HEADER STRUCTURAL PROTEIN 28-JAN-25 9I5E TITLE A COILED COIL MODULE STRATEGY FOR HIGH-RESOLUTION CRYO-EM STRUCTURES TITLE 2 OF SMALL PROTEINS FOR DRUG DISCOVERY COMPND MOL_ID: 1; COMPND 2 MOLECULE: ISOFORM 2B OF GTPASE KRAS,APH2; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: K-RAS 2,KI-RAS,C-K-RAS,C-KI-RAS; COMPND 5 EC: 3.6.5.2; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: FUSION PROTEIN,FUSION PROTEIN; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: NANOBODY 26; COMPND 10 CHAIN: M, N; COMPND 11 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: KRAS, KRAS2, RASK2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CRYOEM IMAGING SCAFFOLD, CANCER, GTPASE, NANOBODIES, COILED-COIL, KEYWDS 2 STRUCTURAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR C.SAMSON,I.DOSSOU,A.STEINMETZ,A.KUMAR,M.MATHIEU,A.RAK REVDAT 1 12-NOV-25 9I5E 0 JRNL AUTH C.SAMSON,I.DOSSOU,A.STEINMETZ,A.KUMAR,M.MATHIEU,A.RAK JRNL TITL A COILED COIL MODULE STRATEGY FOR HIGH-RESOLUTION CRYO-EM JRNL TITL 2 STRUCTURES OF SMALL PROTEINS FOR DRUG DISCOVERY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.77 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) : 3.770 REMARK 3 NUMBER OF PARTICLES : 187753 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 9I5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1292144391. 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 : CRYO-EM STRUCTURE OF KRASG12C REMARK 245 FUSED TO THE APH2 COILED-COIL REMARK 245 IN COMPLEX WITH NANOBODY NB26 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 : 9509 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : DARK FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6000.00 REMARK 245 ILLUMINATION MODE : OTHER REMARK 245 NOMINAL MAGNIFICATION : 240000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, M, N, 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 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 ARG A 73 -2.03 67.97 REMARK 500 ARG M 27 -167.98 -161.69 REMARK 500 SER M 52 -158.58 -150.57 REMARK 500 ALA M 89 -169.34 -165.88 REMARK 500 ARG N 27 -167.80 -160.48 REMARK 500 SER N 52 -159.29 -150.83 REMARK 500 ARG B 73 -1.06 69.32 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 303 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 LYS A 16 O REMARK 620 2 SER A 17 N 55.2 REMARK 620 3 SER A 17 OG 116.3 68.4 REMARK 620 4 GDP A 302 O1B 130.8 138.8 110.4 REMARK 620 5 GDP A 302 O3A 69.8 118.3 173.3 64.7 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG B 302 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 LYS B 16 O REMARK 620 2 SER B 17 N 55.7 REMARK 620 3 SER B 17 OG 119.6 70.4 REMARK 620 4 GDP B 301 O1B 90.3 134.3 150.1 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-52628 RELATED DB: EMDB REMARK 900 A COILED COIL MODULE STRATEGY FOR HIGH-RESOLUTION CRYO-EM REMARK 900 STRUCTURES OF SMALL PROTEINS FOR DRUG DISCOVERY DBREF 9I5E A 1 164 UNP P01116 RASK_HUMAN 1 164 DBREF 9I5E A 165 204 PDB 9I5E 9I5E 165 204 DBREF 9I5E M 2 123 PDB 9I5E 9I5E 2 123 DBREF 9I5E N 2 123 PDB 9I5E 9I5E 2 123 DBREF 9I5E B 1 164 UNP P01116 RASK_HUMAN 1 164 DBREF 9I5E B 165 204 PDB 9I5E 9I5E 165 204 SEQADV 9I5E CYS A 12 UNP P01116 GLY 12 VARIANT SEQADV 9I5E CYS B 12 UNP P01116 GLY 12 VARIANT SEQRES 1 A 204 MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA CYS GLY SEQRES 2 A 204 VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN SEQRES 3 A 204 HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER SEQRES 4 A 204 TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU SEQRES 5 A 204 LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER SEQRES 6 A 204 ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE SEQRES 7 A 204 LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU SEQRES 8 A 204 ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL LYS SEQRES 9 A 204 ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN LYS SEQRES 10 A 204 CYS ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN ALA SEQRES 11 A 204 GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE GLU SEQRES 12 A 204 THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA PHE SEQRES 13 A 204 TYR THR LEU VAL ARG GLU ILE ARG LEU HIS LYS GLU LEU SEQRES 14 A 204 LYS GLN LEU GLU GLU GLU LEU GLN ALA ILE GLU GLU GLN SEQRES 15 A 204 LEU ALA GLN LEU GLN TRP LYS ALA GLN ALA ARG LYS GLU SEQRES 16 A 204 LYS LEU ALA GLN LEU LYS GLU LYS LEU SEQRES 1 M 122 VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN ALA SEQRES 2 M 122 GLY ASP SER LEU ARG LEU SER CYS ALA ALA SER GLY ARG SEQRES 3 M 122 THR PHE SER THR TYR PRO MET GLY TRP PHE ARG GLN ALA SEQRES 4 M 122 PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SER SER SER SEQRES 5 M 122 ARG ALA TYR TYR ALA ASP SER VAL LYS GLY ARG PHE THR SEQRES 6 M 122 ILE SER ARG ASN ASN ALA LYS ASN THR VAL TYR LEU GLN SEQRES 7 M 122 MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR TYR SEQRES 8 M 122 CYS VAL ALA ASP SER SER PRO TYR TYR ARG ARG TYR ASP SEQRES 9 M 122 ALA ALA GLN ASP TYR ASP TYR TRP GLY GLN GLY THR GLN SEQRES 10 M 122 VAL THR VAL SER SER SEQRES 1 N 122 VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN ALA SEQRES 2 N 122 GLY ASP SER LEU ARG LEU SER CYS ALA ALA SER GLY ARG SEQRES 3 N 122 THR PHE SER THR TYR PRO MET GLY TRP PHE ARG GLN ALA SEQRES 4 N 122 PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SER SER SER SEQRES 5 N 122 ARG ALA TYR TYR ALA ASP SER VAL LYS GLY ARG PHE THR SEQRES 6 N 122 ILE SER ARG ASN ASN ALA LYS ASN THR VAL TYR LEU GLN SEQRES 7 N 122 MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR TYR SEQRES 8 N 122 CYS VAL ALA ASP SER SER PRO TYR TYR ARG ARG TYR ASP SEQRES 9 N 122 ALA ALA GLN ASP TYR ASP TYR TRP GLY GLN GLY THR GLN SEQRES 10 N 122 VAL THR VAL SER SER SEQRES 1 B 204 MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA CYS GLY SEQRES 2 B 204 VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN SEQRES 3 B 204 HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER SEQRES 4 B 204 TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU SEQRES 5 B 204 LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER SEQRES 6 B 204 ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE SEQRES 7 B 204 LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU SEQRES 8 B 204 ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL LYS SEQRES 9 B 204 ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN LYS SEQRES 10 B 204 CYS ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN ALA SEQRES 11 B 204 GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE GLU SEQRES 12 B 204 THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA PHE SEQRES 13 B 204 TYR THR LEU VAL ARG GLU ILE ARG LEU HIS LYS GLU LEU SEQRES 14 B 204 LYS GLN LEU GLU GLU GLU LEU GLN ALA ILE GLU GLU GLN SEQRES 15 B 204 LEU ALA GLN LEU GLN TRP LYS ALA GLN ALA ARG LYS GLU SEQRES 16 B 204 LYS LEU ALA GLN LEU LYS GLU LYS LEU HET M1X A 301 43 HET GDP A 302 28 HET MG A 303 1 HET GDP B 301 28 HET MG B 302 1 HET M1X B 303 43 HETNAM M1X {(2S)-4-[7-(8-CHLORONAPHTHALEN-1-YL)-2-{[(2S)-1- HETNAM 2 M1X METHYLPYRROLIDIN-2-YL]METHOXY}-5,6,7,8- HETNAM 3 M1X TETRAHYDROPYRIDO[3,4-D]PYRIMIDIN-4-YL]-1-[(2S)-2- HETNAM 4 M1X FLUOROPROPANOYL]PIPERAZIN-2-YL}ACETONITRILE HETNAM GDP GUANOSINE-5'-DIPHOSPHATE HETNAM MG MAGNESIUM ION FORMUL 5 M1X 2(C32 H37 CL F N7 O2) FORMUL 6 GDP 2(C10 H15 N5 O11 P2) FORMUL 7 MG 2(MG 2+) HELIX 1 AA1 ALA A 18 ASN A 26 1 9 HELIX 2 AA2 SER A 65 MET A 72 1 8 HELIX 3 AA3 ASN A 86 ASP A 105 1 20 HELIX 4 AA4 ASP A 126 GLY A 138 1 13 HELIX 5 AA5 GLY A 151 LEU A 204 1 54 HELIX 6 AA6 LYS M 84 THR M 88 5 5 HELIX 7 AA7 ALA M 106 TYR M 110 5 5 HELIX 8 AA8 LYS N 84 THR N 88 5 5 HELIX 9 AA9 ALA B 18 ASN B 26 1 9 HELIX 10 AB1 SER B 65 MET B 72 1 8 HELIX 11 AB2 ASN B 86 ASP B 105 1 20 HELIX 12 AB3 ASP B 126 GLY B 138 1 13 HELIX 13 AB4 GLY B 151 LEU B 204 1 54 SHEET 1 AA1 6 SER A 39 ILE A 46 0 SHEET 2 AA1 6 GLU A 49 ASP A 57 -1 O LEU A 53 N LYS A 42 SHEET 3 AA1 6 GLU A 3 VAL A 9 1 N LEU A 6 O ASP A 54 SHEET 4 AA1 6 GLY A 77 PHE A 82 1 O LEU A 79 N VAL A 7 SHEET 5 AA1 6 MET A 111 ASN A 116 1 O VAL A 112 N CYS A 80 SHEET 6 AA1 6 PHE A 141 THR A 144 1 O THR A 144 N GLY A 115 SHEET 1 AA2 4 LEU M 4 SER M 7 0 SHEET 2 AA2 4 LEU M 18 ALA M 24 -1 O ALA M 23 N GLN M 5 SHEET 3 AA2 4 THR M 75 MET M 80 -1 O LEU M 78 N LEU M 20 SHEET 4 AA2 4 PHE M 65 ASN M 70 -1 N THR M 66 O GLN M 79 SHEET 1 AA3 6 GLY M 10 GLN M 13 0 SHEET 2 AA3 6 THR M 117 SER M 122 1 O THR M 120 N VAL M 12 SHEET 3 AA3 6 ALA M 89 ALA M 95 -1 N ALA M 89 O VAL M 119 SHEET 4 AA3 6 MET M 34 GLN M 39 -1 N GLY M 35 O VAL M 94 SHEET 5 AA3 6 GLU M 46 SER M 51 -1 O SER M 51 N MET M 34 SHEET 6 AA3 6 TYR M 56 TYR M 57 -1 O TYR M 56 N ALA M 50 SHEET 1 AA4 4 GLY M 10 GLN M 13 0 SHEET 2 AA4 4 THR M 117 SER M 122 1 O THR M 120 N VAL M 12 SHEET 3 AA4 4 ALA M 89 ALA M 95 -1 N ALA M 89 O VAL M 119 SHEET 4 AA4 4 TYR M 112 TRP M 113 -1 O TYR M 112 N ALA M 95 SHEET 1 AA5 4 LEU N 4 SER N 7 0 SHEET 2 AA5 4 LEU N 18 ALA N 24 -1 O SER N 21 N SER N 7 SHEET 3 AA5 4 THR N 75 MET N 80 -1 O LEU N 78 N LEU N 20 SHEET 4 AA5 4 THR N 66 ASN N 70 -1 N ASN N 70 O THR N 75 SHEET 1 AA6 6 GLY N 10 GLN N 13 0 SHEET 2 AA6 6 THR N 117 SER N 122 1 O THR N 120 N VAL N 12 SHEET 3 AA6 6 ALA N 89 ALA N 95 -1 N ALA N 89 O VAL N 119 SHEET 4 AA6 6 MET N 34 GLN N 39 -1 N GLY N 35 O VAL N 94 SHEET 5 AA6 6 GLU N 46 SER N 51 -1 O SER N 51 N MET N 34 SHEET 6 AA6 6 TYR N 56 TYR N 57 -1 O TYR N 56 N ALA N 50 SHEET 1 AA7 4 GLY N 10 GLN N 13 0 SHEET 2 AA7 4 THR N 117 SER N 122 1 O THR N 120 N VAL N 12 SHEET 3 AA7 4 ALA N 89 ALA N 95 -1 N ALA N 89 O VAL N 119 SHEET 4 AA7 4 TYR N 112 TRP N 113 -1 O TYR N 112 N ALA N 95 SHEET 1 AA8 6 SER B 39 ILE B 46 0 SHEET 2 AA8 6 GLU B 49 ASP B 57 -1 O LEU B 53 N LYS B 42 SHEET 3 AA8 6 GLU B 3 VAL B 9 1 N LEU B 6 O ASP B 54 SHEET 4 AA8 6 GLY B 77 PHE B 82 1 O LEU B 79 N VAL B 7 SHEET 5 AA8 6 MET B 111 ASN B 116 1 O VAL B 112 N CYS B 80 SHEET 6 AA8 6 PHE B 141 THR B 144 1 O THR B 144 N GLY B 115 SSBOND 1 CYS M 22 CYS M 93 1555 1555 2.04 SSBOND 2 CYS N 22 CYS N 93 1555 1555 2.03 LINK SG CYS A 12 C39 M1X A 301 1555 1555 1.77 LINK SG CYS B 12 C39 M1X B 303 1555 1555 1.77 LINK O LYS A 16 MG MG A 303 1555 1555 2.03 LINK N SER A 17 MG MG A 303 1555 1555 2.68 LINK OG SER A 17 MG MG A 303 1555 1555 2.18 LINK O1B GDP A 302 MG MG A 303 1555 1555 2.22 LINK O3A GDP A 302 MG MG A 303 1555 1555 2.62 LINK O LYS B 16 MG MG B 302 1555 1555 2.03 LINK N SER B 17 MG MG B 302 1555 1555 2.65 LINK OG SER B 17 MG MG B 302 1555 1555 2.09 LINK O1B GDP B 301 MG MG B 302 1555 1555 1.95 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