HEADER MEMBRANE PROTEIN 23-APR-24 9BIA TITLE CRYO-EM STRUCTURE OF NINJ1 K45Q BOUND TO NB538 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NINJURIN-1; COMPND 3 CHAIN: B, C, A, D; COMPND 4 SYNONYM: NERVE INJURY-INDUCED PROTEIN 1; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: NB538; COMPND 9 CHAIN: E, F; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: NINJ1; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 10 ORGANISM_TAXID: 32630; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS INACTIVE-STATE, MEMBRANE RUPTURE, COMPLEX, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.POURMAL,M.C.JOHNSON,I.DESHPANDE REVDAT 1 16-OCT-24 9BIA 0 JRNL AUTH S.POURMAL,M.C.JOHNSON,I.DESHPANDE JRNL TITL CRYO-EM STRUCTURE OF NINJ1 K45Q BOUND TO NB538 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.00 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) : 3.000 REMARK 3 NUMBER OF PARTICLES : 102877 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 9BIA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-24. REMARK 100 THE DEPOSITION ID IS D_1000283433. 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 : COMPLEX OF NINJ1 WITH NB538 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 : TFS FALCON 4I (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2600.00 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, A, D, E, 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 B 1 REMARK 465 GLU B 2 REMARK 465 SER B 3 REMARK 465 GLY B 4 REMARK 465 THR B 5 REMARK 465 GLU B 6 REMARK 465 GLU B 7 REMARK 465 TYR B 8 REMARK 465 GLU B 9 REMARK 465 LEU B 10 REMARK 465 ASN B 11 REMARK 465 GLY B 12 REMARK 465 ASP B 13 REMARK 465 LEU B 14 REMARK 465 ARG B 15 REMARK 465 PRO B 16 REMARK 465 GLY B 17 REMARK 465 SER B 18 REMARK 465 PRO B 19 REMARK 465 GLY B 20 REMARK 465 SER B 21 REMARK 465 PRO B 22 REMARK 465 ASP B 23 REMARK 465 ALA B 24 REMARK 465 LEU B 25 REMARK 465 PRO B 26 REMARK 465 PRO B 27 REMARK 465 ARG B 28 REMARK 465 TRP B 29 REMARK 465 GLY B 30 REMARK 465 LEU B 31 REMARK 465 ARG B 32 REMARK 465 LYS B 143 REMARK 465 PRO B 144 REMARK 465 VAL B 145 REMARK 465 MET B 146 REMARK 465 ASP B 147 REMARK 465 VAL B 148 REMARK 465 ALA B 149 REMARK 465 PRO B 150 REMARK 465 ARG B 151 REMARK 465 GLN B 152 REMARK 465 GLY B 153 REMARK 465 SER B 154 REMARK 465 GLU B 155 REMARK 465 ASN B 156 REMARK 465 LEU B 157 REMARK 465 TYR B 158 REMARK 465 PHE B 159 REMARK 465 GLN B 160 REMARK 465 GLY B 161 REMARK 465 SER B 162 REMARK 465 ASP B 163 REMARK 465 TYR B 164 REMARK 465 LYS B 165 REMARK 465 ASP B 166 REMARK 465 ASP B 167 REMARK 465 ASP B 168 REMARK 465 ASP B 169 REMARK 465 LYS B 170 REMARK 465 MET C 1 REMARK 465 GLU C 2 REMARK 465 SER C 3 REMARK 465 GLY C 4 REMARK 465 THR C 5 REMARK 465 GLU C 6 REMARK 465 GLU C 7 REMARK 465 TYR C 8 REMARK 465 GLU C 9 REMARK 465 LEU C 10 REMARK 465 ASN C 11 REMARK 465 GLY C 12 REMARK 465 ASP C 13 REMARK 465 LEU C 14 REMARK 465 ARG C 15 REMARK 465 PRO C 16 REMARK 465 GLY C 17 REMARK 465 SER C 18 REMARK 465 PRO C 19 REMARK 465 GLY C 20 REMARK 465 SER C 21 REMARK 465 PRO C 22 REMARK 465 ASP C 23 REMARK 465 ALA C 24 REMARK 465 LEU C 25 REMARK 465 PRO C 26 REMARK 465 PRO C 27 REMARK 465 ARG C 28 REMARK 465 TRP C 29 REMARK 465 GLY C 30 REMARK 465 LEU C 31 REMARK 465 ARG C 32 REMARK 465 ASN C 33 REMARK 465 VAL C 141 REMARK 465 GLN C 142 REMARK 465 LYS C 143 REMARK 465 PRO C 144 REMARK 465 VAL C 145 REMARK 465 MET C 146 REMARK 465 ASP C 147 REMARK 465 VAL C 148 REMARK 465 ALA C 149 REMARK 465 PRO C 150 REMARK 465 ARG C 151 REMARK 465 GLN C 152 REMARK 465 GLY C 153 REMARK 465 SER C 154 REMARK 465 GLU C 155 REMARK 465 ASN C 156 REMARK 465 LEU C 157 REMARK 465 TYR C 158 REMARK 465 PHE C 159 REMARK 465 GLN C 160 REMARK 465 GLY C 161 REMARK 465 SER C 162 REMARK 465 ASP C 163 REMARK 465 TYR C 164 REMARK 465 LYS C 165 REMARK 465 ASP C 166 REMARK 465 ASP C 167 REMARK 465 ASP C 168 REMARK 465 ASP C 169 REMARK 465 LYS C 170 REMARK 465 MET A 1 REMARK 465 GLU A 2 REMARK 465 SER A 3 REMARK 465 GLY A 4 REMARK 465 THR A 5 REMARK 465 GLU A 6 REMARK 465 GLU A 7 REMARK 465 TYR A 8 REMARK 465 GLU A 9 REMARK 465 LEU A 10 REMARK 465 ASN A 11 REMARK 465 GLY A 12 REMARK 465 ASP A 13 REMARK 465 LEU A 14 REMARK 465 ARG A 15 REMARK 465 PRO A 16 REMARK 465 GLY A 17 REMARK 465 SER A 18 REMARK 465 PRO A 19 REMARK 465 GLY A 20 REMARK 465 SER A 21 REMARK 465 PRO A 22 REMARK 465 ASP A 23 REMARK 465 ALA A 24 REMARK 465 LEU A 25 REMARK 465 PRO A 26 REMARK 465 PRO A 27 REMARK 465 ARG A 28 REMARK 465 TRP A 29 REMARK 465 GLY A 30 REMARK 465 LEU A 31 REMARK 465 ARG A 32 REMARK 465 LYS A 143 REMARK 465 PRO A 144 REMARK 465 VAL A 145 REMARK 465 MET A 146 REMARK 465 ASP A 147 REMARK 465 VAL A 148 REMARK 465 ALA A 149 REMARK 465 PRO A 150 REMARK 465 ARG A 151 REMARK 465 GLN A 152 REMARK 465 GLY A 153 REMARK 465 SER A 154 REMARK 465 GLU A 155 REMARK 465 ASN A 156 REMARK 465 LEU A 157 REMARK 465 TYR A 158 REMARK 465 PHE A 159 REMARK 465 GLN A 160 REMARK 465 GLY A 161 REMARK 465 SER A 162 REMARK 465 ASP A 163 REMARK 465 TYR A 164 REMARK 465 LYS A 165 REMARK 465 ASP A 166 REMARK 465 ASP A 167 REMARK 465 ASP A 168 REMARK 465 ASP A 169 REMARK 465 LYS A 170 REMARK 465 MET D 1 REMARK 465 GLU D 2 REMARK 465 SER D 3 REMARK 465 GLY D 4 REMARK 465 THR D 5 REMARK 465 GLU D 6 REMARK 465 GLU D 7 REMARK 465 TYR D 8 REMARK 465 GLU D 9 REMARK 465 LEU D 10 REMARK 465 ASN D 11 REMARK 465 GLY D 12 REMARK 465 ASP D 13 REMARK 465 LEU D 14 REMARK 465 ARG D 15 REMARK 465 PRO D 16 REMARK 465 GLY D 17 REMARK 465 SER D 18 REMARK 465 PRO D 19 REMARK 465 GLY D 20 REMARK 465 SER D 21 REMARK 465 PRO D 22 REMARK 465 ASP D 23 REMARK 465 ALA D 24 REMARK 465 LEU D 25 REMARK 465 PRO D 26 REMARK 465 PRO D 27 REMARK 465 ARG D 28 REMARK 465 TRP D 29 REMARK 465 GLY D 30 REMARK 465 LEU D 31 REMARK 465 ARG D 32 REMARK 465 GLN D 142 REMARK 465 LYS D 143 REMARK 465 PRO D 144 REMARK 465 VAL D 145 REMARK 465 MET D 146 REMARK 465 ASP D 147 REMARK 465 VAL D 148 REMARK 465 ALA D 149 REMARK 465 PRO D 150 REMARK 465 ARG D 151 REMARK 465 GLN D 152 REMARK 465 GLY D 153 REMARK 465 SER D 154 REMARK 465 GLU D 155 REMARK 465 ASN D 156 REMARK 465 LEU D 157 REMARK 465 TYR D 158 REMARK 465 PHE D 159 REMARK 465 GLN D 160 REMARK 465 GLY D 161 REMARK 465 SER D 162 REMARK 465 ASP D 163 REMARK 465 TYR D 164 REMARK 465 LYS D 165 REMARK 465 ASP D 166 REMARK 465 ASP D 167 REMARK 465 ASP D 168 REMARK 465 ASP D 169 REMARK 465 LYS D 170 REMARK 465 SER E 119 REMARK 465 SER E 120 REMARK 465 ASP E 121 REMARK 465 LYS E 122 REMARK 465 THR E 123 REMARK 465 HIS E 124 REMARK 465 THR E 125 REMARK 465 GLY E 126 REMARK 465 GLY E 127 REMARK 465 SER E 128 REMARK 465 SER E 129 REMARK 465 GLY E 130 REMARK 465 GLY E 131 REMARK 465 SER E 132 REMARK 465 HIS E 133 REMARK 465 HIS E 134 REMARK 465 HIS E 135 REMARK 465 HIS E 136 REMARK 465 HIS E 137 REMARK 465 HIS E 138 REMARK 465 GLY E 139 REMARK 465 SER E 140 REMARK 465 SER F 119 REMARK 465 SER F 120 REMARK 465 ASP F 121 REMARK 465 LYS F 122 REMARK 465 THR F 123 REMARK 465 HIS F 124 REMARK 465 THR F 125 REMARK 465 GLY F 126 REMARK 465 GLY F 127 REMARK 465 SER F 128 REMARK 465 SER F 129 REMARK 465 GLY F 130 REMARK 465 GLY F 131 REMARK 465 SER F 132 REMARK 465 HIS F 133 REMARK 465 HIS F 134 REMARK 465 HIS F 135 REMARK 465 HIS F 136 REMARK 465 HIS F 137 REMARK 465 HIS F 138 REMARK 465 GLY F 139 REMARK 465 SER F 140 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 HZ2 LYS B 44 OD1 ASN D 120 1.55 REMARK 500 HZ2 LYS C 44 OD1 ASN A 120 1.57 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 PHE E 104 64.73 35.81 REMARK 500 LEU F 11 54.05 -148.23 REMARK 500 ASN F 80 55.68 35.98 REMARK 500 VAL F 116 -60.26 64.92 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44585 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF NINJ1 K45Q BOUND TO NB538 DBREF 9BIA B 1 152 UNP O70131 NINJ1_MOUSE 1 152 DBREF 9BIA C 1 152 UNP O70131 NINJ1_MOUSE 1 152 DBREF 9BIA A 1 152 UNP O70131 NINJ1_MOUSE 1 152 DBREF 9BIA D 1 152 UNP O70131 NINJ1_MOUSE 1 152 DBREF 9BIA E 1 140 PDB 9BIA 9BIA 1 140 DBREF 9BIA F 1 140 PDB 9BIA 9BIA 1 140 SEQADV 9BIA GLN B 45 UNP O70131 LYS 45 ENGINEERED MUTATION SEQADV 9BIA GLY B 153 UNP O70131 EXPRESSION TAG SEQADV 9BIA SER B 154 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLU B 155 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASN B 156 UNP O70131 EXPRESSION TAG SEQADV 9BIA LEU B 157 UNP O70131 EXPRESSION TAG SEQADV 9BIA TYR B 158 UNP O70131 EXPRESSION TAG SEQADV 9BIA PHE B 159 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLN B 160 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLY B 161 UNP O70131 EXPRESSION TAG SEQADV 9BIA SER B 162 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP B 163 UNP O70131 EXPRESSION TAG SEQADV 9BIA TYR B 164 UNP O70131 EXPRESSION TAG SEQADV 9BIA LYS B 165 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP B 166 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP B 167 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP B 168 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP B 169 UNP O70131 EXPRESSION TAG SEQADV 9BIA LYS B 170 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLN C 45 UNP O70131 LYS 45 ENGINEERED MUTATION SEQADV 9BIA GLY C 153 UNP O70131 EXPRESSION TAG SEQADV 9BIA SER C 154 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLU C 155 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASN C 156 UNP O70131 EXPRESSION TAG SEQADV 9BIA LEU C 157 UNP O70131 EXPRESSION TAG SEQADV 9BIA TYR C 158 UNP O70131 EXPRESSION TAG SEQADV 9BIA PHE C 159 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLN C 160 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLY C 161 UNP O70131 EXPRESSION TAG SEQADV 9BIA SER C 162 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP C 163 UNP O70131 EXPRESSION TAG SEQADV 9BIA TYR C 164 UNP O70131 EXPRESSION TAG SEQADV 9BIA LYS C 165 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP C 166 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP C 167 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP C 168 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP C 169 UNP O70131 EXPRESSION TAG SEQADV 9BIA LYS C 170 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLN A 45 UNP O70131 LYS 45 ENGINEERED MUTATION SEQADV 9BIA GLY A 153 UNP O70131 EXPRESSION TAG SEQADV 9BIA SER A 154 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLU A 155 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASN A 156 UNP O70131 EXPRESSION TAG SEQADV 9BIA LEU A 157 UNP O70131 EXPRESSION TAG SEQADV 9BIA TYR A 158 UNP O70131 EXPRESSION TAG SEQADV 9BIA PHE A 159 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLN A 160 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLY A 161 UNP O70131 EXPRESSION TAG SEQADV 9BIA SER A 162 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP A 163 UNP O70131 EXPRESSION TAG SEQADV 9BIA TYR A 164 UNP O70131 EXPRESSION TAG SEQADV 9BIA LYS A 165 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP A 166 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP A 167 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP A 168 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP A 169 UNP O70131 EXPRESSION TAG SEQADV 9BIA LYS A 170 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLN D 45 UNP O70131 LYS 45 ENGINEERED MUTATION SEQADV 9BIA GLY D 153 UNP O70131 EXPRESSION TAG SEQADV 9BIA SER D 154 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLU D 155 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASN D 156 UNP O70131 EXPRESSION TAG SEQADV 9BIA LEU D 157 UNP O70131 EXPRESSION TAG SEQADV 9BIA TYR D 158 UNP O70131 EXPRESSION TAG SEQADV 9BIA PHE D 159 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLN D 160 UNP O70131 EXPRESSION TAG SEQADV 9BIA GLY D 161 UNP O70131 EXPRESSION TAG SEQADV 9BIA SER D 162 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP D 163 UNP O70131 EXPRESSION TAG SEQADV 9BIA TYR D 164 UNP O70131 EXPRESSION TAG SEQADV 9BIA LYS D 165 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP D 166 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP D 167 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP D 168 UNP O70131 EXPRESSION TAG SEQADV 9BIA ASP D 169 UNP O70131 EXPRESSION TAG SEQADV 9BIA LYS D 170 UNP O70131 EXPRESSION TAG SEQRES 1 B 170 MET GLU SER GLY THR GLU GLU TYR GLU LEU ASN GLY ASP SEQRES 2 B 170 LEU ARG PRO GLY SER PRO GLY SER PRO ASP ALA LEU PRO SEQRES 3 B 170 PRO ARG TRP GLY LEU ARG ASN ARG PRO ILE ASN VAL ASN SEQRES 4 B 170 HIS TYR ALA ASN LYS GLN SER ALA ALA GLU SER MET LEU SEQRES 5 B 170 ASP ILE ALA LEU LEU MET ALA ASN ALA SER GLN LEU LYS SEQRES 6 B 170 ALA VAL VAL GLU GLN GLY ASN ASP PHE ALA PHE PHE VAL SEQRES 7 B 170 PRO LEU VAL VAL LEU ILE SER ILE SER LEU VAL LEU GLN SEQRES 8 B 170 ILE GLY VAL GLY VAL LEU LEU ILE PHE LEU VAL LYS TYR SEQRES 9 B 170 ASP LEU ASN ASN PRO ALA LYS HIS ALA LYS LEU ASP PHE SEQRES 10 B 170 LEU ASN ASN LEU ALA THR GLY LEU VAL PHE ILE ILE VAL SEQRES 11 B 170 VAL VAL ASN ILE PHE ILE THR ALA PHE GLY VAL GLN LYS SEQRES 12 B 170 PRO VAL MET ASP VAL ALA PRO ARG GLN GLY SER GLU ASN SEQRES 13 B 170 LEU TYR PHE GLN GLY SER ASP TYR LYS ASP ASP ASP ASP SEQRES 14 B 170 LYS SEQRES 1 C 170 MET GLU SER GLY THR GLU GLU TYR GLU LEU ASN GLY ASP SEQRES 2 C 170 LEU ARG PRO GLY SER PRO GLY SER PRO ASP ALA LEU PRO SEQRES 3 C 170 PRO ARG TRP GLY LEU ARG ASN ARG PRO ILE ASN VAL ASN SEQRES 4 C 170 HIS TYR ALA ASN LYS GLN SER ALA ALA GLU SER MET LEU SEQRES 5 C 170 ASP ILE ALA LEU LEU MET ALA ASN ALA SER GLN LEU LYS SEQRES 6 C 170 ALA VAL VAL GLU GLN GLY ASN ASP PHE ALA PHE PHE VAL SEQRES 7 C 170 PRO LEU VAL VAL LEU ILE SER ILE SER LEU VAL LEU GLN SEQRES 8 C 170 ILE GLY VAL GLY VAL LEU LEU ILE PHE LEU VAL LYS TYR SEQRES 9 C 170 ASP LEU ASN ASN PRO ALA LYS HIS ALA LYS LEU ASP PHE SEQRES 10 C 170 LEU ASN ASN LEU ALA THR GLY LEU VAL PHE ILE ILE VAL SEQRES 11 C 170 VAL VAL ASN ILE PHE ILE THR ALA PHE GLY VAL GLN LYS SEQRES 12 C 170 PRO VAL MET ASP VAL ALA PRO ARG GLN GLY SER GLU ASN SEQRES 13 C 170 LEU TYR PHE GLN GLY SER ASP TYR LYS ASP ASP ASP ASP SEQRES 14 C 170 LYS SEQRES 1 A 170 MET GLU SER GLY THR GLU GLU TYR GLU LEU ASN GLY ASP SEQRES 2 A 170 LEU ARG PRO GLY SER PRO GLY SER PRO ASP ALA LEU PRO SEQRES 3 A 170 PRO ARG TRP GLY LEU ARG ASN ARG PRO ILE ASN VAL ASN SEQRES 4 A 170 HIS TYR ALA ASN LYS GLN SER ALA ALA GLU SER MET LEU SEQRES 5 A 170 ASP ILE ALA LEU LEU MET ALA ASN ALA SER GLN LEU LYS SEQRES 6 A 170 ALA VAL VAL GLU GLN GLY ASN ASP PHE ALA PHE PHE VAL SEQRES 7 A 170 PRO LEU VAL VAL LEU ILE SER ILE SER LEU VAL LEU GLN SEQRES 8 A 170 ILE GLY VAL GLY VAL LEU LEU ILE PHE LEU VAL LYS TYR SEQRES 9 A 170 ASP LEU ASN ASN PRO ALA LYS HIS ALA LYS LEU ASP PHE SEQRES 10 A 170 LEU ASN ASN LEU ALA THR GLY LEU VAL PHE ILE ILE VAL SEQRES 11 A 170 VAL VAL ASN ILE PHE ILE THR ALA PHE GLY VAL GLN LYS SEQRES 12 A 170 PRO VAL MET ASP VAL ALA PRO ARG GLN GLY SER GLU ASN SEQRES 13 A 170 LEU TYR PHE GLN GLY SER ASP TYR LYS ASP ASP ASP ASP SEQRES 14 A 170 LYS SEQRES 1 D 170 MET GLU SER GLY THR GLU GLU TYR GLU LEU ASN GLY ASP SEQRES 2 D 170 LEU ARG PRO GLY SER PRO GLY SER PRO ASP ALA LEU PRO SEQRES 3 D 170 PRO ARG TRP GLY LEU ARG ASN ARG PRO ILE ASN VAL ASN SEQRES 4 D 170 HIS TYR ALA ASN LYS GLN SER ALA ALA GLU SER MET LEU SEQRES 5 D 170 ASP ILE ALA LEU LEU MET ALA ASN ALA SER GLN LEU LYS SEQRES 6 D 170 ALA VAL VAL GLU GLN GLY ASN ASP PHE ALA PHE PHE VAL SEQRES 7 D 170 PRO LEU VAL VAL LEU ILE SER ILE SER LEU VAL LEU GLN SEQRES 8 D 170 ILE GLY VAL GLY VAL LEU LEU ILE PHE LEU VAL LYS TYR SEQRES 9 D 170 ASP LEU ASN ASN PRO ALA LYS HIS ALA LYS LEU ASP PHE SEQRES 10 D 170 LEU ASN ASN LEU ALA THR GLY LEU VAL PHE ILE ILE VAL SEQRES 11 D 170 VAL VAL ASN ILE PHE ILE THR ALA PHE GLY VAL GLN LYS SEQRES 12 D 170 PRO VAL MET ASP VAL ALA PRO ARG GLN GLY SER GLU ASN SEQRES 13 D 170 LEU TYR PHE GLN GLY SER ASP TYR LYS ASP ASP ASP ASP SEQRES 14 D 170 LYS SEQRES 1 E 140 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 140 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 140 PHE ASN VAL TYR SER SER SER TYR TYR TYR VAL GLY TRP SEQRES 4 E 140 VAL ARG ARG ALA PRO GLY LYS GLY GLU GLU LEU VAL ALA SEQRES 5 E 140 ARG ILE SER PRO SER TYR GLY TYR THR TYR TYR ALA ASP SEQRES 6 E 140 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 E 140 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 E 140 GLU ASP THR ALA VAL TYR TYR CYS GLU VAL TYR ILE PHE SEQRES 9 E 140 GLY GLN TYR PHE GLU SER GLY GLN GLY THR LEU VAL THR SEQRES 10 E 140 VAL SER SER ASP LYS THR HIS THR GLY GLY SER SER GLY SEQRES 11 E 140 GLY SER HIS HIS HIS HIS HIS HIS GLY SER SEQRES 1 F 140 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 140 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 140 PHE ASN VAL TYR SER SER SER TYR TYR TYR VAL GLY TRP SEQRES 4 F 140 VAL ARG ARG ALA PRO GLY LYS GLY GLU GLU LEU VAL ALA SEQRES 5 F 140 ARG ILE SER PRO SER TYR GLY TYR THR TYR TYR ALA ASP SEQRES 6 F 140 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 F 140 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 F 140 GLU ASP THR ALA VAL TYR TYR CYS GLU VAL TYR ILE PHE SEQRES 9 F 140 GLY GLN TYR PHE GLU SER GLY GLN GLY THR LEU VAL THR SEQRES 10 F 140 VAL SER SER ASP LYS THR HIS THR GLY GLY SER SER GLY SEQRES 11 F 140 GLY SER HIS HIS HIS HIS HIS HIS GLY SER HELIX 1 AA1 ASN B 37 GLY B 71 1 35 HELIX 2 AA2 ASN B 72 PHE B 74 5 3 HELIX 3 AA3 PHE B 76 TYR B 104 1 29 HELIX 4 AA4 LYS B 111 VAL B 141 1 31 HELIX 5 AA5 ASN C 37 GLY C 71 1 35 HELIX 6 AA6 ASN C 72 PHE C 74 5 3 HELIX 7 AA7 PHE C 76 TYR C 104 1 29 HELIX 8 AA8 ASN C 108 ALA C 110 5 3 HELIX 9 AA9 LYS C 111 PHE C 139 1 29 HELIX 10 AB1 ASN A 37 GLU A 69 1 33 HELIX 11 AB2 GLN A 70 PHE A 74 5 5 HELIX 12 AB3 PHE A 76 VAL A 102 1 27 HELIX 13 AB4 LYS A 111 VAL A 141 1 31 HELIX 14 AB5 ASN D 37 GLY D 71 1 35 HELIX 15 AB6 ASN D 72 PHE D 74 5 3 HELIX 16 AB7 PHE D 76 TYR D 104 1 29 HELIX 17 AB8 LYS D 111 VAL D 141 1 31 HELIX 18 AB9 THR E 77 LYS E 79 5 3 HELIX 19 AC1 ARG E 90 THR E 94 5 5 HELIX 20 AC2 ARG F 90 THR F 94 5 5 SHEET 1 AA1 4 GLN E 3 SER E 7 0 SHEET 2 AA1 4 LEU E 18 SER E 25 -1 O ALA E 23 N VAL E 5 SHEET 3 AA1 4 THR E 81 MET E 86 -1 O MET E 86 N LEU E 18 SHEET 4 AA1 4 PHE E 71 ASP E 76 -1 N THR E 72 O GLN E 85 SHEET 1 AA2 6 GLY E 10 LEU E 11 0 SHEET 2 AA2 6 THR E 114 THR E 117 1 O THR E 117 N GLY E 10 SHEET 3 AA2 6 ALA E 95 ILE E 103 -1 N TYR E 97 O THR E 114 SHEET 4 AA2 6 TYR E 35 ARG E 42 -1 N VAL E 40 O TYR E 98 SHEET 5 AA2 6 GLU E 49 ILE E 54 -1 O ILE E 54 N VAL E 37 SHEET 6 AA2 6 THR E 61 TYR E 63 -1 O TYR E 62 N ARG E 53 SHEET 1 AA3 4 GLY E 10 LEU E 11 0 SHEET 2 AA3 4 THR E 114 THR E 117 1 O THR E 117 N GLY E 10 SHEET 3 AA3 4 ALA E 95 ILE E 103 -1 N TYR E 97 O THR E 114 SHEET 4 AA3 4 GLN E 106 GLU E 109 -1 O GLN E 106 N ILE E 103 SHEET 1 AA4 4 GLN F 3 SER F 7 0 SHEET 2 AA4 4 LEU F 18 SER F 25 -1 O ALA F 23 N VAL F 5 SHEET 3 AA4 4 THR F 81 MET F 86 -1 O MET F 86 N LEU F 18 SHEET 4 AA4 4 PHE F 71 ASP F 76 -1 N SER F 74 O TYR F 83 SHEET 1 AA5 5 THR F 61 TYR F 63 0 SHEET 2 AA5 5 LYS F 46 ILE F 54 -1 N ARG F 53 O TYR F 62 SHEET 3 AA5 5 TYR F 36 ALA F 43 -1 N ARG F 41 O GLU F 49 SHEET 4 AA5 5 VAL F 96 ILE F 103 -1 O TYR F 98 N VAL F 40 SHEET 5 AA5 5 GLN F 106 GLU F 109 -1 O GLN F 106 N ILE F 103 SSBOND 1 CYS E 22 CYS E 99 1555 1555 2.03 SSBOND 2 CYS F 22 CYS F 99 1555 1555 2.03 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