HEADER IMMUNE SYSTEM 27-FEB-24 8S6K TITLE CRYSTAL STRUCTURE OF SCFV-G2D11 COMPLEXED TO A BIS-TN GLYCOPEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SCFV-G2D11; COMPND 3 CHAIN: A, H; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: COMPND 6 SSGGGGSGGGGGSSGSSDVVMTQSHKFMSTSVGDRVSITCKASQDVGTAVAWYQQKPGQSPKLLIYWAS COMPND 7 TRHTGVPDRFTGSGSGTDFTLTISNVQSEDLADYFCQQYSSYPLTFGGGTKLEMKRGGHHHHHH; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: MUCIN-1 SUBUNIT ALPHA; COMPND 10 CHAIN: M, N; COMPND 11 SYNONYM: MUC1-NT,MUC1-ALPHA; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4922; SOURCE 6 MOL_ID: 2; SOURCE 7 SYNTHETIC: YES; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606 KEYWDS MONOCLONAL ANTIBODY, SCFV-G2D11, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.HURTADO-GUERRERO,J.MACIAS-LEON REVDAT 1 25-JUN-25 8S6K 0 JRNL AUTH R.HURTADO-GUERRERO,S.GATOS,I.GINES-ALCOBER,J.MACIAS-LEON, JRNL AUTH 2 A.MANUEL GONZALEZ-RAMIREZ,I.KASAPOGLU,B.VELOZ,I.COMPANON, JRNL AUTH 3 M.GHIRARDELLO,P.MERINO,F.CORZANA,O.BLIXT JRNL TITL RECOGNIZING TN AND STN EPITOPES IN PROTEIN CONTEXT: JRNL TITL 2 STRUCTURAL ADVANCES IN PHAGE DISPLAY LIBRARIES FOR JRNL TITL 3 TUMOR-SPECIFIC ANTIBODY DISCOVERY JRNL REF NAT.CHEM.BIOL. 2025 JRNL REFN ESSN 1552-4469 REMARK 2 REMARK 2 RESOLUTION. 1.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.90 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1 REMARK 3 NUMBER OF REFLECTIONS : 50086 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.184 REMARK 3 R VALUE (WORKING SET) : 0.182 REMARK 3 FREE R VALUE : 0.221 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2094 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2867 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.66 REMARK 3 BIN R VALUE (WORKING SET) : 0.2570 REMARK 3 BIN FREE R VALUE SET COUNT : 120 REMARK 3 BIN FREE R VALUE : 0.2870 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3630 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 104 REMARK 3 SOLVENT ATOMS : 455 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.74 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.60000 REMARK 3 B22 (A**2) : -0.17000 REMARK 3 B33 (A**2) : -0.95000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.81000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.117 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.116 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.487 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3842 ; 0.015 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 3507 ; 0.004 ; 0.018 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5190 ; 1.945 ; 1.699 REMARK 3 BOND ANGLES OTHERS (DEGREES): 8137 ; 1.611 ; 1.656 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 469 ; 7.550 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 163 ;30.150 ;23.497 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 608 ;15.896 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;20.628 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 512 ; 0.102 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4289 ; 0.011 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 855 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1870 ; 1.368 ; 1.677 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1869 ; 1.367 ; 1.676 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2329 ; 2.139 ; 2.506 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2330 ; 2.139 ; 2.507 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1972 ; 2.052 ; 1.870 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1973 ; 2.051 ; 1.872 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2858 ; 3.148 ; 2.692 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4337 ; 5.843 ;20.955 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4337 ; 5.840 ;20.959 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NCS TYPE: LOCAL REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 2 REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT REMARK 3 1 A 1 112 H 1 112 3554 0.10 0.05 REMARK 3 2 A 122 1106 H 122 1106 3404 0.07 0.05 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 112 REMARK 3 ORIGIN FOR THE GROUP (A): 19.5470 -6.2963 30.9222 REMARK 3 T TENSOR REMARK 3 T11: 0.0163 T22: 0.0976 REMARK 3 T33: 0.0422 T12: -0.0022 REMARK 3 T13: -0.0089 T23: 0.0103 REMARK 3 L TENSOR REMARK 3 L11: 0.2445 L22: 0.3813 REMARK 3 L33: 0.6536 L12: -0.1094 REMARK 3 L13: 0.0885 L23: -0.0636 REMARK 3 S TENSOR REMARK 3 S11: 0.0391 S12: 0.0096 S13: 0.0007 REMARK 3 S21: 0.0183 S22: -0.0205 S23: 0.0296 REMARK 3 S31: 0.0562 S32: 0.0561 S33: -0.0187 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 121 A 1107 REMARK 3 ORIGIN FOR THE GROUP (A): -0.3958 -7.4121 24.6951 REMARK 3 T TENSOR REMARK 3 T11: 0.0124 T22: 0.1034 REMARK 3 T33: 0.0372 T12: -0.0295 REMARK 3 T13: 0.0108 T23: -0.0166 REMARK 3 L TENSOR REMARK 3 L11: 0.6960 L22: 0.3947 REMARK 3 L33: 0.6446 L12: 0.3446 REMARK 3 L13: 0.4813 L23: -0.0171 REMARK 3 S TENSOR REMARK 3 S11: -0.0120 S12: -0.0572 S13: -0.0541 REMARK 3 S21: -0.0493 S22: 0.0425 S23: -0.0530 REMARK 3 S31: 0.0348 S32: -0.0957 S33: -0.0306 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 112 REMARK 3 ORIGIN FOR THE GROUP (A): 12.5194 23.3694 6.0410 REMARK 3 T TENSOR REMARK 3 T11: 0.1341 T22: 0.0915 REMARK 3 T33: 0.0592 T12: 0.0013 REMARK 3 T13: -0.0626 T23: -0.0074 REMARK 3 L TENSOR REMARK 3 L11: 0.0221 L22: 0.3085 REMARK 3 L33: 1.6491 L12: -0.0438 REMARK 3 L13: 0.0465 L23: -0.6467 REMARK 3 S TENSOR REMARK 3 S11: 0.0320 S12: 0.0164 S13: -0.0318 REMARK 3 S21: 0.0868 S22: -0.0980 S23: 0.0167 REMARK 3 S31: -0.3184 S32: 0.1308 S33: 0.0659 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 122 H 1107 REMARK 3 ORIGIN FOR THE GROUP (A): -0.7522 24.5120 22.0105 REMARK 3 T TENSOR REMARK 3 T11: 0.0707 T22: 0.0689 REMARK 3 T33: 0.0263 T12: 0.0164 REMARK 3 T13: -0.0371 T23: -0.0142 REMARK 3 L TENSOR REMARK 3 L11: 0.3533 L22: 0.2747 REMARK 3 L33: 1.1580 L12: -0.2410 REMARK 3 L13: 0.0104 L23: 0.3491 REMARK 3 S TENSOR REMARK 3 S11: 0.0185 S12: -0.0297 S13: 0.0225 REMARK 3 S21: -0.0504 S22: -0.0157 S23: -0.0115 REMARK 3 S31: -0.0977 S32: -0.0924 S33: -0.0027 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 8S6K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1292136912. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-DEC-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52287 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.08500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84 REMARK 200 COMPLETENESS FOR SHELL (%) : 84.6 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.48900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.58 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM CHLORIDE TRIS PEG 8000, PH 8, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 34.83350 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, M 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, N 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 SER A 113 REMARK 465 SER A 114 REMARK 465 SER A 115 REMARK 465 GLY A 116 REMARK 465 GLY A 117 REMARK 465 GLY A 118 REMARK 465 GLY A 119 REMARK 465 SER A 120 REMARK 465 ARG A 1108 REMARK 465 GLY A 1109 REMARK 465 GLY A 1110 REMARK 465 HIS A 1111 REMARK 465 HIS A 1112 REMARK 465 HIS A 1113 REMARK 465 HIS A 1114 REMARK 465 HIS A 1115 REMARK 465 HIS A 1116 REMARK 465 SER H 113 REMARK 465 SER H 114 REMARK 465 SER H 115 REMARK 465 GLY H 116 REMARK 465 GLY H 117 REMARK 465 GLY H 118 REMARK 465 GLY H 119 REMARK 465 SER H 120 REMARK 465 GLY H 121 REMARK 465 ARG H 1108 REMARK 465 GLY H 1109 REMARK 465 GLY H 1110 REMARK 465 HIS H 1111 REMARK 465 HIS H 1112 REMARK 465 HIS H 1113 REMARK 465 HIS H 1114 REMARK 465 HIS H 1115 REMARK 465 HIS H 1116 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OD1 ASP A 72 OD2 ASP A 1070 1655 1.94 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 PRO N 7 CA PRO N 7 C -0.124 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 THR A1013 CB - CA - C ANGL. DEV. = -18.7 DEGREES REMARK 500 LYS H 93 CG - CD - CE ANGL. DEV. = -18.6 DEGREES REMARK 500 THR H1013 CB - CA - C ANGL. DEV. = -18.2 DEGREES 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 41 124.75 -36.31 REMARK 500 SER A 95 -172.94 71.81 REMARK 500 ALA A1051 -38.21 71.74 REMARK 500 ALA A1084 175.73 179.80 REMARK 500 GLN H 43 -148.72 -112.29 REMARK 500 SER H 95 -170.26 68.81 REMARK 500 ALA H1051 -37.59 76.61 REMARK 500 REMARK 500 REMARK: NULL DBREF 8S6K A 1 1116 PDB 8S6K 8S6K 1 1116 DBREF 8S6K H 1 1116 PDB 8S6K 8S6K 1 1116 DBREF 8S6K M 1 7 UNP P15941 MUC1_HUMAN 127 133 DBREF 8S6K N 1 7 UNP P15941 MUC1_HUMAN 127 133 SEQADV 8S6K NH2 M 8 UNP P15941 AMIDATION SEQADV 8S6K NH2 N 8 UNP P15941 AMIDATION SEQRES 1 A 250 GLN VAL GLN LEU GLN GLN SER ASP ALA GLU LEU VAL LYS SEQRES 2 A 250 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 A 250 TYR ILE PHE ALA ASP HIS ALA ILE HIS TRP VAL LYS ARG SEQRES 4 A 250 LYS PRO GLU GLN GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 A 250 PRO GLY ASN ASP ASP ILE LYS TYR ASN GLU LYS PHE LYS SEQRES 6 A 250 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 A 250 ALA TYR MET GLN LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 A 250 ALA VAL TYR PHE CYS LYS ARG SER LEU PRO GLY THR PHE SEQRES 9 A 250 ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER SEQRES 10 A 250 SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY GLY SER SEQRES 11 A 250 SER GLY SER SER ASP VAL VAL MET THR GLN SER HIS LYS SEQRES 12 A 250 PHE MET SER THR SER VAL GLY ASP ARG VAL SER ILE THR SEQRES 13 A 250 CYS LYS ALA SER GLN ASP VAL GLY THR ALA VAL ALA TRP SEQRES 14 A 250 TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU LEU ILE SEQRES 15 A 250 TYR TRP ALA SER THR ARG HIS THR GLY VAL PRO ASP ARG SEQRES 16 A 250 PHE THR GLY SER GLY SER GLY THR ASP PHE THR LEU THR SEQRES 17 A 250 ILE SER ASN VAL GLN SER GLU ASP LEU ALA ASP TYR PHE SEQRES 18 A 250 CYS GLN GLN TYR SER SER TYR PRO LEU THR PHE GLY GLY SEQRES 19 A 250 GLY THR LYS LEU GLU MET LYS ARG GLY GLY HIS HIS HIS SEQRES 20 A 250 HIS HIS HIS SEQRES 1 H 250 GLN VAL GLN LEU GLN GLN SER ASP ALA GLU LEU VAL LYS SEQRES 2 H 250 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 250 TYR ILE PHE ALA ASP HIS ALA ILE HIS TRP VAL LYS ARG SEQRES 4 H 250 LYS PRO GLU GLN GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 H 250 PRO GLY ASN ASP ASP ILE LYS TYR ASN GLU LYS PHE LYS SEQRES 6 H 250 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 H 250 ALA TYR MET GLN LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 H 250 ALA VAL TYR PHE CYS LYS ARG SER LEU PRO GLY THR PHE SEQRES 9 H 250 ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER SEQRES 10 H 250 SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY GLY SER SEQRES 11 H 250 SER GLY SER SER ASP VAL VAL MET THR GLN SER HIS LYS SEQRES 12 H 250 PHE MET SER THR SER VAL GLY ASP ARG VAL SER ILE THR SEQRES 13 H 250 CYS LYS ALA SER GLN ASP VAL GLY THR ALA VAL ALA TRP SEQRES 14 H 250 TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU LEU ILE SEQRES 15 H 250 TYR TRP ALA SER THR ARG HIS THR GLY VAL PRO ASP ARG SEQRES 16 H 250 PHE THR GLY SER GLY SER GLY THR ASP PHE THR LEU THR SEQRES 17 H 250 ILE SER ASN VAL GLN SER GLU ASP LEU ALA ASP TYR PHE SEQRES 18 H 250 CYS GLN GLN TYR SER SER TYR PRO LEU THR PHE GLY GLY SEQRES 19 H 250 GLY THR LYS LEU GLU MET LYS ARG GLY GLY HIS HIS HIS SEQRES 20 H 250 HIS HIS HIS SEQRES 1 M 8 ALA PRO GLY SER THR ALA PRO NH2 SEQRES 1 N 8 ALA PRO GLY SER THR ALA PRO NH2 HET NH2 M 8 1 HET NH2 N 8 1 HET EDO A 301 4 HET EDO A 302 4 HET EDO A 303 4 HET EDO A 304 4 HET EDO A 305 4 HET EDO A 306 4 HET EDO A 307 4 HET EDO H 301 4 HET EDO H 302 4 HET EDO H 303 4 HET EDO H 304 4 HET EDO H 305 4 HET A2G M 101 14 HET A2G M 102 14 HET A2G N 101 14 HET A2G N 102 14 HETNAM NH2 AMINO GROUP HETNAM EDO 1,2-ETHANEDIOL HETNAM A2G 2-ACETAMIDO-2-DEOXY-ALPHA-D-GALACTOPYRANOSE HETSYN EDO ETHYLENE GLYCOL HETSYN A2G N-ACETYL-ALPHA-D-GALACTOSAMINE; 2-ACETAMIDO-2-DEOXY- HETSYN 2 A2G ALPHA-D-GALACTOSE; 2-ACETAMIDO-2-DEOXY-D-GALACTOSE; 2- HETSYN 3 A2G ACETAMIDO-2-DEOXY-GALACTOSE; N-ACETYL-2-DEOXY-2-AMINO- HETSYN 4 A2G GALACTOSE FORMUL 3 NH2 2(H2 N) FORMUL 5 EDO 12(C2 H6 O2) FORMUL 17 A2G 4(C8 H15 N O6) FORMUL 21 HOH *455(H2 O) HELIX 1 AA1 ILE A 28 HIS A 32 5 5 HELIX 2 AA2 GLU A 61 LYS A 64 5 4 HELIX 3 AA3 THR A 83 SER A 87 5 5 HELIX 4 AA4 GLN A 1079 LEU A 1083 5 5 HELIX 5 AA5 ILE H 28 HIS H 32 5 5 HELIX 6 AA6 GLU H 61 LYS H 64 5 4 HELIX 7 AA7 LYS H 73 SER H 75 5 3 HELIX 8 AA8 THR H 83 SER H 87 5 5 HELIX 9 AA9 GLN H 1079 LEU H 1083 5 5 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N GLN A 5 SHEET 3 AA1 4 THR A 77 LEU A 82 -1 O MET A 80 N ILE A 20 SHEET 4 AA1 4 ALA A 67 ASP A 72 -1 N ASP A 72 O THR A 77 SHEET 1 AA2 6 GLU A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 107 VAL A 111 1 O THR A 110 N GLU A 10 SHEET 3 AA2 6 ALA A 88 ARG A 94 -1 N ALA A 88 O LEU A 109 SHEET 4 AA2 6 ILE A 34 ARG A 39 -1 N ARG A 39 O VAL A 89 SHEET 5 AA2 6 LEU A 45 SER A 52 -1 O ILE A 48 N TRP A 36 SHEET 6 AA2 6 ASP A 56A TYR A 59 -1 O ASP A 56A N SER A 52 SHEET 1 AA3 4 GLU A 10 VAL A 12 0 SHEET 2 AA3 4 THR A 107 VAL A 111 1 O THR A 110 N GLU A 10 SHEET 3 AA3 4 ALA A 88 ARG A 94 -1 N ALA A 88 O LEU A 109 SHEET 4 AA3 4 TYR A 102 TRP A 103 -1 O TYR A 102 N ARG A 94 SHEET 1 AA4 4 MET A1004 THR A1005 0 SHEET 2 AA4 4 VAL A1019 ALA A1025 -1 O LYS A1024 N THR A1005 SHEET 3 AA4 4 ASP A1070 ILE A1075 -1 O PHE A1071 N CYS A1023 SHEET 4 AA4 4 PHE A1062 SER A1067 -1 N THR A1063 O THR A1074 SHEET 1 AA5 6 PHE A1010 THR A1013 0 SHEET 2 AA5 6 THR A1102 MET A1106 1 O GLU A1105 N MET A1011 SHEET 3 AA5 6 ALA A1084 GLN A1090 -1 N ALA A1084 O LEU A1104 SHEET 4 AA5 6 VAL A1033 GLN A1038 -1 N GLN A1038 O ASP A1085 SHEET 5 AA5 6 LYS A1045 TYR A1049 -1 O LEU A1047 N TRP A1035 SHEET 6 AA5 6 THR A1053 ARG A1054 -1 O THR A1053 N TYR A1049 SHEET 1 AA6 4 PHE A1010 THR A1013 0 SHEET 2 AA6 4 THR A1102 MET A1106 1 O GLU A1105 N MET A1011 SHEET 3 AA6 4 ALA A1084 GLN A1090 -1 N ALA A1084 O LEU A1104 SHEET 4 AA6 4 THR A1097 PHE A1098 -1 O THR A1097 N GLN A1090 SHEET 1 AA7 4 GLN H 3 GLN H 6 0 SHEET 2 AA7 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA7 4 THR H 77 LEU H 82 -1 O MET H 80 N ILE H 20 SHEET 4 AA7 4 ALA H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA8 6 GLU H 10 VAL H 12 0 SHEET 2 AA8 6 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10 SHEET 3 AA8 6 ALA H 88 ARG H 94 -1 N ALA H 88 O LEU H 109 SHEET 4 AA8 6 ILE H 34 ARG H 39 -1 N ARG H 39 O VAL H 89 SHEET 5 AA8 6 LEU H 45 SER H 52 -1 O ILE H 48 N TRP H 36 SHEET 6 AA8 6 ASP H 56A TYR H 59 -1 O ASP H 56A N SER H 52 SHEET 1 AA9 4 GLU H 10 VAL H 12 0 SHEET 2 AA9 4 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10 SHEET 3 AA9 4 ALA H 88 ARG H 94 -1 N ALA H 88 O LEU H 109 SHEET 4 AA9 4 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AB1 4 MET H1004 THR H1005 0 SHEET 2 AB1 4 VAL H1019 ALA H1025 -1 O LYS H1024 N THR H1005 SHEET 3 AB1 4 ASP H1070 ILE H1075 -1 O LEU H1073 N ILE H1021 SHEET 4 AB1 4 PHE H1062 SER H1067 -1 N THR H1063 O THR H1074 SHEET 1 AB2 6 PHE H1010 THR H1013 0 SHEET 2 AB2 6 THR H1102 MET H1106 1 O GLU H1105 N MET H1011 SHEET 3 AB2 6 ALA H1084 GLN H1090 -1 N ALA H1084 O LEU H1104 SHEET 4 AB2 6 VAL H1033 GLN H1038 -1 N GLN H1038 O ASP H1085 SHEET 5 AB2 6 LYS H1045 TYR H1049 -1 O LEU H1047 N TRP H1035 SHEET 6 AB2 6 THR H1053 ARG H1054 -1 O THR H1053 N TYR H1049 SHEET 1 AB3 4 PHE H1010 THR H1013 0 SHEET 2 AB3 4 THR H1102 MET H1106 1 O GLU H1105 N MET H1011 SHEET 3 AB3 4 ALA H1084 GLN H1090 -1 N ALA H1084 O LEU H1104 SHEET 4 AB3 4 THR H1097 PHE H1098 -1 O THR H1097 N GLN H1090 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.12 SSBOND 2 CYS A 1023 CYS A 1088 1555 1555 2.14 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.10 SSBOND 4 CYS H 1023 CYS H 1088 1555 1555 2.15 LINK OG SER M 4 C1 A2G M 101 1555 1555 1.44 LINK OG1 THR M 5 C1 A2G M 102 1555 1555 1.47 LINK C PRO M 7 N NH2 M 8 1555 1555 1.27 LINK OG SER N 4 C1 A2G N 101 1555 1555 1.40 LINK OG1 THR N 5 C1 A2G N 102 1555 1555 1.48 LINK C PRO N 7 N NH2 N 8 1555 1555 1.33 CISPEP 1 TYR A 1094 PRO A 1095 0 -2.86 CISPEP 2 TYR H 1094 PRO H 1095 0 -1.64 CISPEP 3 ALA M 1 PRO M 2 0 7.14 CISPEP 4 ALA N 1 PRO N 2 0 -0.70 CRYST1 45.992 69.667 87.367 90.00 102.99 90.00 P 1 21 1 4 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 0.021743 0.000000 0.005015 0.00000 SCALE2 0.000000 0.014354 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011747 0.00000