HEADER CELL CYCLE 28-JUN-21 7OZT TITLE NANOBODIES RESTORE STABILITY TO CANCER-ASSOCIATED MUTANTS OF TUMOR TITLE 2 SUPPRESSOR PROTEIN P16INK4A COMPND MOL_ID: 1; COMPND 2 MOLECULE: CAMELID NANOBODY NB09; COMPND 3 CHAIN: AAA; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CYCLIN-DEPENDENT KINASE INHIBITOR 2A; COMPND 7 CHAIN: BBB; COMPND 8 SYNONYM: CYCLIN-DEPENDENT KINASE 4 INHIBITOR A,CDK4I,MULTIPLE TUMOR COMPND 9 SUPPRESSOR 1,MTS-1,P16-INK4A,P16-INK4,P16INK4A; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_COMMON: LLAMA; SOURCE 4 ORGANISM_TAXID: 9844; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA2; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMESY4; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: CDKN2A, CDKN2, MTS1; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 16 EXPRESSION_SYSTEM_VARIANT: LEMO21; SOURCE 17 EXPRESSION_SYSTEM_PLASMID: POPINF KEYWDS NANOBODY-P16INK4A COMPLEX, TUMOUR-SUPPRESSOR, CHECKPOINT, KEYWDS 2 PHARMACOLOGICAL CHAPERONE, CELL CYCLE EXPDTA X-RAY DIFFRACTION AUTHOR M.W.PASTOK,O.BURBIDGE,L.ITZHAKI,J.A.ENDICOTT,M.E.M.NOBLE JRNL AUTH O.BURBIDGE,M.W.PASTOK,S.L.HODDER,G.ZENKEVICIUTE,M.E.M.NOBLE, JRNL AUTH 2 J.A.ENDICOTT,L.ITZHAKI JRNL TITL NANOBODIES RESTORE STABILITY TO CANCER-ASSOCIATED MUTANTS OF JRNL TITL 2 TUMOR SUPPRESSOR PROTEIN P16INK4A JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.74 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.47 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 26427 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM SELECTION REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.180 REMARK 3 FREE R VALUE : 0.209 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.519 REMARK 3 FREE R VALUE TEST SET COUNT : 930 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) : 1.74 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1911 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.3270 REMARK 3 BIN FREE R VALUE SET COUNT : 0 REMARK 3 BIN FREE R VALUE : 0.2590 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1854 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 90 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.96 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.17500 REMARK 3 B22 (A**2) : -1.03800 REMARK 3 B33 (A**2) : -0.13700 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.106 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.123 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1919 ; 0.016 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 1814 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2608 ; 2.081 ; 1.639 REMARK 3 BOND ANGLES OTHERS (DEGREES): 4150 ; 1.410 ; 1.579 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 253 ; 6.884 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 105 ;31.079 ;19.714 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 303 ;15.269 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;18.676 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 242 ; 0.102 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2422 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 470 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 323 ; 0.206 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 37 ; 0.249 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 896 ; 0.160 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 82 ; 0.202 ; 0.200 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): 1006 ; 2.006 ; 2.258 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1005 ; 1.979 ; 2.254 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1261 ; 3.184 ; 3.370 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1262 ; 3.186 ; 3.374 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 913 ; 3.382 ; 2.758 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 914 ; 3.380 ; 2.761 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1347 ; 5.461 ; 3.964 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1348 ; 5.459 ; 3.968 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL 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 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 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 : AA 1 AA 122 REMARK 3 ORIGIN FOR THE GROUP (A): -8.2490 12.4238 2.5774 REMARK 3 T TENSOR REMARK 3 T11: 0.0015 T22: 0.0527 REMARK 3 T33: 0.0476 T12: 0.0062 REMARK 3 T13: 0.0051 T23: 0.0383 REMARK 3 L TENSOR REMARK 3 L11: 0.1624 L22: 1.8680 REMARK 3 L33: 0.4043 L12: 0.0131 REMARK 3 L13: -0.2545 L23: 0.0223 REMARK 3 S TENSOR REMARK 3 S11: -0.0025 S12: -0.0431 S13: 0.0152 REMARK 3 S21: 0.0069 S22: 0.0351 S23: 0.1077 REMARK 3 S31: 0.0057 S32: 0.0552 S33: -0.0326 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 : BB 10 BB 134 REMARK 3 ORIGIN FOR THE GROUP (A): 4.3730 35.3509 -2.7296 REMARK 3 T TENSOR REMARK 3 T11: 0.0217 T22: 0.0392 REMARK 3 T33: 0.0186 T12: 0.0004 REMARK 3 T13: -0.0017 T23: -0.0184 REMARK 3 L TENSOR REMARK 3 L11: 0.7638 L22: 0.7590 REMARK 3 L33: 0.2977 L12: -0.1098 REMARK 3 L13: -0.2744 L23: 0.0369 REMARK 3 S TENSOR REMARK 3 S11: -0.0197 S12: -0.0274 S13: 0.0299 REMARK 3 S21: 0.1160 S22: 0.0424 S23: -0.0309 REMARK 3 S31: -0.0206 S32: 0.0377 S33: -0.0226 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT 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 THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 7OZT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292116515. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-FEB-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97622 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26446 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740 REMARK 200 RESOLUTION RANGE LOW (A) : 91.470 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : 0.10100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 9.04 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 91.47 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 5.60 REMARK 200 R MERGE FOR SHELL (I) : 0.04600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL 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: 1BI7, 3OGO REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 35.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: MOLECULAR DIMENSIONS MORPHEUS SCREEN REMARK 280 CONDITION G4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.61250 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.61250 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 21.05950 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 91.46550 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 21.05950 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 91.46550 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 32.61250 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 21.05950 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 91.46550 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 32.61250 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 21.05950 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 91.46550 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1270 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 11620 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAA, BBB 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 236 LIES ON A SPECIAL POSITION. REMARK 375 HOH B 245 LIES ON A SPECIAL POSITION. 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 HIS A 123 REMARK 465 HIS A 124 REMARK 465 HIS A 125 REMARK 465 HIS A 126 REMARK 465 HIS A 127 REMARK 465 HIS A 128 REMARK 465 GLU A 129 REMARK 465 PRO A 130 REMARK 465 GLU A 131 REMARK 465 ALA A 132 REMARK 465 MET B -18 REMARK 465 ALA B -17 REMARK 465 HIS B -16 REMARK 465 HIS B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 SER B -10 REMARK 465 SER B -9 REMARK 465 GLY B -8 REMARK 465 LEU B -7 REMARK 465 GLU B -6 REMARK 465 VAL B -5 REMARK 465 LEU B -4 REMARK 465 PHE B -3 REMARK 465 GLN B -2 REMARK 465 GLY B -1 REMARK 465 PRO B 0 REMARK 465 MET B 1 REMARK 465 GLU B 2 REMARK 465 PRO B 3 REMARK 465 ALA B 4 REMARK 465 ALA B 5 REMARK 465 GLY B 6 REMARK 465 SER B 7 REMARK 465 SER B 8 REMARK 465 MET B 9 REMARK 465 GLY B 135 REMARK 465 GLY B 136 REMARK 465 THR B 137 REMARK 465 ARG B 138 REMARK 465 GLY B 139 REMARK 465 SER B 140 REMARK 465 ASN B 141 REMARK 465 HIS B 142 REMARK 465 ALA B 143 REMARK 465 ARG B 144 REMARK 465 ILE B 145 REMARK 465 ASP B 146 REMARK 465 ALA B 147 REMARK 465 ALA B 148 REMARK 465 GLU B 149 REMARK 465 GLY B 150 REMARK 465 PRO B 151 REMARK 465 SER B 152 REMARK 465 ASP B 153 REMARK 465 ILE B 154 REMARK 465 PRO B 155 REMARK 465 ASP B 156 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 H ARGBB 80 HD2 HISBB 83 1.24 REMARK 500 HH TYRAA 62 H ILEAA 72 1.25 REMARK 500 O HOHBB 233 O HOHBB 240 1.97 REMARK 500 REMARK 500 REMARK: NULL 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 HG3 ARGBB 58 HG3 ARGBB 58 3554 1.26 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 ARGBB 99 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES REMARK 500 ARGBB 99 NE - CZ - NH2 ANGL. DEV. = 5.3 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 SERBB 43 -35.90 -34.15 REMARK 500 METBB 53 105.20 -56.72 REMARK 500 METBB 53 105.20 -56.57 REMARK 500 ALABB 76 -64.75 -98.70 REMARK 500 REMARK 500 REMARK: NULL DBREF 7OZTAA 1 132 PDB 7OZT 7OZT 1 132 DBREF 7OZTBB 1 156 UNP P42771 CDN2A_HUMAN 1 156 SEQADV 7OZT METBB -18 UNP P42771 INITIATING METHIONINE SEQADV 7OZT ALABB -17 UNP P42771 EXPRESSION TAG SEQADV 7OZT HISBB -16 UNP P42771 EXPRESSION TAG SEQADV 7OZT HISBB -15 UNP P42771 EXPRESSION TAG SEQADV 7OZT HISBB -14 UNP P42771 EXPRESSION TAG SEQADV 7OZT HISBB -13 UNP P42771 EXPRESSION TAG SEQADV 7OZT HISBB -12 UNP P42771 EXPRESSION TAG SEQADV 7OZT HISBB -11 UNP P42771 EXPRESSION TAG SEQADV 7OZT SERBB -10 UNP P42771 EXPRESSION TAG SEQADV 7OZT SERBB -9 UNP P42771 EXPRESSION TAG SEQADV 7OZT GLYBB -8 UNP P42771 EXPRESSION TAG SEQADV 7OZT LEUBB -7 UNP P42771 EXPRESSION TAG SEQADV 7OZT GLUBB -6 UNP P42771 EXPRESSION TAG SEQADV 7OZT VALBB -5 UNP P42771 EXPRESSION TAG SEQADV 7OZT LEUBB -4 UNP P42771 EXPRESSION TAG SEQADV 7OZT PHEBB -3 UNP P42771 EXPRESSION TAG SEQADV 7OZT GLNBB -2 UNP P42771 EXPRESSION TAG SEQADV 7OZT GLYBB -1 UNP P42771 EXPRESSION TAG SEQADV 7OZT PROBB 0 UNP P42771 EXPRESSION TAG SEQRES 1AA 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2AA 132 ALA GLY ALA SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3AA 132 SER THR TYR MET PHE SER ILE SER ALA MET GLY TRP TYR SEQRES 4AA 132 ARG GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA ALA SEQRES 5AA 132 ILE THR SER GLY GLY GLY ASP THR ASN TYR ALA ASP SER SEQRES 6AA 132 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ARG ALA LYS SEQRES 7AA 132 ASN MET VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8AA 132 ASP THR ALA VAL TYR TYR CYS ASN PHE ALA PRO GLY LEU SEQRES 9AA 132 GLN SER VAL ARG SER GLY SER TRP GLY GLN GLY THR GLN SEQRES 10AA 132 VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS GLU PRO SEQRES 11AA 132 GLU ALA SEQRES 1BB 175 MET ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU SEQRES 2BB 175 VAL LEU PHE GLN GLY PRO MET GLU PRO ALA ALA GLY SER SEQRES 3BB 175 SER MET GLU PRO SER ALA ASP TRP LEU ALA THR ALA ALA SEQRES 4BB 175 ALA ARG GLY ARG VAL GLU GLU VAL ARG ALA LEU LEU GLU SEQRES 5BB 175 ALA GLY ALA LEU PRO ASN ALA PRO ASN SER TYR GLY ARG SEQRES 6BB 175 ARG PRO ILE GLN VAL MET MET MET GLY SER ALA ARG VAL SEQRES 7BB 175 ALA GLU LEU LEU LEU LEU HIS GLY ALA GLU PRO ASN CYS SEQRES 8BB 175 ALA ASP PRO ALA THR LEU THR ARG PRO VAL HIS ASP ALA SEQRES 9BB 175 ALA ARG GLU GLY PHE LEU ASP THR LEU VAL VAL LEU HIS SEQRES 10BB 175 ARG ALA GLY ALA ARG LEU ASP VAL ARG ASP ALA TRP GLY SEQRES 11BB 175 ARG LEU PRO VAL ASP LEU ALA GLU GLU LEU GLY HIS ARG SEQRES 12BB 175 ASP VAL ALA ARG TYR LEU ARG ALA ALA ALA GLY GLY THR SEQRES 13BB 175 ARG GLY SER ASN HIS ALA ARG ILE ASP ALA ALA GLU GLY SEQRES 14BB 175 PRO SER ASP ILE PRO ASP FORMUL 3 HOH *90(H2 O) HELIX 1 AA1 SERAA 27 ILEAA 33 1 7 HELIX 2 AA2 LYSAA 89 THRAA 93 5 5 HELIX 3 AA3 PROAA 102 GLNAA 105 5 4 HELIX 4 AA4 PROBB 11 ARGBB 22 1 12 HELIX 5 AA5 ARGBB 24 ALABB 34 1 11 HELIX 6 AA6 ARGBB 47 METBB 52 1 6 HELIX 7 AA7 SERBB 56 HISBB 66 1 11 HELIX 8 AA8 ARGBB 80 GLUBB 88 1 9 HELIX 9 AA9 PHEBB 90 GLYBB 101 1 12 HELIX 10 AB1 LEUBB 113 GLYBB 122 1 10 HELIX 11 AB2 HISBB 123 ALABB 134 1 12 SHEET 1 AA1 4 VALAA 2 SERAA 7 0 SHEET 2 AA1 4 LEUAA 18 GLYAA 26 -1 O SERAA 25 N GLNAA 3 SHEET 3 AA1 4 METAA 80 METAA 85 -1 O METAA 85 N LEUAA 18 SHEET 4 AA1 4 PHEAA 70 ASPAA 75 -1 N SERAA 73 O TYRAA 82 SHEET 1 AA2 6 GLYAA 10 GLNAA 13 0 SHEET 2 AA2 6 THRAA 116 SERAA 121 1 O THRAA 119 N GLYAA 10 SHEET 3 AA2 6 ALAAA 94 PHEAA 100 -1 N ALAAA 94 O VALAA 118 SHEET 4 AA2 6 METAA 36 GLNAA 41 -1 N TYRAA 39 O TYRAA 97 SHEET 5 AA2 6 GLUAA 48 ILEAA 53 -1 O VALAA 50 N TRPAA 38 SHEET 6 AA2 6 THRAA 60 TYRAA 62 -1 O ASNAA 61 N ALAAA 52 SSBOND 1 CYSAA 22 CYSAA 98 1555 1555 2.05 CRYST1 42.119 182.931 65.225 90.00 90.00 90.00 C 2 2 21 8 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 0.023742 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005467 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015332 0.00000