQRES 3 A 369 THR LEU GLY ASN VAL SER ALA GLY PRO SER PRO ALA GLY SEQRES 4 A 369 LEU ALA VAL SER GLY VAL LEU ILE PRO LEU VAL TYR LEU SEQRES 5 A 369 VAL VAL CYS VAL VAL GLY LEU LEU GLY ASN SER LEU VAL SEQRES 6 A 369 ILE TYR VAL VAL LEU ARG HIS THR ALA SER PRO SER VAL SEQRES 7 A 369 THR ASN VAL TYR ILE LEU ASN LEU ALA LEU ALA ASP GLU SEQRES 8 A 369 LEU PHE MET LEU GLY LEU PRO PHE LEU ALA ALA GLN ASN SEQRES 9 A 369 ALA LEU SER TYR TRP PRO PHE GLY SER LEU MET CYS ARG SEQRES 10 A 369 LEU VAL MET ALA VAL ASP GLY ILE ASN GLN PHE THR SER SEQRES 11 A 369 ILE PHE CYS LEU THR VAL MET SER VAL ASP ARG TYR LEU SEQRES 12 A 369 ALA VAL VAL HIS PRO THR ARG SER ALA ARG TRP ARG THR SEQRES 13 A 369 ALA PRO VAL ALA ARG THR VAL SER ALA ALA VAL TRP VAL SEQRES 14 A 369 ALA SER ALA VAL VAL VAL LEU PRO VAL VAL VAL PHE SER SEQRES 15 A 369 GLY VAL PRO ARG GLY MET SER THR CYS HIS MET GLN TRP SEQRES 16 A 369 PRO GLU PRO ALA ALA ALA TRP ARG ALA GLY PHE ILE ILE SEQRES 17 A 369 TYR THR ALA ALA LEU GLY PHE PHE GLY PRO LEU LEU VAL SEQRES 18 A 369 ILE CYS LEU CYS TYR LEU LEU ILE VAL VAL LYS VAL ARG SEQRES 19 A 369 SER ALA GLY ARG ARG VAL TRP ALA PRO SER CYS GLN ARG SEQRES 20 A 369 ARG ARG ARG SER GLU ARG ARG VAL THR ARG MET VAL VAL SEQRES 21 A 369 ALA VAL VAL ALA LEU PHE VAL LEU CYS TRP MET PRO PHE SEQRES 22 A 369 TYR VAL LEU ASN ILE VAL ASN VAL VAL CYS PRO LEU PRO SEQRES 23 A 369 GLU GLU PRO ALA PHE PHE GLY LEU TYR PHE LEU VAL VAL SEQRES 24 A 369 ALA LEU PRO TYR ALA ASN SER CYS ALA ASN PRO ILE LEU SEQRES 25 A 369 TYR GLY PHE LEU SER TYR ARG PHE LYS GLN GLY PHE ARG SEQRES 26 A 369 ARG VAL LEU LEU ARG PRO SER ARG ARG VAL ARG SER GLN SEQRES 27 A 369 GLU PRO THR VAL GLY PRO PRO GLU LYS THR GLU GLU GLU SEQRES 28 A 369 ASP GLU GLU GLU GLU ASP GLY GLU GLU SER ARG GLU GLY SEQRES 29 A 369 GLY LYS GLY LYS GLU SEQRES 1 B 361 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 B 361 GLU ARG SER LYS MET ILE GLU LYS GLN LEU GLN LYS ASP SEQRES 3 B 361 LYS GLN VAL TYR ARG ALA THR HIS ARG LEU LEU LEU LEU SEQRES 4 B 361 GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 B 361 MET ARG ILE TYR HIS VAL ASN GLY TYR SER GLU GLU GLU SEQRES 6 B 361 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 B 361 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 B 361 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 B 361 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 B 361 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 B 361 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 B 361 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 B 361 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 B 361 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR SER SEQRES 15 B 361 GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS VAL ASN SEQRES 16 B 361 PHE HIS MET PHE ASP VAL GLY ALA GLN ARG ASP GLU ARG SEQRES 17 B 361 ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR ALA ILE SEQRES 18 B 361 ILE PHE VAL VAL ASP SER SER ASP TYR ASN ARG LEU GLN SEQRES 19 B 361 GLU ALA LEU ASN ASP PHE LYS SER ILE TRP ASN ASN ARG SEQRES 20 B 361 TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS SEQRES 21 B 361 GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER SEQRES 22 B 361 LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR SEQRES 23 B 361 THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO SEQRES 24 B 361 ARG VAL THR ARG ALA LYS TYR PHE ILE ARG ASP GLU PHE SEQRES 25 B 361 LEU ARG ILE SER THR ALA SER GLY ASP GLY ARG HIS TYR SEQRES 26 B 361 CYS TYR PRO HIS PHE THR CYS SER VAL ASP THR GLU ASN SEQRES 27 B 361 ALA ARG ARG ILE PHE ASN ASP VAL THR ASP ILE ILE ILE SEQRES 28 B 361 LYS MET ASN LEU ARG ASP CYS GLY LEU PHE SEQRES 1 C 369 MET LEU LEU GLN SER GLU LEU ASP GLN LEU ARG GLN GLU SEQRES 2 C 369 ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA ARG LYS SEQRES 3 C 369 ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR ASN ASN SEQRES 4 C 369 ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR ARG ARG SEQRES 5 C 369 THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA MET HIS SEQRES 6 C 369 TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SER GLN SEQRES 7 C 369 ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR THR ASN SEQRES 8 C 369 LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP VAL MET SEQRES 9 C 369 THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL ALA CYS SEQRES 10 C 369 GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN LEU LYS SEQRES 11 C 369 THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU LEU ALA SEQRES 12 C 369 GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE LEU ASP SEQRES 13 C 369 ASP ASN GLN ILE VAL THR SER SER GLY ASP THR THR CYS SEQRES 14 C 369 ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR THR THR SEQRES 15 C 369 PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SER LEU SEQRES 16 C 369 ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA CYS ASP SEQRES 17 C 369 ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY MET CYS SEQRES 18 C 369 ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE ASN ALA SEQRES 19 C 369 ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA THR GLY SEQRES 20 C 369 SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU ARG ALA SEQRES 21 C 369 ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN ILE ILE SEQRES 22 C 369 CYS GLY ILE THR SER VAL SER PHE SER LYS SER GLY ARG SEQRES 23 C 369 LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS ASN VAL SEQRES 24 C 369 TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL LEU ALA SEQRES 25 C 369 GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL THR ASP SEQRES 26 C 369 ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SER PHE SEQRES 27 C 369 LEU LYS ILE TRP ASN GLY SER SER GLY GLY GLY GLY SER SEQRES 28 C 369 GLY GLY GLY GLY SER SER GLY VAL SER GLY TRP ARG LEU SEQRES 29 C 369 PHE LYS LYS ILE SER SEQRES 1 D 156 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 D 156 LEU LEU ALA ALA GLN PRO ALA MET ALA GLN VAL GLN LEU SEQRES 3 D 156 GLN GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER SEQRES 4 D 156 LEU ARG LEU SER CYS ALA ALA SER GLY PHE THR PHE SER SEQRES 5 D 156 ASN TYR LYS MET ASN TRP VAL ARG GLN ALA PRO GLY LYS SEQRES 6 D 156 GLY LEU GLU TRP VAL SER ASP ILE SER GLN SER GLY ALA SEQRES 7 D 156 SER ILE SER TYR THR GLY SER VAL LYS GLY ARG PHE THR SEQRES 8 D 156 ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU GLN SEQRES 9 D 156 MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR TYR SEQRES 10 D 156 CYS ALA ARG CYS PRO ALA PRO PHE THR ARG ASP CYS PHE SEQRES 11 D 156 ASP VAL THR SER THR THR TYR ALA TYR ARG GLY GLN GLY SEQRES 12 D 156 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 G 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 G 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 G 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 G 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 G 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 G 71 PHE PHE CYS ALA ILE LEU SEQRES 1 F 4 NIT FC0 NLE D5B HET NIT F 1 15 HET FC0 F 2 22 HET NLE F 3 19 HET D5B F 4 26 HETNAM NIT 4-NITROANILINE HETNAM FC0 N-CARBOXY-L-PHENYLALANINE HETNAM NLE NORLEUCINE HETSYN NIT PARANITROANILINE FORMUL 6 NIT C6 H6 N2 O2 FORMUL 6 FC0 C10 H11 N O4 FORMUL 6 NLE C6 H13 N O2 FORMUL 6 D5B FORMUL 7 HOH *11(H2 O) HELIX 1 AA1 VAL A 42 ARG A 71 1 30 HELIX 2 AA2 SER A 77 LEU A 95 1 19 HELIX 3 AA3 GLY A 96 LEU A 106 1 11 HELIX 4 AA4 GLY A 112 HIS A 147 1 36 HELIX 5 AA5 HIS A 147 ALA A 152 1 6 HELIX 6 AA6 THR A 156 SER A 182 1 27 HELIX 7 AA7 PRO A 198 TRP A 241 1 44 HELIX 8 AA8 ALA A 242 GLN A 246 5 5 HELIX 9 AA9 ARG A 247 CYS A 283 1 37 HELIX 10 AB1 GLU A 288 TYR A 313 1 26 HELIX 11 AB2 SER A 317 PHE A 324 1 8 HELIX 12 AB3 ARG A 325 VAL A 327 5 3 HELIX 13 AB4 SER B 6 ALA B 32 1 27 HELIX 14 AB5 ASP B 42 SER B 44 5 3 HELIX 15 AB6 GLY B 45 LYS B 51 1 7 HELIX 16 AB7 LYS B 210 VAL B 218 5 9 HELIX 17 AB8 ASP B 229 ASN B 245 1 17 HELIX 18 AB9 LYS B 260 GLY B 271 1 12 HELIX 19 AC1 LYS B 274 TYR B 278 5 5 HELIX 20 AC2 PHE B 279 TYR B 285 5 7 HELIX 21 AC3 ASP B 298 ALA B 318 1 21 HELIX 22 AC4 GLU B 337 LEU B 355 1 19 HELIX 23 AC5 LEU C 12 ALA C 31 1 20 HELIX 24 AC6 THR C 34 THR C 39 1 6 HELIX 25 AC7 THR D 30 TYR D 34 5 5 HELIX 26 AC8 LYS D 89 THR D 93 5 5 HELIX 27 AC9 ILE G 9 ASN G 24 1 16 HELIX 28 AD1 LYS G 29 HIS G 44 1 16 SHEET 1 AA1 6 ILE B 184 VAL B 191 0 SHEET 2 AA1 6 VAL B 194 VAL B 201 -1 O PHE B 196 N PHE B 189 SHEET 3 AA1 6 THR B 33 GLY B 40 1 N HIS B 34 O ASN B 195 SHEET 4 AA1 6 ALA B 220 ASP B 226 1 O ILE B 222 N LEU B 39 SHEET 5 AA1 6 SER B 253 ASN B 259 1 O PHE B 257 N VAL B 225 SHEET 6 AA1 6 CYS B 326 PHE B 330 1 O HIS B 329 N LEU B 258 SHEET 1 AA2 4 ARG C 51 ARG C 57 0 SHEET 2 AA2 4 PHE C 340 ASN C 345 -1 O LEU C 341 N LEU C 56 SHEET 3 AA2 4 VAL C 332 SER C 336 -1 N VAL C 332 O TRP C 344 SHEET 4 AA2 4 VAL C 320 VAL C 325 -1 N CYS C 322 O GLY C 335 SHEET 1 AA3 4 ILE C 63 TRP C 68 0 SHEET 2 AA3 4 LEU C 74 SER C 79 -1 O ALA C 78 N TYR C 64 SHEET 3 AA3 4 LYS C 83 ASP C 88 -1 O ILE C 85 N SER C 77 SHEET 4 AA3 4 LYS C 94 PRO C 99 -1 O VAL C 95 N ILE C 86 SHEET 1 AA4 4 VAL C 105 TYR C 110 0 SHEET 2 AA4 4 TYR C 116 GLY C 121 -1 O GLY C 120 N MET C 106 SHEET 3 AA4 4 ILE C 125 ASN C 130 -1 O TYR C 129 N VAL C 117 SHEET 4 AA4 4 ARG C 139 ALA C 145 -1 O LEU C 144 N CYS C 126 SHEET 1 AA5 4 LEU C 151 PHE C 156 0 SHEET 2 AA5 4 GLN C 161 SER C 166 -1 O SER C 165 N CYS C 153 SHEET 3 AA5 4 CYS C 171 ASP C 175 -1 O TRP C 174 N ILE C 162 SHEET 4 AA5 4 GLN C 181 PHE C 185 -1 O THR C 182 N LEU C 173 SHEET 1 AA6 4 SER C 194 LEU C 197 0 SHEET 2 AA6 4 LEU C 203 GLY C 207 -1 O VAL C 205 N SER C 196 SHEET 3 AA6 4 ALA C 213 ASP C 217 -1 O LYS C 214 N SER C 206 SHEET 4 AA6 4 CYS C 223 PHE C 227 -1 O ARG C 224 N LEU C 215 SHEET 1 AA7 4 ILE C 234 PHE C 239 0 SHEET 2 AA7 4 ALA C 245 SER C 250 -1 O GLY C 249 N ASN C 235 SHEET 3 AA7 4 CYS C 255 ASP C 259 -1 O PHE C 258 N PHE C 246 SHEET 4 AA7 4 GLN C 264 TYR C 269 -1 O LEU C 266 N LEU C 257 SHEET 1 AA8 4 ILE C 278 PHE C 283 0 SHEET 2 AA8 4 LEU C 289 TYR C 294 -1 O GLY C 293 N THR C 279 SHEET 3 AA8 4 CYS C 299 ASP C 303 -1 O ASN C 300 N ALA C 292 SHEET 4 AA8 4 ARG C 309 LEU C 313 -1 O GLY C 311 N VAL C 301 SHEET 1 AA9 4 GLN D 5 SER D 9 0 SHEET 2 AA9 4 SER D 19 SER D 27 -1 O ALA D 25 N GLN D 7 SHEET 3 AA9 4 THR D 80 ASN D 86 -1 O LEU D 81 N CYS D 24 SHEET 4 AA9 4 PHE D 70 ASP D 75 -1 N THR D 71 O GLN D 84 SHEET 1 AB1 4 ILE D 60 TYR D 62 0 SHEET 2 AB1 4 LEU D 47 ILE D 53 -1 N ASP D 52 O SER D 61 SHEET 3 AB1 4 MET D 36 GLN D 41 -1 N ARG D 40 O GLU D 48 SHEET 4 AB1 4 VAL D 95 ARG D 100 -1 O TYR D 97 N VAL D 39 LINK N1 NIT F 1 C FC0 F 2 1555 1555 1.44 LINK C1 FC0 F 2 N NLE F 3 1555 1555 1.45 LINK C NLE F 3 N D5B F 4 1555 1555 1.46 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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