HEADER IMMUNE SYSTEM 12-OCT-24 9JY2 TITLE FAB-CD3-DELTA EPSILON-TCR COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD3 ZETA CHAIN; COMPND 3 CHAIN: a, b; COMPND 4 SYNONYM: T-CELL RECEPTOR T3 ZETA CHAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD3 DELTA CHAIN; COMPND 8 CHAIN: d; COMPND 9 SYNONYM: T-CELL RECEPTOR T3 DELTA CHAIN; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD3 EPSILON CHAIN; COMPND 13 CHAIN: e, f; COMPND 14 SYNONYM: T-CELL SURFACE ANTIGEN T3/LEU-4 EPSILON CHAIN; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD3 GAMMA CHAIN; COMPND 18 CHAIN: g; COMPND 19 SYNONYM: T-CELL RECEPTOR T3 GAMMA CHAIN; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: T CELL RECEPTOR DELTA CONSTANT; COMPND 23 CHAIN: m; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 6; COMPND 26 MOLECULE: T CELL RECEPTOR GAMMA CONSTANT 1; COMPND 27 CHAIN: n; COMPND 28 ENGINEERED: YES; COMPND 29 MOL_ID: 7; COMPND 30 MOLECULE: FAB LIGHT CHAIN; COMPND 31 CHAIN: A; COMPND 32 ENGINEERED: YES; COMPND 33 MOL_ID: 8; COMPND 34 MOLECULE: FAB HEAVY CHAIN; COMPND 35 CHAIN: B; COMPND 36 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: CD247, CD3Z, T3Z, TCRZ; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: CD3D, T3D; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: CD3E, T3E; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 GENE: CD3G, T3G; SOURCE 27 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 31 ORGANISM_COMMON: HUMAN; SOURCE 32 ORGANISM_TAXID: 9606; SOURCE 33 GENE: TRDC; SOURCE 34 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 36 MOL_ID: 6; SOURCE 37 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 38 ORGANISM_COMMON: HUMAN; SOURCE 39 ORGANISM_TAXID: 9606; SOURCE 40 GENE: TRGC1, TCRGC1; SOURCE 41 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 42 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 43 MOL_ID: 7; SOURCE 44 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 45 ORGANISM_COMMON: HUMAN; SOURCE 46 ORGANISM_TAXID: 9606; SOURCE 47 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 48 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 49 MOL_ID: 8; SOURCE 50 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 51 ORGANISM_COMMON: HUMAN; SOURCE 52 ORGANISM_TAXID: 9606; SOURCE 53 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 54 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS T CELL RECEPTOR, GAMMA DELTA TCR, IMMUNE CELL, FAB COMPLEX, IMMUNE KEYWDS 2 SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR L.WANG,J.LI,Z.LI REVDAT 1 26-NOV-25 9JY2 0 JRNL AUTH L.WANG,Z.LI,Y.FAN,J.LI JRNL TITL STRUCTURES OF THE APO AND AGONIST-CROSSLINKED HUMAN GAMMA JRNL TITL 2 DELTA T-CELL RECEPTOR JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.24 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, 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) : 3.240 REMARK 3 NUMBER OF PARTICLES : 232138 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 9JY2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 15-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1300052444. 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 : FAB-CD3-DELTA EPSILON-TCR REMARK 245 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 : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1400.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 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) : 5000.00 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: DECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: a, b, d, e, f, g, m, n, A, B 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 LEU b 26 REMARK 465 SER b 56 REMARK 465 ASN e 154 REMARK 465 GLU f 70 REMARK 465 ASP f 71 REMARK 465 ASP f 72 REMARK 465 LYS f 73 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 OD1 ASN d 38 OG1 THR d 76 2.02 REMARK 500 NH1 ARG f 117 O CYS g 104 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 ASP a 28 169.16 67.00 REMARK 500 PHE a 55 -130.87 58.58 REMARK 500 LEU d 52 -178.30 -68.20 REMARK 500 ASP d 66 70.76 57.69 REMARK 500 GLU e 79 -128.00 54.20 REMARK 500 ASN g 28 19.14 59.37 REMARK 500 GLU g 49 76.09 -102.83 REMARK 500 ASP g 68 -7.86 72.75 REMARK 500 LEU g 110 54.71 -97.34 REMARK 500 TYR A 50 -152.74 59.83 REMARK 500 ASN A 77 117.81 -39.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-61885 RELATED DB: EMDB REMARK 900 FAB-CD3-DELTA EPSILON-TCR COMPLEX DBREF 9JY2 a 26 56 UNP P20963 CD3Z_HUMAN 26 56 DBREF 9JY2 b 26 56 UNP P20963 CD3Z_HUMAN 26 56 DBREF 9JY2 d 22 126 UNP P04234 CD3D_HUMAN 22 126 DBREF 9JY2 e 33 154 UNP P07766 CD3E_HUMAN 33 154 DBREF 9JY2 f 33 154 UNP P07766 CD3E_HUMAN 33 154 DBREF 9JY2 g 26 140 UNP P09693 CD3G_HUMAN 26 140 DBREF 9JY2 m 254 289 UNP B7Z8K6 TRDC_HUMAN 117 152 DBREF 9JY2 n 251 288 UNP P0CF51 TRGC1_HUMAN 127 164 DBREF 9JY2 A 1 104 PDB 9JY2 9JY2 1 104 DBREF 9JY2 B 1 121 PDB 9JY2 9JY2 1 121 SEQRES 1 a 31 LEU LEU ASP PRO LYS LEU CYS TYR LEU LEU ASP GLY ILE SEQRES 2 a 31 LEU PHE ILE TYR GLY VAL ILE LEU THR ALA LEU PHE LEU SEQRES 3 a 31 ARG VAL LYS PHE SER SEQRES 1 b 31 LEU LEU ASP PRO LYS LEU CYS TYR LEU LEU ASP GLY ILE SEQRES 2 b 31 LEU PHE ILE TYR GLY VAL ILE LEU THR ALA LEU PHE LEU SEQRES 3 b 31 ARG VAL LYS PHE SER SEQRES 1 d 105 PHE LYS ILE PRO ILE GLU GLU LEU GLU ASP ARG VAL PHE SEQRES 2 d 105 VAL ASN CYS ASN THR SER ILE THR TRP VAL GLU GLY THR SEQRES 3 d 105 VAL GLY THR LEU LEU SER ASP ILE THR ARG LEU ASP LEU SEQRES 4 d 105 GLY LYS ARG ILE LEU ASP PRO ARG GLY ILE TYR ARG CYS SEQRES 5 d 105 ASN GLY THR ASP ILE TYR LYS ASP LYS GLU SER THR VAL SEQRES 6 d 105 GLN VAL HIS TYR ARG MET CYS GLN SER CYS VAL GLU LEU SEQRES 7 d 105 ASP PRO ALA THR VAL ALA GLY ILE ILE VAL THR ASP VAL SEQRES 8 d 105 ILE ALA THR LEU LEU LEU ALA LEU GLY VAL PHE CYS PHE SEQRES 9 d 105 ALA SEQRES 1 e 122 GLN THR PRO TYR LYS VAL SER ILE SER GLY THR THR VAL SEQRES 2 e 122 ILE LEU THR CYS PRO GLN TYR PRO GLY SER GLU ILE LEU SEQRES 3 e 122 TRP GLN HIS ASN ASP LYS ASN ILE GLY GLY ASP GLU ASP SEQRES 4 e 122 ASP LYS ASN ILE GLY SER ASP GLU ASP HIS LEU SER LEU SEQRES 5 e 122 LYS GLU PHE SER GLU LEU GLU GLN SER GLY TYR TYR VAL SEQRES 6 e 122 CYS TYR PRO ARG GLY SER LYS PRO GLU ASP ALA ASN PHE SEQRES 7 e 122 TYR LEU TYR LEU ARG ALA ARG VAL CYS GLU ASN CYS MET SEQRES 8 e 122 GLU MET ASP VAL MET SER VAL ALA THR ILE VAL ILE VAL SEQRES 9 e 122 ASP ILE CYS ILE THR GLY GLY LEU LEU LEU LEU VAL TYR SEQRES 10 e 122 TYR TRP SER LYS ASN SEQRES 1 f 122 GLN THR PRO TYR LYS VAL SER ILE SER GLY THR THR VAL SEQRES 2 f 122 ILE LEU THR CYS PRO GLN TYR PRO GLY SER GLU ILE LEU SEQRES 3 f 122 TRP GLN HIS ASN ASP LYS ASN ILE GLY GLY ASP GLU ASP SEQRES 4 f 122 ASP LYS ASN ILE GLY SER ASP GLU ASP HIS LEU SER LEU SEQRES 5 f 122 LYS GLU PHE SER GLU LEU GLU GLN SER GLY TYR TYR VAL SEQRES 6 f 122 CYS TYR PRO ARG GLY SER LYS PRO GLU ASP ALA ASN PHE SEQRES 7 f 122 TYR LEU TYR LEU ARG ALA ARG VAL CYS GLU ASN CYS MET SEQRES 8 f 122 GLU MET ASP VAL MET SER VAL ALA THR ILE VAL ILE VAL SEQRES 9 f 122 ASP ILE CYS ILE THR GLY GLY LEU LEU LEU LEU VAL TYR SEQRES 10 f 122 TYR TRP SER LYS ASN SEQRES 1 g 115 LYS GLY ASN HIS LEU VAL LYS VAL TYR ASP TYR GLN GLU SEQRES 2 g 115 ASP GLY SER VAL LEU LEU THR CYS ASP ALA GLU ALA LYS SEQRES 3 g 115 ASN ILE THR TRP PHE LYS ASP GLY LYS MET ILE GLY PHE SEQRES 4 g 115 LEU THR GLU ASP LYS LYS LYS TRP ASN LEU GLY SER ASN SEQRES 5 g 115 ALA LYS ASP PRO ARG GLY MET TYR GLN CYS LYS GLY SER SEQRES 6 g 115 GLN ASN LYS SER LYS PRO LEU GLN VAL TYR TYR ARG MET SEQRES 7 g 115 CYS GLN ASN CYS ILE GLU LEU ASN ALA ALA THR ILE SER SEQRES 8 g 115 GLY PHE LEU PHE ALA GLU ILE VAL SER ILE PHE VAL LEU SEQRES 9 g 115 ALA VAL GLY VAL TYR PHE ILE ALA GLY GLN ASP SEQRES 1 m 36 VAL HIS THR GLU LYS VAL ASN MET MET SER LEU THR VAL SEQRES 2 m 36 LEU GLY LEU ARG MET LEU PHE ALA LYS THR VAL ALA VAL SEQRES 3 m 36 ASN PHE LEU LEU THR ALA LYS LEU PHE PHE SEQRES 1 n 38 ASP THR LEU LEU LEU GLN LEU THR ASN THR SER ALA TYR SEQRES 2 n 38 TYR MET TYR LEU LEU LEU LEU LEU LYS SER VAL VAL TYR SEQRES 3 n 38 PHE ALA ILE ILE THR CYS CYS LEU LEU ARG ARG THR SEQRES 1 A 104 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 A 104 SER LEU GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER SEQRES 3 A 104 GLN ASP ILE ARG ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 A 104 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 A 104 ARG LEU HIS SER GLY VAL PRO SER LYS PHE SER GLY SER SEQRES 6 A 104 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 A 104 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN GLY SEQRES 8 A 104 ASN THR LEU PRO TRP THR PHE ALA GLY GLY THR LYS LEU SEQRES 1 B 121 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 B 121 PRO GLY ALA SER MET LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 B 121 TYR SER PHE THR GLY TYR THR MET ASN TRP VAL LYS GLN SEQRES 4 B 121 SER HIS GLY LYS ASN LEU GLU TRP MET GLY LEU ILE ASN SEQRES 5 B 121 PRO TYR LYS GLY VAL SER THR TYR ASN GLN LYS PHE LYS SEQRES 6 B 121 ASP LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 B 121 ALA TYR MET GLU LEU LEU SER LEU THR SER GLU ASP SER SEQRES 8 B 121 ALA VAL TYR TYR CYS ALA ARG SER GLY TYR TYR GLY ASP SEQRES 9 B 121 SER ASP TRP TYR PHE ASP VAL TRP GLY GLN GLY THR THR SEQRES 10 B 121 LEU THR VAL PHE HET CLR b 301 28 HET NAG d 201 14 HET NAG d 202 14 HETNAM CLR CHOLESTEROL HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 11 CLR C27 H46 O FORMUL 12 NAG 2(C8 H15 N O6) HELIX 1 AA1 PRO a 29 LYS a 54 1 26 HELIX 2 AA2 ASP b 28 PHE b 55 1 28 HELIX 3 AA3 ILE d 64 ASP d 66 5 3 HELIX 4 AA4 ASP d 100 ALA d 126 1 27 HELIX 5 AA5 SER e 88 SER e 93 1 6 HELIX 6 AA6 ASP e 126 LYS e 153 1 28 HELIX 7 AA7 ASP f 126 ASN f 154 1 29 HELIX 8 AA8 SER g 76 ASP g 80 5 5 HELIX 9 AA9 ASN g 111 ASP g 140 1 30 HELIX 10 AB1 THR m 256 PHE m 289 1 34 HELIX 11 AB2 THR n 252 THR n 288 1 37 HELIX 12 AB3 SER B 28 THR B 30 5 3 HELIX 13 AB4 GLN B 62 LYS B 65 5 4 HELIX 14 AB5 THR B 87 SER B 91 5 5 SHEET 1 AA1 4 ILE d 26 LEU d 29 0 SHEET 2 AA1 4 ARG d 32 ASN d 36 -1 O PHE d 34 N GLU d 27 SHEET 3 AA1 4 ARG d 57 LYS d 62 -1 O LEU d 58 N VAL d 35 SHEET 4 AA1 4 THR d 50 LEU d 51 -1 N THR d 50 O ASP d 59 SHEET 1 AA2 7 ILE d 41 GLY d 46 0 SHEET 2 AA2 7 ARG d 68 CYS d 73 -1 O ILE d 70 N VAL d 44 SHEET 3 AA2 7 SER d 84 ARG d 91 -1 O VAL d 86 N TYR d 71 SHEET 4 AA2 7 PHE e 110 ALA e 116 1 O TYR e 111 N GLN d 87 SHEET 5 AA2 7 GLY e 94 PRO e 100 -1 N TYR e 96 O LEU e 112 SHEET 6 AA2 7 ILE e 57 HIS e 61 -1 N LEU e 58 O TYR e 99 SHEET 7 AA2 7 LYS e 64 ILE e 66 -1 O LYS e 64 N HIS e 61 SHEET 1 AA3 2 CYS d 96 GLU d 98 0 SHEET 2 AA3 2 CYS e 122 GLU e 124 -1 O MET e 123 N VAL d 97 SHEET 1 AA4 4 LYS e 37 SER e 41 0 SHEET 2 AA4 4 THR e 44 THR e 48 -1 O THR e 44 N SER e 41 SHEET 3 AA4 4 HIS e 81 LEU e 84 -1 O LEU e 82 N LEU e 47 SHEET 4 AA4 4 ILE e 75 ASP e 78 -1 N GLY e 76 O SER e 83 SHEET 1 AA5 4 LYS f 37 SER f 41 0 SHEET 2 AA5 4 THR f 44 THR f 48 -1 O ILE f 46 N SER f 39 SHEET 3 AA5 4 LEU f 82 LEU f 84 -1 O LEU f 82 N LEU f 47 SHEET 4 AA5 4 GLY f 76 SER f 77 -1 N GLY f 76 O SER f 83 SHEET 1 AA6 3 LYS f 64 ILE f 66 0 SHEET 2 AA6 3 LEU f 58 HIS f 61 -1 N HIS f 61 O LYS f 64 SHEET 3 AA6 3 TYR f 96 TYR f 99 -1 O VAL f 97 N GLN f 60 SHEET 1 AA7 2 LEU f 112 ALA f 116 0 SHEET 2 AA7 2 GLN g 98 ARG g 102 1 O TYR g 100 N TYR f 113 SHEET 1 AA8 2 CYS f 122 GLU f 124 0 SHEET 2 AA8 2 CYS g 107 GLU g 109 -1 O ILE g 108 N MET f 123 SHEET 1 AA9 3 VAL g 31 TYR g 34 0 SHEET 2 AA9 3 VAL g 42 CYS g 46 -1 O THR g 45 N LYS g 32 SHEET 3 AA9 3 TRP g 72 GLY g 75 -1 O GLY g 75 N VAL g 42 SHEET 1 AB1 4 LYS g 60 GLY g 63 0 SHEET 2 AB1 4 TRP g 55 LYS g 57 -1 N LYS g 57 O LYS g 60 SHEET 3 AB1 4 TYR g 85 LYS g 88 -1 O GLN g 86 N PHE g 56 SHEET 4 AB1 4 LYS g 93 SER g 94 -1 O SER g 94 N CYS g 87 SHEET 1 AB2 4 MET A 4 GLN A 6 0 SHEET 2 AB2 4 VAL A 19 ALA A 25 -1 O ARG A 24 N THR A 5 SHEET 3 AB2 4 ASP A 70 ILE A 75 -1 O TYR A 71 N CYS A 23 SHEET 4 AB2 4 GLY A 64 SER A 67 -1 N SER A 65 O SER A 72 SHEET 1 AB3 5 ARG A 53 LEU A 54 0 SHEET 2 AB3 5 VAL A 44 TYR A 49 -1 N TYR A 49 O ARG A 53 SHEET 3 AB3 5 LEU A 33 GLN A 38 -1 N TRP A 35 O LEU A 47 SHEET 4 AB3 5 THR A 85 GLN A 90 -1 O THR A 85 N GLN A 38 SHEET 5 AB3 5 THR A 102 LYS A 103 -1 O THR A 102 N TYR A 86 SHEET 1 AB4 4 GLN B 3 GLN B 6 0 SHEET 2 AB4 4 SER B 17 SER B 25 -1 O LYS B 23 N GLN B 5 SHEET 3 AB4 4 THR B 78 LEU B 84 -1 O ALA B 79 N CYS B 22 SHEET 4 AB4 4 ALA B 68 ASP B 73 -1 N THR B 71 O TYR B 80 SHEET 1 AB5 5 SER B 58 TYR B 60 0 SHEET 2 AB5 5 ASN B 44 ILE B 51 -1 N LEU B 50 O THR B 59 SHEET 3 AB5 5 TYR B 32 SER B 40 -1 N MET B 34 O ILE B 51 SHEET 4 AB5 5 ALA B 92 GLY B 100 -1 O ALA B 97 N ASN B 35 SHEET 5 AB5 5 VAL B 111 TRP B 112 -1 O VAL B 111 N ARG B 98 SHEET 1 AB6 5 SER B 58 TYR B 60 0 SHEET 2 AB6 5 ASN B 44 ILE B 51 -1 N LEU B 50 O THR B 59 SHEET 3 AB6 5 TYR B 32 SER B 40 -1 N MET B 34 O ILE B 51 SHEET 4 AB6 5 ALA B 92 GLY B 100 -1 O ALA B 97 N ASN B 35 SHEET 5 AB6 5 THR B 116 LEU B 118 -1 O THR B 116 N TYR B 94 SSBOND 1 CYS d 37 CYS d 73 1555 1555 2.03 SSBOND 2 CYS d 93 CYS d 96 1555 1555 2.02 SSBOND 3 CYS e 49 CYS e 98 1555 1555 2.03 SSBOND 4 CYS f 49 CYS f 98 1555 1555 2.03 SSBOND 5 CYS f 119 CYS f 122 1555 1555 2.03 SSBOND 6 CYS g 46 CYS g 87 1555 1555 2.03 SSBOND 7 CYS g 104 CYS g 107 1555 1555 2.04 SSBOND 8 CYS A 23 CYS A 88 1555 1555 2.03 SSBOND 9 CYS B 22 CYS B 96 1555 1555 2.03 LINK ND2 ASN d 38 C1 NAG d 202 1555 1555 1.47 LINK ND2 ASN d 74 C1 NAG d 201 1555 1555 1.44 CISPEP 1 LEU A 94 PRO A 95 0 -2.09 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