HEADER IMMUNE SYSTEM 14-MAR-25 9NRJ TITLE ABTCR BOUND TO SAR444200, A NOVEL ANTI-GPC3 T-CELL ENGAGER, FOR THE TITLE 2 TREATMENT OF GPC3+ SOLID TUMORS CAVEAT 9NRJ VAL A 152 HAS WRONG CHIRALITY AT ATOM CA ILE A 192 HAS WRONG CAVEAT 2 9NRJ CHIRALITY AT ATOM CB ILE T 31 HAS WRONG CHIRALITY AT ATOM CAVEAT 3 9NRJ CB ILE T 53 HAS WRONG CHIRALITY AT ATOM CB NAG D 1 HAS CAVEAT 4 9NRJ WRONG CHIRALITY AT ATOM C1 NAG F 1 HAS WRONG CHIRALITY AT CAVEAT 5 9NRJ ATOM C1 ENTRY CONTAINS MULTIPLE IMPROPER PEPTIDE LINKAGES. COMPND MOL_ID: 1; COMPND 2 MOLECULE: M1-SPECIFIC T CELL RECEPTOR ALPHA CHAIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: TR ALPHA CHAIN TRAV27*01J42*01C*01; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: M1-SPECIFIC T CELL RECEPTOR BETA CHAIN; COMPND 8 CHAIN: B; COMPND 9 SYNONYM: TR BETA CHAIN TRBV19*01J2S7*01C*02; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: 2C04; COMPND 13 CHAIN: C; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: TCE01; COMPND 17 CHAIN: T; COMPND 18 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: TRA; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: TRB; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 24 MOL_ID: 4; SOURCE 25 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 26 ORGANISM_COMMON: HUMAN; SOURCE 27 ORGANISM_TAXID: 9606; SOURCE 28 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 29 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 30 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS TCR, T-CELL RECEPTOR, NANOBODY, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR E.SVIDRITSKIY,Y.QIU,Z.YANFENG REVDAT 1 15-OCT-25 9NRJ 0 JRNL AUTH P.MEONI,A.P.B.VINTEM,V.F.CORTEZ-RETAMOZO,J.JACOBS, JRNL AUTH 2 E.DE TAVERNIER,P.FIORENTINI,D.VAN HOORICK,J.D.BATCHELOR, JRNL AUTH 3 E.SVIDRITSKIY,Y.QIU,E.DEJONCKHEERE,A.LI,L.I.PAO,M.A.BUYSE JRNL TITL IDENTIFICATION AND NON-CLINICAL CHARACTERIZATION OF JRNL TITL 2 SAR444200, A NOVEL ANTI-GPC3 NANOBODY® T-CELL ENGAGER, JRNL TITL 3 FOR THE TREATMENT OF GPC3+ SOLID TUMORS. JRNL REF MOL.CANCER THER. 2025 JRNL REFN ESSN 1538-8514 JRNL PMID 41041827 JRNL DOI 10.1158/1535-7163.MCT-24-1049 REMARK 2 REMARK 2 RESOLUTION. 3.40 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) : 3.400 REMARK 3 NUMBER OF PARTICLES : 95366 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 9NRJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1000294079. 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 : 2D ARRAY REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : TCRAB 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 : 7.40 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 K2 QUANTUM (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1200.00 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) : 8000.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, T, 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 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 ASP A 151 OG SER A 176 1.32 REMARK 500 O VAL A 152 O TRP A 175 1.64 REMARK 500 OD1 ASP A 151 OG SER A 176 1.71 REMARK 500 C ASP A 151 OG SER A 176 1.74 REMARK 500 NZ LYS A 126 O VAL B 127 1.84 REMARK 500 O ASP A 151 CB SER A 176 1.86 REMARK 500 O TYR B 35 N ALA B 94 1.92 REMARK 500 O ASP A 151 N ASN A 177 1.94 REMARK 500 O ASP A 151 CA SER A 176 1.98 REMARK 500 CE1 TYR A 120 CA GLU B 134 2.00 REMARK 500 O TYR A 153 CA ALA A 174 2.00 REMARK 500 OG1 THR A 155 O VAL A 173 2.06 REMARK 500 OE1 GLN A 14 NE2 GLN C 44 2.15 REMARK 500 N CYS T 22 O VAL T 78 2.18 REMARK 500 N TYR B 37 O LEU B 92 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLN A 2 N GLN A 2 CA 0.249 REMARK 500 PRO A 8 CA PRO A 8 CB 0.164 REMARK 500 SER A 12 CA SER A 12 CB 0.137 REMARK 500 GLU A 17 C GLU A 17 O -0.124 REMARK 500 GLU A 17 C ASN A 18 N -0.155 REMARK 500 VAL A 21 CA VAL A 21 C -0.199 REMARK 500 SER A 30 CA SER A 30 CB -0.100 REMARK 500 SER A 30 C SER A 30 O 0.178 REMARK 500 LEU A 32 C GLN A 33 N -0.138 REMARK 500 LYS A 56 C LYS A 57 N -0.140 REMARK 500 LEU A 61 C THR A 62 N -0.145 REMARK 500 THR A 62 C PHE A 63 N -0.158 REMARK 500 SER A 72 CB SER A 72 OG 0.113 REMARK 500 SER A 73 CB SER A 73 OG 0.089 REMARK 500 HIS A 75 NE2 HIS A 75 CD2 -0.114 REMARK 500 ILE A 76 C THR A 77 N -0.171 REMARK 500 GLY A 82 C GLY A 82 O 0.172 REMARK 500 TYR A 87 CG TYR A 87 CD1 -0.112 REMARK 500 TYR A 87 CZ TYR A 87 CE2 -0.120 REMARK 500 ALA A 90 CA ALA A 90 CB 0.217 REMARK 500 PHE A 100 CG PHE A 100 CD2 0.096 REMARK 500 SER A 107 N SER A 107 CA -0.122 REMARK 500 SER A 107 CA SER A 107 CB -0.123 REMARK 500 LYS A 109 CB LYS A 109 CG 0.165 REMARK 500 LYS A 109 CA LYS A 109 C -0.185 REMARK 500 LYS A 109 C PRO A 110 N -0.115 REMARK 500 PRO A 110 CA PRO A 110 CB -0.138 REMARK 500 PRO A 110 CD PRO A 110 N -0.137 REMARK 500 ASP A 116 CG ASP A 116 OD2 0.189 REMARK 500 VAL A 119 CA VAL A 119 CB -0.128 REMARK 500 TYR A 120 CG TYR A 120 CD2 -0.085 REMARK 500 ARG A 123 C ARG A 123 O 0.227 REMARK 500 ASP A 124 CG ASP A 124 OD2 0.194 REMARK 500 VAL A 132 CB VAL A 132 CG2 0.182 REMARK 500 VAL A 132 C VAL A 132 O 0.196 REMARK 500 CYS A 133 C CYS A 133 O 0.135 REMARK 500 SER A 140 CA SER A 140 CB -0.145 REMARK 500 SER A 147 CB SER A 147 OG 0.174 REMARK 500 ASP A 151 C ASP A 151 O 0.323 REMARK 500 ASP A 151 C VAL A 152 N 0.230 REMARK 500 VAL A 152 C VAL A 152 O 0.408 REMARK 500 VAL A 152 C TYR A 153 N 0.142 REMARK 500 TYR A 153 CA TYR A 153 C 0.159 REMARK 500 TYR A 153 C TYR A 153 O 0.344 REMARK 500 ILE A 154 C ILE A 154 O 0.146 REMARK 500 CYS A 158 C CYS A 158 O 0.197 REMARK 500 LYS A 168 N LYS A 168 CA -0.127 REMARK 500 VAL A 173 C VAL A 173 O 0.140 REMARK 500 ALA A 174 CA ALA A 174 CB 0.143 REMARK 500 ALA A 174 C ALA A 174 O 0.138 REMARK 500 REMARK 500 THIS ENTRY HAS 178 BOND DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLN A 2 CA - C - O ANGL. DEV. = -16.9 DEGREES REMARK 500 SER A 7 N - CA - C ANGL. DEV. = -17.8 DEGREES REMARK 500 PHE A 10 CB - CA - C ANGL. DEV. = -20.6 DEGREES REMARK 500 PHE A 10 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES REMARK 500 PHE A 10 O - C - N ANGL. DEV. = -10.6 DEGREES REMARK 500 LEU A 11 CB - CA - C ANGL. DEV. = 26.5 DEGREES REMARK 500 ILE A 13 CB - CA - C ANGL. DEV. = -26.8 DEGREES REMARK 500 GLU A 17 CB - CG - CD ANGL. DEV. = 18.2 DEGREES REMARK 500 ASN A 18 O - C - N ANGL. DEV. = -10.8 DEGREES REMARK 500 LEU A 19 CB - CA - C ANGL. DEV. = -12.0 DEGREES REMARK 500 LEU A 19 CB - CG - CD1 ANGL. DEV. = -10.3 DEGREES REMARK 500 THR A 20 CA - CB - OG1 ANGL. DEV. = 13.9 DEGREES REMARK 500 VAL A 21 CG1 - CB - CG2 ANGL. DEV. = -18.0 DEGREES REMARK 500 VAL A 21 CA - CB - CG2 ANGL. DEV. = 12.3 DEGREES REMARK 500 TYR A 22 CB - CA - C ANGL. DEV. = -13.6 DEGREES REMARK 500 TYR A 22 N - CA - CB ANGL. DEV. = 15.9 DEGREES REMARK 500 ASN A 24 C - N - CA ANGL. DEV. = -18.4 DEGREES REMARK 500 VAL A 28 CA - CB - CG2 ANGL. DEV. = 14.6 DEGREES REMARK 500 PHE A 29 CB - CA - C ANGL. DEV. = -16.3 DEGREES REMARK 500 SER A 30 CA - C - N ANGL. DEV. = -13.8 DEGREES REMARK 500 SER A 30 O - C - N ANGL. DEV. = 9.7 DEGREES REMARK 500 SER A 31 C - N - CA ANGL. DEV. = -19.3 DEGREES REMARK 500 SER A 31 O - C - N ANGL. DEV. = 14.5 DEGREES REMARK 500 LEU A 32 C - N - CA ANGL. DEV. = -16.6 DEGREES REMARK 500 LEU A 32 N - CA - CB ANGL. DEV. = 14.4 DEGREES REMARK 500 LEU A 32 CB - CG - CD2 ANGL. DEV. = 14.1 DEGREES REMARK 500 GLN A 33 CB - CA - C ANGL. DEV. = -18.9 DEGREES REMARK 500 TYR A 35 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES REMARK 500 TYR A 35 CB - CG - CD1 ANGL. DEV. = 6.2 DEGREES REMARK 500 TYR A 35 CG - CD1 - CE1 ANGL. DEV. = 7.9 DEGREES REMARK 500 TYR A 35 CD1 - CE1 - CZ ANGL. DEV. = -6.0 DEGREES REMARK 500 ARG A 36 CB - CA - C ANGL. DEV. = -12.9 DEGREES REMARK 500 ARG A 36 N - CA - C ANGL. DEV. = -24.4 DEGREES REMARK 500 PRO A 39 CA - N - CD ANGL. DEV. = 10.3 DEGREES REMARK 500 GLU A 41 N - CA - CB ANGL. DEV. = 12.6 DEGREES REMARK 500 GLY A 42 C - N - CA ANGL. DEV. = -15.1 DEGREES REMARK 500 PRO A 43 C - N - CD ANGL. DEV. = -15.2 DEGREES REMARK 500 VAL A 44 CB - CA - C ANGL. DEV. = -12.4 DEGREES REMARK 500 VAL A 47 C - N - CA ANGL. DEV. = -18.9 DEGREES REMARK 500 VAL A 47 CB - CA - C ANGL. DEV. = -19.7 DEGREES REMARK 500 VAL A 47 CG1 - CB - CG2 ANGL. DEV. = -11.0 DEGREES REMARK 500 THR A 48 N - CA - C ANGL. DEV. = -19.3 DEGREES REMARK 500 LYS A 57 CB - CA - C ANGL. DEV. = 15.7 DEGREES REMARK 500 PHE A 63 CB - CA - C ANGL. DEV. = -18.1 DEGREES REMARK 500 GLN A 64 CB - CA - C ANGL. DEV. = -14.3 DEGREES REMARK 500 PHE A 65 CB - CG - CD2 ANGL. DEV. = -7.5 DEGREES REMARK 500 ARG A 69 CB - CG - CD ANGL. DEV. = 22.7 DEGREES REMARK 500 ARG A 69 CG - CD - NE ANGL. DEV. = -13.6 DEGREES REMARK 500 ASP A 71 CA - CB - CG ANGL. DEV. = 16.8 DEGREES REMARK 500 SER A 73 O - C - N ANGL. DEV. = 10.9 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 845 ANGLE DEVIATIONS. 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 PRO A 8 167.06 -25.07 REMARK 500 ILE A 13 156.40 173.77 REMARK 500 GLU A 15 121.84 -37.89 REMARK 500 SER A 27 129.94 107.89 REMARK 500 VAL A 47 -179.34 177.96 REMARK 500 VAL A 50 -58.01 -122.77 REMARK 500 LYS A 59 -139.69 75.11 REMARK 500 ALA A 78 102.92 68.33 REMARK 500 ALA A 92 140.63 -39.44 REMARK 500 GLN A 95 7.28 179.73 REMARK 500 SER A 128 157.21 179.94 REMARK 500 ASP A 137 12.71 59.84 REMARK 500 ASP A 151 21.81 171.97 REMARK 500 TYR A 153 118.29 51.78 REMARK 500 MET A 162 77.39 -104.26 REMARK 500 SER A 164 -2.85 96.08 REMARK 500 SER A 169 116.55 -163.56 REMARK 500 SER A 179 -163.94 54.09 REMARK 500 ILE B 48 -78.07 -95.41 REMARK 500 ASN B 55 -14.46 63.04 REMARK 500 ALA B 63 1.87 156.44 REMARK 500 LYS B 72 133.55 53.77 REMARK 500 LYS B 73 2.85 -62.37 REMARK 500 SER B 82 141.69 37.45 REMARK 500 LYS B 85 21.79 129.93 REMARK 500 ASN B 86 74.74 57.01 REMARK 500 ALA B 89 -154.62 -160.90 REMARK 500 ARG B 98 97.10 -52.30 REMARK 500 SER B 99 -26.93 -151.47 REMARK 500 TYR B 101 68.84 72.68 REMARK 500 ASP B 116 -164.79 -117.75 REMARK 500 LEU B 117 14.35 -155.72 REMARK 500 ALA B 141 110.68 -165.54 REMARK 500 ASP B 153 43.29 -66.95 REMARK 500 ASN B 162 42.72 13.04 REMARK 500 PRO B 174 -80.81 -58.10 REMARK 500 PRO B 176 131.28 -35.49 REMARK 500 GLN B 180 78.51 76.00 REMARK 500 ASP B 185 50.27 80.88 REMARK 500 PRO B 204 21.69 -75.29 REMARK 500 SER B 218 -100.51 -69.59 REMARK 500 GLU B 219 132.42 -177.54 REMARK 500 ASN B 220 59.93 70.53 REMARK 500 GLU B 222 171.36 117.82 REMARK 500 TRP B 223 102.31 168.22 REMARK 500 GLN B 225 -170.28 -46.05 REMARK 500 ALA B 228 152.38 -44.72 REMARK 500 CYS C 22 112.16 -162.95 REMARK 500 ILE C 31 -157.94 -79.59 REMARK 500 HIS C 32 -50.28 -171.93 REMARK 500 REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLN A 2 LEU A 3 146.46 REMARK 500 SER A 7 PRO A 8 -41.33 REMARK 500 GLU A 38 PRO A 39 -146.87 REMARK 500 PRO A 43 VAL A 44 -148.20 REMARK 500 CYS A 89 ALA A 90 149.42 REMARK 500 GLY A 96 ASN A 97 141.13 REMARK 500 LYS A 105 LEU A 106 146.61 REMARK 500 ALA A 118 VAL A 119 139.82 REMARK 500 VAL A 152 TYR A 153 -149.67 REMARK 500 SER A 171 ALA A 172 149.65 REMARK 500 SER A 179 ASP A 180 141.18 REMARK 500 PHE A 198 PRO A 199 -146.95 REMARK 500 LYS B 16 GLU B 17 -145.65 REMARK 500 GLN B 19 ASN B 20 149.30 REMARK 500 ASN B 20 VAL B 21 149.36 REMARK 500 LEU B 45 ARG B 46 147.64 REMARK 500 ILE B 53 VAL B 54 -145.12 REMARK 500 LYS B 72 LYS B 73 135.59 REMARK 500 GLN B 84 LYS B 85 -149.99 REMARK 500 PRO B 87 THR B 88 144.90 REMARK 500 SER B 96 SER B 97 141.97 REMARK 500 GLU B 102 GLN B 103 -147.55 REMARK 500 LYS B 118 ASN B 119 -148.38 REMARK 500 GLU B 129 PRO B 130 -137.83 REMARK 500 THR B 142 LEU B 143 147.89 REMARK 500 VAL B 161 ASN B 162 -147.74 REMARK 500 ASN B 162 GLY B 163 143.88 REMARK 500 GLN B 175 PRO B 176 148.63 REMARK 500 LEU B 183 ASN B 184 149.79 REMARK 500 TYR B 215 GLY B 216 -144.91 REMARK 500 ASN B 220 ASP B 221 143.42 REMARK 500 GLN B 225 ASP B 226 -136.98 REMARK 500 SER C 7 GLY C 8 143.61 REMARK 500 VAL C 29 GLY C 30 149.36 REMARK 500 GLY C 30 ILE C 31 -130.08 REMARK 500 ASP C 61 PHE C 62 -139.82 REMARK 500 VAL C 63 LYS C 64 120.04 REMARK 500 ARG C 71 ASP C 72 -144.98 REMARK 500 SER C 114 SER C 115 147.74 REMARK 500 ASP T 1 VAL T 2 137.18 REMARK 500 VAL T 2 GLN T 3 -140.33 REMARK 500 GLY T 9 GLY T 10 -148.29 REMARK 500 GLY T 10 VAL T 11 -107.25 REMARK 500 VAL T 23 ALA T 24 -142.72 REMARK 500 VAL T 28 HIS T 29 146.77 REMARK 500 HIS T 29 LYS T 30 -148.81 REMARK 500 LYS T 30 ILE T 31 -147.00 REMARK 500 GLY T 54 ASP T 55 145.31 REMARK 500 TYR T 59 ALA T 60 -131.65 REMARK 500 ALA T 60 ASP T 61 139.07 REMARK 500 REMARK 500 THIS ENTRY HAS 60 NON CIS, NON-TRANS OMEGA OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 TYR A 35 0.09 SIDE CHAIN REMARK 500 ARG A 60 0.08 SIDE CHAIN REMARK 500 TYR A 87 0.13 SIDE CHAIN REMARK 500 TYR A 120 0.10 SIDE CHAIN REMARK 500 PHE A 181 0.12 SIDE CHAIN REMARK 500 PHE A 197 0.11 SIDE CHAIN REMARK 500 PHE A 198 0.11 SIDE CHAIN REMARK 500 TYR B 12 0.05 SIDE CHAIN REMARK 500 PHE B 14 0.09 SIDE CHAIN REMARK 500 GLN B 19 0.07 SIDE CHAIN REMARK 500 ASN B 28 0.08 SIDE CHAIN REMARK 500 TYR B 35 0.08 SIDE CHAIN REMARK 500 TYR B 37 0.10 SIDE CHAIN REMARK 500 TYR B 50 0.08 SIDE CHAIN REMARK 500 TYR B 66 0.10 SIDE CHAIN REMARK 500 ARG B 70 0.07 SIDE CHAIN REMARK 500 GLN B 84 0.14 SIDE CHAIN REMARK 500 TYR B 91 0.19 SIDE CHAIN REMARK 500 PHE B 105 0.11 SIDE CHAIN REMARK 500 PHE B 128 0.10 SIDE CHAIN REMARK 500 HIS B 137 0.08 SIDE CHAIN REMARK 500 ASN B 162 0.10 SIDE CHAIN REMARK 500 TYR B 188 0.08 SIDE CHAIN REMARK 500 PHE B 200 0.13 SIDE CHAIN REMARK 500 ASN B 206 0.07 SIDE CHAIN REMARK 500 ARG B 209 0.08 SIDE CHAIN REMARK 500 TYR B 215 0.10 SIDE CHAIN REMARK 500 GLN B 225 0.10 SIDE CHAIN REMARK 500 TYR C 37 0.12 SIDE CHAIN REMARK 500 HIS C 58 0.11 SIDE CHAIN REMARK 500 TYR C 93 0.09 SIDE CHAIN REMARK 500 PHE C 97 0.07 SIDE CHAIN REMARK 500 ASN C 98 0.07 SIDE CHAIN REMARK 500 TYR C 104 0.07 SIDE CHAIN REMARK 500 HIS T 29 0.07 SIDE CHAIN REMARK 500 TYR T 34 0.08 SIDE CHAIN REMARK 500 TYR T 37 0.07 SIDE CHAIN REMARK 500 ARG T 45 0.10 SIDE CHAIN REMARK 500 ARG T 71 0.07 SIDE CHAIN REMARK 500 TYR T 79 0.07 SIDE CHAIN REMARK 500 TYR T 94 0.12 SIDE CHAIN REMARK 500 ARG T 100 0.17 SIDE CHAIN REMARK 500 TYR T 104 0.11 SIDE CHAIN REMARK 500 TYR T 106 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 SER A 7 -18.48 REMARK 500 GLN A 9 -13.56 REMARK 500 PHE A 10 19.98 REMARK 500 LEU A 11 -15.02 REMARK 500 SER A 12 -22.22 REMARK 500 ILE A 13 15.79 REMARK 500 GLU A 17 -18.29 REMARK 500 ASN A 18 -18.61 REMARK 500 LEU A 19 -12.56 REMARK 500 VAL A 21 -15.65 REMARK 500 GLN A 33 -17.45 REMARK 500 TRP A 34 -24.48 REMARK 500 GLN A 37 17.79 REMARK 500 GLU A 41 10.56 REMARK 500 PRO A 43 18.09 REMARK 500 LEU A 46 -10.05 REMARK 500 GLU A 54 -17.99 REMARK 500 LYS A 56 -14.32 REMARK 500 LYS A 57 -17.54 REMARK 500 ARG A 60 10.85 REMARK 500 THR A 62 11.04 REMARK 500 GLY A 66 -11.61 REMARK 500 LEU A 74 15.35 REMARK 500 PRO A 81 17.63 REMARK 500 GLY A 85 15.71 REMARK 500 TYR A 87 28.52 REMARK 500 LEU A 88 -13.30 REMARK 500 CYS A 89 -27.35 REMARK 500 ALA A 90 -16.06 REMARK 500 ILE A 99 14.26 REMARK 500 LYS A 105 14.21 REMARK 500 LYS A 109 -23.47 REMARK 500 PRO A 110 18.01 REMARK 500 ASN A 111 10.12 REMARK 500 GLN A 121 -10.86 REMARK 500 PHE A 135 15.82 REMARK 500 GLN A 141 10.39 REMARK 500 VAL A 144 15.56 REMARK 500 THR A 155 -11.81 REMARK 500 LEU A 160 -14.18 REMARK 500 SER A 171 -21.18 REMARK 500 PHE A 181 -15.41 REMARK 500 ALA A 184 20.17 REMARK 500 ALA A 186 23.85 REMARK 500 ILE A 191 17.84 REMARK 500 ILE A 192 -14.16 REMARK 500 GLU A 194 -17.93 REMARK 500 THR A 196 12.57 REMARK 500 PHE A 197 11.74 REMARK 500 PHE A 198 16.09 REMARK 500 REMARK 500 THIS ENTRY HAS 160 MAIN CHAIN PLANARITY DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-49735 RELATED DB: EMDB REMARK 900 ABTCR BOUND TO SAR444200, A NOVEL ANTI-GPC3 T-CELL ENGAGER, FOR THE REMARK 900 TREATMENT OF GPC3+ SOLID TUMORS DBREF 9NRJ A 2 200 UNP P0DSE1 TRAR1_HUMAN 20 217 DBREF 9NRJ B 3 244 UNP P0DSE2 TRBR1_HUMAN 20 261 DBREF 9NRJ C 2 115 PDB 9NRJ 9NRJ 2 115 DBREF 9NRJ T 1 117 PDB 9NRJ 9NRJ 1 117 SEQADV 9NRJ ALA A 92 UNP P0DSE1 GLY 110 CONFLICT SEQADV 9NRJ ASN A 111 UNP P0DSE1 INSERTION SEQADV 9NRJ CYS A 158 UNP P0DSE1 THR 175 CONFLICT SEQADV 9NRJ SER B 97 UNP P0DSE2 ILE 114 CONFLICT SEQADV 9NRJ GLU B 124 UNP P0DSE2 LYS 141 CONFLICT SEQADV 9NRJ CYS B 171 UNP P0DSE2 SER 188 CONFLICT SEQADV 9NRJ SER B 189 UNP P0DSE2 CYS 206 CONFLICT SEQRES 1 A 199 GLN LEU LEU GLU GLN SER PRO GLN PHE LEU SER ILE GLN SEQRES 2 A 199 GLU GLY GLU ASN LEU THR VAL TYR CYS ASN SER SER SER SEQRES 3 A 199 VAL PHE SER SER LEU GLN TRP TYR ARG GLN GLU PRO GLY SEQRES 4 A 199 GLU GLY PRO VAL LEU LEU VAL THR VAL VAL THR GLY GLY SEQRES 5 A 199 GLU VAL LYS LYS LEU LYS ARG LEU THR PHE GLN PHE GLY SEQRES 6 A 199 ASP ALA ARG LYS ASP SER SER LEU HIS ILE THR ALA ALA SEQRES 7 A 199 GLN PRO GLY ASP THR GLY LEU TYR LEU CYS ALA GLY ALA SEQRES 8 A 199 GLY SER GLN GLY ASN LEU ILE PHE GLY LYS GLY THR LYS SEQRES 9 A 199 LEU SER VAL LYS PRO ASN ILE GLN ASN PRO ASP PRO ALA SEQRES 10 A 199 VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER SEQRES 11 A 199 VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL SEQRES 12 A 199 SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS SEQRES 13 A 199 CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN SEQRES 14 A 199 SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS SEQRES 15 A 199 ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR SEQRES 16 A 199 PHE PHE PRO SER SEQRES 1 B 242 ASP GLY GLY ILE THR GLN SER PRO LYS TYR LEU PHE ARG SEQRES 2 B 242 LYS GLU GLY GLN ASN VAL THR LEU SER CYS GLU GLN ASN SEQRES 3 B 242 LEU ASN HIS ASP ALA MET TYR TRP TYR ARG GLN ASP PRO SEQRES 4 B 242 GLY GLN GLY LEU ARG LEU ILE TYR TYR SER GLN ILE VAL SEQRES 5 B 242 ASN ASP PHE GLN LYS GLY ASP ILE ALA GLU GLY TYR SER SEQRES 6 B 242 VAL SER ARG GLU LYS LYS GLU SER PHE PRO LEU THR VAL SEQRES 7 B 242 THR SER ALA GLN LYS ASN PRO THR ALA PHE TYR LEU CYS SEQRES 8 B 242 ALA SER SER SER ARG SER SER TYR GLU GLN TYR PHE GLY SEQRES 9 B 242 PRO GLY THR ARG LEU THR VAL THR GLU ASP LEU LYS ASN SEQRES 10 B 242 VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU SEQRES 11 B 242 ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS SEQRES 12 B 242 LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER SEQRES 13 B 242 TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS SEQRES 14 B 242 THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN SEQRES 15 B 242 ASP SER ARG TYR SER LEU SER SER ARG LEU ARG VAL SER SEQRES 16 B 242 ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG CYS SEQRES 17 B 242 GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP SEQRES 18 B 242 THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER SEQRES 19 B 242 ALA GLU ALA TRP GLY ARG ALA ASP SEQRES 1 C 114 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN ALA SEQRES 2 C 114 GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SER SEQRES 3 C 114 ILE VAL GLY ILE HIS SER VAL GLY TRP TYR ARG GLN VAL SEQRES 4 C 114 PRO GLY ARG GLN ARG GLU LEU VAL ALA THR ILE VAL THR SEQRES 5 C 114 ASP THR GLY THR HIS TYR ARG ASP PHE VAL LYS GLY ARG SEQRES 6 C 114 PHE THR ILE SER ARG ASP ILE ALA LYS ASN THR LEU TYR SEQRES 7 C 114 LEU GLN MET ASN SER LEU GLN PRO GLU ASP THR ALA VAL SEQRES 8 C 114 TYR TYR CYS TYR PHE ASN LEU ILE ARG GLY ARG TYR TRP SEQRES 9 C 114 ALA GLN GLY THR LEU VAL THR VAL SER SER SEQRES 1 T 117 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 T 117 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 T 117 TYR VAL HIS LYS ILE ASN PHE TYR GLY TRP TYR ARG GLN SEQRES 4 T 117 ALA PRO GLY LYS GLU ARG GLU LYS VAL ALA HIS ILE SER SEQRES 5 T 117 ILE GLY ASP GLN THR ASP TYR ALA ASP SER ALA LYS GLY SEQRES 6 T 117 ARG PHE THR ILE SER ARG ASP GLU SER LYS ASN THR VAL SEQRES 7 T 117 TYR LEU GLN MET ASN SER LEU ARG PRO GLU ASP THR ALA SEQRES 8 T 117 ALA TYR TYR CYS ARG ALA LEU SER ARG ILE TRP PRO TYR SEQRES 9 T 117 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER HET NAG D 1 14 HET NAG D 2 14 HET FUC D 3 10 HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET NAG F 1 14 HET NAG F 2 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE 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 HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 5 NAG 6(C8 H15 N O6) FORMUL 5 FUC C6 H12 O5 FORMUL 6 BMA C6 H12 O6 HELIX 1 AA1 GLN A 80 THR A 84 5 5 HELIX 2 AA2 SER B 131 GLN B 139 1 9 HELIX 3 AA3 ALA B 198 GLN B 202 1 5 HELIX 4 AA4 GLN C 86 THR C 90 5 5 HELIX 5 AA5 ARG T 86 THR T 90 5 5 SHEET 1 AA1 5 GLU A 5 SER A 7 0 SHEET 2 AA1 5 LEU A 19 ASN A 24 -1 O ASN A 24 N GLU A 5 SHEET 3 AA1 5 ASP A 71 ILE A 76 -1 O LEU A 74 N VAL A 21 SHEET 4 AA1 5 LEU A 61 PHE A 65 -1 N THR A 62 O HIS A 75 SHEET 5 AA1 5 VAL A 55 LEU A 58 -1 N LEU A 58 O LEU A 61 SHEET 1 AA2 5 PHE A 10 GLN A 14 0 SHEET 2 AA2 5 THR A 104 LYS A 109 1 O SER A 107 N LEU A 11 SHEET 3 AA2 5 GLY A 85 GLY A 91 -1 N TYR A 87 O THR A 104 SHEET 4 AA2 5 LEU A 32 GLN A 37 -1 N GLN A 33 O ALA A 90 SHEET 5 AA2 5 VAL A 44 VAL A 49 -1 O VAL A 49 N LEU A 32 SHEET 1 AA3 4 PHE A 10 GLN A 14 0 SHEET 2 AA3 4 THR A 104 LYS A 109 1 O SER A 107 N LEU A 11 SHEET 3 AA3 4 GLY A 85 GLY A 91 -1 N TYR A 87 O THR A 104 SHEET 4 AA3 4 ILE A 99 PHE A 100 -1 O ILE A 99 N GLY A 91 SHEET 1 AA4 4 ALA A 118 LEU A 122 0 SHEET 2 AA4 4 LYS A 130 THR A 136 -1 O LEU A 134 N TYR A 120 SHEET 3 AA4 4 PHE A 167 ASN A 177 -1 O ALA A 172 N PHE A 135 SHEET 4 AA4 4 CYS A 158 MET A 162 -1 N MET A 162 O PHE A 167 SHEET 1 AA5 4 ILE B 6 SER B 9 0 SHEET 2 AA5 4 VAL B 21 GLN B 27 -1 O GLU B 26 N THR B 7 SHEET 3 AA5 4 LEU B 78 VAL B 80 -1 O LEU B 78 N LEU B 23 SHEET 4 AA5 4 TYR B 66 VAL B 68 -1 N SER B 67 O THR B 79 SHEET 1 AA6 6 TYR B 12 LYS B 16 0 SHEET 2 AA6 6 THR B 109 THR B 114 1 O ARG B 110 N LEU B 13 SHEET 3 AA6 6 PHE B 90 SER B 96 -1 N TYR B 91 O THR B 109 SHEET 4 AA6 6 ALA B 33 GLN B 39 -1 N TYR B 35 O ALA B 94 SHEET 5 AA6 6 LEU B 45 SER B 51 -1 O SER B 51 N MET B 34 SHEET 6 AA6 6 GLN B 58 LYS B 59 -1 O GLN B 58 N TYR B 50 SHEET 1 AA7 4 TYR B 12 LYS B 16 0 SHEET 2 AA7 4 THR B 109 THR B 114 1 O ARG B 110 N LEU B 13 SHEET 3 AA7 4 PHE B 90 SER B 96 -1 N TYR B 91 O THR B 109 SHEET 4 AA7 4 TYR B 104 PHE B 105 -1 O TYR B 104 N SER B 95 SHEET 1 AA8 4 GLU B 124 PHE B 128 0 SHEET 2 AA8 4 LYS B 140 PHE B 150 -1 O LEU B 146 N ALA B 126 SHEET 3 AA8 4 TYR B 188 SER B 197 -1 O TYR B 188 N PHE B 150 SHEET 4 AA8 4 VAL B 170 THR B 172 -1 N CYS B 171 O ARG B 193 SHEET 1 AA9 4 GLU B 124 PHE B 128 0 SHEET 2 AA9 4 LYS B 140 PHE B 150 -1 O LEU B 146 N ALA B 126 SHEET 3 AA9 4 TYR B 188 SER B 197 -1 O TYR B 188 N PHE B 150 SHEET 4 AA9 4 LEU B 177 LYS B 178 -1 N LEU B 177 O SER B 189 SHEET 1 AB1 4 LYS B 164 GLU B 165 0 SHEET 2 AB1 4 VAL B 155 VAL B 161 -1 N VAL B 161 O LYS B 164 SHEET 3 AB1 4 HIS B 207 PHE B 214 -1 O GLN B 211 N SER B 158 SHEET 4 AB1 4 ILE B 234 TRP B 240 -1 O ALA B 239 N PHE B 208 SHEET 1 AB2 4 LEU C 4 SER C 7 0 SHEET 2 AB2 4 SER C 17 ALA C 24 -1 O ALA C 23 N VAL C 5 SHEET 3 AB2 4 THR C 77 ASN C 83 -1 O MET C 82 N LEU C 18 SHEET 4 AB2 4 THR C 68 ARG C 71 -1 N THR C 68 O GLN C 81 SHEET 1 AB3 6 GLY C 10 GLN C 13 0 SHEET 2 AB3 6 THR C 109 SER C 114 1 O LEU C 110 N GLY C 10 SHEET 3 AB3 6 ALA C 91 PHE C 97 -1 N TYR C 93 O THR C 109 SHEET 4 AB3 6 TRP C 36 GLN C 39 -1 N GLN C 39 O VAL C 92 SHEET 5 AB3 6 ARG C 45 ILE C 51 -1 O ALA C 49 N TRP C 36 SHEET 6 AB3 6 THR C 57 TYR C 59 -1 O HIS C 58 N THR C 50 SHEET 1 AB4 4 GLY C 10 GLN C 13 0 SHEET 2 AB4 4 THR C 109 SER C 114 1 O LEU C 110 N GLY C 10 SHEET 3 AB4 4 ALA C 91 PHE C 97 -1 N TYR C 93 O THR C 109 SHEET 4 AB4 4 TYR C 104 TRP C 105 -1 O TYR C 104 N PHE C 97 SHEET 1 AB5 4 VAL T 2 SER T 7 0 SHEET 2 AB5 4 LEU T 18 GLY T 26 -1 O SER T 21 N SER T 7 SHEET 3 AB5 4 THR T 77 MET T 82 -1 O VAL T 78 N CYS T 22 SHEET 4 AB5 4 PHE T 67 ARG T 71 -1 N THR T 68 O GLN T 81 SHEET 1 AB6 6 GLY T 10 VAL T 12 0 SHEET 2 AB6 6 THR T 111 VAL T 115 1 O THR T 114 N VAL T 12 SHEET 3 AB6 6 ALA T 91 LEU T 98 -1 N ALA T 91 O VAL T 113 SHEET 4 AB6 6 PHE T 33 GLN T 39 -1 N TYR T 37 O TYR T 94 SHEET 5 AB6 6 GLU T 46 SER T 52 -1 O ALA T 49 N TRP T 36 SHEET 6 AB6 6 GLN T 56 ASP T 58 -1 O ASP T 58 N HIS T 50 SHEET 1 AB7 4 GLY T 10 VAL T 12 0 SHEET 2 AB7 4 THR T 111 VAL T 115 1 O THR T 114 N VAL T 12 SHEET 3 AB7 4 ALA T 91 LEU T 98 -1 N ALA T 91 O VAL T 113 SHEET 4 AB7 4 ASP T 105 TRP T 107 -1 O TYR T 106 N ALA T 97 SSBOND 1 CYS A 23 CYS A 89 1555 1555 2.16 SSBOND 2 CYS A 133 CYS A 183 1555 1555 2.19 SSBOND 3 CYS A 158 CYS B 171 1555 1555 2.13 SSBOND 4 CYS B 25 CYS B 93 1555 1555 2.26 SSBOND 5 CYS B 145 CYS B 210 1555 1555 2.12 SSBOND 6 CYS T 22 CYS T 95 1555 1555 2.16 LINK ND2 ASN A 18 C1 NAG E 1 1555 1555 1.45 LINK ND2 ASN A 143 C1 NAG D 1 1555 1555 1.39 LINK ND2 ASN B 20 C1 NAG F 1 1555 1555 1.47 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.42 LINK O6 NAG D 1 C1 FUC D 3 1555 1555 1.52 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.46 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45 CISPEP 1 SER B 9 PRO B 10 0 4.70 CISPEP 2 TYR B 151 PRO B 152 0 21.78 CISPEP 3 ALA B 243 ASP B 244 0 0.48 CISPEP 4 TRP T 102 PRO T 103 0 -13.06 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