HEADER IMMUNE SYSTEM 15-JUN-24 8ZXW TITLE CRYSTAL STRUCTURE OF THE ANTI-PHOSPHORYLATED PEPTIDE C7 FAB ANTIBODY TITLE 2 WITH PEPTIDE BOUND COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB, HEAVY CHAIN; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB, LIGHT CHAIN; COMPND 7 CHAIN: L, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: RAC-GAMMA SERINE/THREONINE-PROTEIN KINASE; COMPND 11 CHAIN: C, D; COMPND 12 SYNONYM: PROTEIN KINASE AKT-3,PROTEIN KINASE B GAMMA,PKB GAMMA,RAC- COMPND 13 PK-GAMMA,STK-2; COMPND 14 EC: 2.7.11.1; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 3 ORGANISM_TAXID: 9986; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: EXPI293; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 9 ORGANISM_TAXID: 9986; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_STRAIN: EXPI293; SOURCE 13 MOL_ID: 3; SOURCE 14 SYNTHETIC: YES; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606 KEYWDS PHOSPHORYLATED PEPTIDE, ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.M.M.CAAVEIRO,K.KASAHARA,K.TSUMOTO REVDAT 1 11-DEC-24 8ZXW 0 JRNL AUTH K.KASAHARA,R.KAWADE,M.NAKAKIDO,R.MATSUNAGA,H.AKIBA, JRNL AUTH 2 K.C.ENTZMINGER,T.MARUYAMA,S.C.J.OKUMURA,J.M.M.CAAVEIRO, JRNL AUTH 3 D.KURODA,K.TSUMOTO JRNL TITL ORIGIN OF HIGH BINDING AFFINITY AND SELECTIVITY OF JRNL TITL 2 PHOSPHORYLATED EPITOPE-SPECIFIC RABBIT ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.33 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0419 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) : 1.33 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.04 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5 REMARK 3 NUMBER OF REFLECTIONS : 188006 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.137 REMARK 3 FREE R VALUE : 0.165 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.086 REMARK 3 FREE R VALUE TEST SET COUNT : 9562 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.33 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.37 REMARK 3 REFLECTION IN BIN (WORKING SET) : 10028 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.90 REMARK 3 BIN R VALUE (WORKING SET) : 0.2120 REMARK 3 BIN FREE R VALUE SET COUNT : 564 REMARK 3 BIN FREE R VALUE : 0.2250 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6531 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 7 REMARK 3 SOLVENT ATOMS : 848 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.56 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.02300 REMARK 3 B22 (A**2) : -0.07400 REMARK 3 B33 (A**2) : -0.03100 REMARK 3 B12 (A**2) : -0.16600 REMARK 3 B13 (A**2) : 0.02200 REMARK 3 B23 (A**2) : 0.12500 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.050 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.028 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.537 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.971 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6874 ; 0.008 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 6248 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9474 ; 1.532 ; 1.788 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14501 ; 0.567 ; 1.718 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 938 ; 7.146 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 22 ; 7.496 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1031 ;10.046 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1142 ; 0.084 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8137 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1523 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1024 ; 0.228 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 63 ; 0.201 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3379 ; 0.174 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 578 ; 0.233 ; 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): 3578 ; 5.138 ; 1.950 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3578 ; 5.136 ; 1.950 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4477 ; 7.495 ; 3.495 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4478 ; 7.495 ; 3.495 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3296 ; 5.482 ; 2.092 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3297 ; 5.481 ; 2.092 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4961 ; 8.005 ; 3.766 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4962 ; 8.004 ; 3.767 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): 13122 ; 3.054 ; 3.000 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 : NULL 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 8ZXW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1300048734. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-NOV-23 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 : PHOTON FACTORY REMARK 200 BEAMLINE : BL-5A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 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 20230630 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.9 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 188006 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.330 REMARK 200 RESOLUTION RANGE LOW (A) : 48.040 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.04300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.33 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.35 REMARK 200 COMPLETENESS FOR SHELL (%) : 66.6 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : 0.46300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.8.3 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.84 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CHLORIDE 19% POLYETHYLENE REMARK 280 GLYCOL 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4730 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, C 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4500 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19060 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D 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 GLY H 135 REMARK 465 ASP H 136 REMARK 465 THR H 137 REMARK 465 SER H 217 REMARK 465 THR H 218 REMARK 465 CYS H 219 REMARK 465 SER H 220 REMARK 465 LYS H 221 REMARK 465 PRO H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 HIS H 226 REMARK 465 HIS H 227 REMARK 465 HIS H 228 REMARK 465 ARG C 1 REMARK 465 PRO C 2 REMARK 465 ALA C 15 REMARK 465 SER C 16 REMARK 465 ASP A 136 REMARK 465 THR A 137 REMARK 465 PRO A 138 REMARK 465 THR A 218 REMARK 465 CYS A 219 REMARK 465 SER A 220 REMARK 465 LYS A 221 REMARK 465 PRO A 222 REMARK 465 HIS A 223 REMARK 465 HIS A 224 REMARK 465 HIS A 225 REMARK 465 HIS A 226 REMARK 465 HIS A 227 REMARK 465 HIS A 228 REMARK 465 ARG D 1 REMARK 465 PRO D 2 REMARK 465 ALA D 15 REMARK 465 SER D 16 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 OG SER A 194 O HOH L 531 1554 1.97 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 ASP B 156 CG ASP B 156 OD2 0.271 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 ARG A 9 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ASN L 32 -24.94 69.93 REMARK 500 ALA L 53 -39.62 75.96 REMARK 500 LYS L 144 75.64 44.74 REMARK 500 CYS L 176 -0.56 75.42 REMARK 500 ASN B 32 -34.12 71.54 REMARK 500 ALA B 53 -40.68 72.69 REMARK 500 LYS B 144 77.15 44.58 REMARK 500 REMARK 500 REMARK: NULL DBREF 8ZXW H 1 228 PDB 8ZXW 8ZXW 1 228 DBREF 8ZXW L 1 217 PDB 8ZXW 8ZXW 1 217 DBREF 8ZXW C 1 16 UNP Q9Y243 AKT3_HUMAN 465 476 DBREF 8ZXW A 1 228 PDB 8ZXW 8ZXW 1 228 DBREF 8ZXW B 1 217 PDB 8ZXW 8ZXW 1 217 DBREF 8ZXW D 1 16 UNP Q9Y243 AKT3_HUMAN 465 476 SEQRES 1 H 228 GLN SER LEU GLU GLU SER GLY GLY ARG LEU VAL THR PRO SEQRES 2 H 228 GLY THR PRO LEU THR LEU THR CYS THR VAL SER GLY PHE SEQRES 3 H 228 SER LEU ASN ASN ASN ALA MET THR TRP VAL ARG GLN ALA SEQRES 4 H 228 PRO GLY LYS GLY LEU GLU TRP ILE GLY LEU ILE SER ARG SEQRES 5 H 228 SER GLY ILE THR HIS TYR ALA ASN TRP ALA LYS GLY ARG SEQRES 6 H 228 PHE THR ILE SER LYS THR SER THR THR VAL ASP LEU LYS SEQRES 7 H 228 ILE THR THR SER THR THR GLU ASP THR ALA THR TYR PHE SEQRES 8 H 228 CYS ALA ARG VAL ASP TYR ASP ASP TYR ARG ASP TRP GLY SEQRES 9 H 228 SER PHE ASN VAL TRP GLY PRO GLY THR LEU VAL THR VAL SEQRES 10 H 228 SER LEU GLY GLN PRO LYS ALA PRO SER VAL PHE PRO LEU SEQRES 11 H 228 ALA PRO CYS CYS GLY ASP THR PRO SER SER THR VAL THR SEQRES 12 H 228 LEU GLY CYS LEU VAL LYS GLY TYR LEU PRO GLU PRO VAL SEQRES 13 H 228 THR VAL THR TRP ASN SER GLY THR LEU THR ASN GLY VAL SEQRES 14 H 228 ARG THR PHE PRO SER VAL ARG GLN SER SER GLY LEU TYR SEQRES 15 H 228 SER LEU SER SER VAL VAL SER VAL THR SER SER SER GLN SEQRES 16 H 228 PRO VAL THR CYS ASN VAL ALA HIS PRO ALA THR ASN THR SEQRES 17 H 228 LYS VAL ASP LYS THR VAL ALA PRO SER THR CYS SER LYS SEQRES 18 H 228 PRO HIS HIS HIS HIS HIS HIS SEQRES 1 L 217 ALA ALA VAL LEU THR GLN THR PRO SER SER VAL SER SER SEQRES 2 L 217 ALA VAL GLY GLY THR VAL THR ILE ASN CYS GLN ALA SER SEQRES 3 L 217 GLN SER LEU TYR ASN ASN LYS ASN LEU ALA TRP TYR GLN SEQRES 4 L 217 GLN LYS PRO GLY GLN ARG PRO LYS LEU LEU ILE TYR SER SEQRES 5 L 217 ALA SER THR LEU ALA SER GLY VAL PRO SER ARG PHE SER SEQRES 6 L 217 GLY SER GLY SER GLY THR GLN PHE THR LEU THR ILE ASN SEQRES 7 L 217 GLY VAL GLN CYS ASP ASP ALA ALA THR TYR TYR CYS GLN SEQRES 8 L 217 GLY GLU PHE SER CYS SER SER ALA ASP CYS ASN ALA PHE SEQRES 9 L 217 GLY GLY GLY THR GLU VAL VAL VAL LYS GLY ASP PRO VAL SEQRES 10 L 217 ALA PRO THR VAL LEU ILE PHE PRO PRO ALA ALA ASP GLN SEQRES 11 L 217 VAL ALA THR GLY THR VAL THR ILE VAL CYS VAL ALA ASN SEQRES 12 L 217 LYS TYR PHE PRO ASP VAL THR VAL THR TRP GLU VAL ASP SEQRES 13 L 217 GLY THR THR GLN THR THR GLY ILE GLU ASN SER LYS THR SEQRES 14 L 217 PRO GLN ASN SER ALA ASP CYS THR TYR ASN LEU SER SER SEQRES 15 L 217 THR LEU THR LEU THR SER THR GLN TYR ASN SER HIS LYS SEQRES 16 L 217 GLU TYR THR CYS LYS VAL THR GLN GLY THR THR SER VAL SEQRES 17 L 217 VAL GLN SER PHE ASN ARG GLY ASP CYS SEQRES 1 C 12 ARG PRO HIS PHE PRO GLN PHE SEP TYR SER ALA SER SEQRES 1 A 228 GLN SER LEU GLU GLU SER GLY GLY ARG LEU VAL THR PRO SEQRES 2 A 228 GLY THR PRO LEU THR LEU THR CYS THR VAL SER GLY PHE SEQRES 3 A 228 SER LEU ASN ASN ASN ALA MET THR TRP VAL ARG GLN ALA SEQRES 4 A 228 PRO GLY LYS GLY LEU GLU TRP ILE GLY LEU ILE SER ARG SEQRES 5 A 228 SER GLY ILE THR HIS TYR ALA ASN TRP ALA LYS GLY ARG SEQRES 6 A 228 PHE THR ILE SER LYS THR SER THR THR VAL ASP LEU LYS SEQRES 7 A 228 ILE THR THR SER THR THR GLU ASP THR ALA THR TYR PHE SEQRES 8 A 228 CYS ALA ARG VAL ASP TYR ASP ASP TYR ARG ASP TRP GLY SEQRES 9 A 228 SER PHE ASN VAL TRP GLY PRO GLY THR LEU VAL THR VAL SEQRES 10 A 228 SER LEU GLY GLN PRO LYS ALA PRO SER VAL PHE PRO LEU SEQRES 11 A 228 ALA PRO CYS CYS GLY ASP THR PRO SER SER THR VAL THR SEQRES 12 A 228 LEU GLY CYS LEU VAL LYS GLY TYR LEU PRO GLU PRO VAL SEQRES 13 A 228 THR VAL THR TRP ASN SER GLY THR LEU THR ASN GLY VAL SEQRES 14 A 228 ARG THR PHE PRO SER VAL ARG GLN SER SER GLY LEU TYR SEQRES 15 A 228 SER LEU SER SER VAL VAL SER VAL THR SER SER SER GLN SEQRES 16 A 228 PRO VAL THR CYS ASN VAL ALA HIS PRO ALA THR ASN THR SEQRES 17 A 228 LYS VAL ASP LYS THR VAL ALA PRO SER THR CYS SER LYS SEQRES 18 A 228 PRO HIS HIS HIS HIS HIS HIS SEQRES 1 B 217 ALA ALA VAL LEU THR GLN THR PRO SER SER VAL SER SER SEQRES 2 B 217 ALA VAL GLY GLY THR VAL THR ILE ASN CYS GLN ALA SER SEQRES 3 B 217 GLN SER LEU TYR ASN ASN LYS ASN LEU ALA TRP TYR GLN SEQRES 4 B 217 GLN LYS PRO GLY GLN ARG PRO LYS LEU LEU ILE TYR SER SEQRES 5 B 217 ALA SER THR LEU ALA SER GLY VAL PRO SER ARG PHE SER SEQRES 6 B 217 GLY SER GLY SER GLY THR GLN PHE THR LEU THR ILE ASN SEQRES 7 B 217 GLY VAL GLN CYS ASP ASP ALA ALA THR TYR TYR CYS GLN SEQRES 8 B 217 GLY GLU PHE SER CYS SER SER ALA ASP CYS ASN ALA PHE SEQRES 9 B 217 GLY GLY GLY THR GLU VAL VAL VAL LYS GLY ASP PRO VAL SEQRES 10 B 217 ALA PRO THR VAL LEU ILE PHE PRO PRO ALA ALA ASP GLN SEQRES 11 B 217 VAL ALA THR GLY THR VAL THR ILE VAL CYS VAL ALA ASN SEQRES 12 B 217 LYS TYR PHE PRO ASP VAL THR VAL THR TRP GLU VAL ASP SEQRES 13 B 217 GLY THR THR GLN THR THR GLY ILE GLU ASN SER LYS THR SEQRES 14 B 217 PRO GLN ASN SER ALA ASP CYS THR TYR ASN LEU SER SER SEQRES 15 B 217 THR LEU THR LEU THR SER THR GLN TYR ASN SER HIS LYS SEQRES 16 B 217 GLU TYR THR CYS LYS VAL THR GLN GLY THR THR SER VAL SEQRES 17 B 217 VAL GLN SER PHE ASN ARG GLY ASP CYS SEQRES 1 D 12 ARG PRO HIS PHE PRO GLN PHE SEP TYR SER ALA SER MODRES 8ZXW SEP C 8 SER MODIFIED RESIDUE MODRES 8ZXW SEP D 8 SER MODIFIED RESIDUE HET SEP C 8 10 HET SEP D 8 10 HET GOL H 301 6 HET CL A 301 1 HETNAM SEP PHOSPHOSERINE HETNAM GOL GLYCEROL HETNAM CL CHLORIDE ION HETSYN SEP PHOSPHONOSERINE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 SEP 2(C3 H8 N O6 P) FORMUL 7 GOL C3 H8 O3 FORMUL 8 CL CL 1- FORMUL 9 HOH *848(H2 O) HELIX 1 AA1 SER H 27 ASN H 31 5 5 HELIX 2 AA2 THR H 83 THR H 87 5 5 HELIX 3 AA3 SER H 162 THR H 164 5 3 HELIX 4 AA4 PRO H 204 ASN H 207 5 4 HELIX 5 AA5 LEU L 29 LYS L 33 5 5 HELIX 6 AA6 GLN L 81 ALA L 85 5 5 HELIX 7 AA7 GLN L 130 THR L 133 5 4 HELIX 8 AA8 SER L 188 SER L 193 1 6 HELIX 9 AA9 GLY L 215 CYS L 217 5 3 HELIX 10 AB1 PRO C 5 TYR C 13 5 5 HELIX 11 AB2 THR A 83 THR A 87 5 5 HELIX 12 AB3 SER A 162 THR A 164 5 3 HELIX 13 AB4 PRO A 204 ASN A 207 5 4 HELIX 14 AB5 GLN B 81 ALA B 85 5 5 HELIX 15 AB6 GLN B 130 THR B 133 5 4 HELIX 16 AB7 SER B 188 ASN B 192 1 5 HELIX 17 AB8 GLY B 215 CYS B 217 5 3 HELIX 18 AB9 PRO D 5 TYR D 13 5 5 SHEET 1 AA1 4 SER H 2 SER H 6 0 SHEET 2 AA1 4 LEU H 17 SER H 24 -1 O SER H 24 N SER H 2 SHEET 3 AA1 4 THR H 74 ILE H 79 -1 O ILE H 79 N LEU H 17 SHEET 4 AA1 4 PHE H 66 LYS H 70 -1 N SER H 69 O ASP H 76 SHEET 1 AA2 6 LEU H 10 VAL H 11 0 SHEET 2 AA2 6 THR H 113 VAL H 117 1 O THR H 116 N VAL H 11 SHEET 3 AA2 6 ALA H 88 TYR H 97 -1 N ALA H 88 O VAL H 115 SHEET 4 AA2 6 MET H 33 GLN H 38 -1 N VAL H 36 O PHE H 91 SHEET 5 AA2 6 LEU H 44 ILE H 50 -1 O ILE H 50 N MET H 33 SHEET 6 AA2 6 THR H 56 TYR H 58 -1 O HIS H 57 N LEU H 49 SHEET 1 AA3 4 LEU H 10 VAL H 11 0 SHEET 2 AA3 4 THR H 113 VAL H 117 1 O THR H 116 N VAL H 11 SHEET 3 AA3 4 ALA H 88 TYR H 97 -1 N ALA H 88 O VAL H 115 SHEET 4 AA3 4 ASP H 102 TRP H 109 -1 O SER H 105 N ASP H 96 SHEET 1 AA4 4 SER H 126 LEU H 130 0 SHEET 2 AA4 4 THR H 141 TYR H 151 -1 O LYS H 149 N SER H 126 SHEET 3 AA4 4 TYR H 182 THR H 191 -1 O LEU H 184 N VAL H 148 SHEET 4 AA4 4 VAL H 169 THR H 171 -1 N ARG H 170 O VAL H 187 SHEET 1 AA5 4 SER H 126 LEU H 130 0 SHEET 2 AA5 4 THR H 141 TYR H 151 -1 O LYS H 149 N SER H 126 SHEET 3 AA5 4 TYR H 182 THR H 191 -1 O LEU H 184 N VAL H 148 SHEET 4 AA5 4 VAL H 175 ARG H 176 -1 N VAL H 175 O SER H 183 SHEET 1 AA6 3 THR H 157 TRP H 160 0 SHEET 2 AA6 3 VAL H 197 HIS H 203 -1 O ALA H 202 N THR H 157 SHEET 3 AA6 3 THR H 208 VAL H 214 -1 O VAL H 214 N VAL H 197 SHEET 1 AA7 4 LEU L 4 THR L 7 0 SHEET 2 AA7 4 THR L 18 ALA L 25 -1 O ASN L 22 N THR L 7 SHEET 3 AA7 4 GLN L 72 ASN L 78 -1 O PHE L 73 N CYS L 23 SHEET 4 AA7 4 PHE L 64 SER L 69 -1 N SER L 65 O THR L 76 SHEET 1 AA8 6 SER L 10 ALA L 14 0 SHEET 2 AA8 6 THR L 108 LYS L 113 1 O VAL L 111 N VAL L 11 SHEET 3 AA8 6 ALA L 86 GLU L 93 -1 N ALA L 86 O VAL L 110 SHEET 4 AA8 6 LEU L 35 GLN L 40 -1 N TYR L 38 O TYR L 89 SHEET 5 AA8 6 LYS L 47 TYR L 51 -1 O LEU L 49 N TRP L 37 SHEET 6 AA8 6 THR L 55 LEU L 56 -1 O THR L 55 N TYR L 51 SHEET 1 AA9 4 SER L 10 ALA L 14 0 SHEET 2 AA9 4 THR L 108 LYS L 113 1 O VAL L 111 N VAL L 11 SHEET 3 AA9 4 ALA L 86 GLU L 93 -1 N ALA L 86 O VAL L 110 SHEET 4 AA9 4 ASN L 102 PHE L 104 -1 O ALA L 103 N GLY L 92 SHEET 1 AB1 4 THR L 120 PHE L 124 0 SHEET 2 AB1 4 THR L 135 TYR L 145 -1 O ASN L 143 N THR L 120 SHEET 3 AB1 4 TYR L 178 THR L 187 -1 O TYR L 178 N TYR L 145 SHEET 4 AB1 4 ILE L 164 LYS L 168 -1 N SER L 167 O SER L 181 SHEET 1 AB2 4 THR L 158 THR L 159 0 SHEET 2 AB2 4 THR L 150 VAL L 155 -1 N VAL L 155 O THR L 158 SHEET 3 AB2 4 GLU L 196 GLN L 203 -1 O LYS L 200 N THR L 152 SHEET 4 AB2 4 THR L 206 ASN L 213 -1 O VAL L 208 N VAL L 201 SHEET 1 AB3 4 SER A 2 SER A 6 0 SHEET 2 AB3 4 LEU A 17 SER A 24 -1 O SER A 24 N SER A 2 SHEET 3 AB3 4 THR A 74 ILE A 79 -1 O ILE A 79 N LEU A 17 SHEET 4 AB3 4 PHE A 66 LYS A 70 -1 N SER A 69 O ASP A 76 SHEET 1 AB4 6 LEU A 10 VAL A 11 0 SHEET 2 AB4 6 THR A 113 VAL A 117 1 O THR A 116 N VAL A 11 SHEET 3 AB4 6 ALA A 88 TYR A 97 -1 N TYR A 90 O THR A 113 SHEET 4 AB4 6 MET A 33 GLN A 38 -1 N VAL A 36 O PHE A 91 SHEET 5 AB4 6 LEU A 44 ILE A 50 -1 O GLU A 45 N ARG A 37 SHEET 6 AB4 6 THR A 56 TYR A 58 -1 O HIS A 57 N LEU A 49 SHEET 1 AB5 4 LEU A 10 VAL A 11 0 SHEET 2 AB5 4 THR A 113 VAL A 117 1 O THR A 116 N VAL A 11 SHEET 3 AB5 4 ALA A 88 TYR A 97 -1 N TYR A 90 O THR A 113 SHEET 4 AB5 4 ASP A 102 TRP A 109 -1 O SER A 105 N ASP A 96 SHEET 1 AB6 4 SER A 126 LEU A 130 0 SHEET 2 AB6 4 THR A 141 TYR A 151 -1 O LYS A 149 N SER A 126 SHEET 3 AB6 4 TYR A 182 THR A 191 -1 O LEU A 184 N VAL A 148 SHEET 4 AB6 4 VAL A 169 THR A 171 -1 N ARG A 170 O VAL A 187 SHEET 1 AB7 4 SER A 126 LEU A 130 0 SHEET 2 AB7 4 THR A 141 TYR A 151 -1 O LYS A 149 N SER A 126 SHEET 3 AB7 4 TYR A 182 THR A 191 -1 O LEU A 184 N VAL A 148 SHEET 4 AB7 4 VAL A 175 ARG A 176 -1 N VAL A 175 O SER A 183 SHEET 1 AB8 3 THR A 157 TRP A 160 0 SHEET 2 AB8 3 VAL A 197 HIS A 203 -1 O ASN A 200 N THR A 159 SHEET 3 AB8 3 THR A 208 VAL A 214 -1 O VAL A 214 N VAL A 197 SHEET 1 AB9 4 LEU B 4 THR B 7 0 SHEET 2 AB9 4 THR B 18 ALA B 25 -1 O ASN B 22 N THR B 7 SHEET 3 AB9 4 GLN B 72 ASN B 78 -1 O PHE B 73 N CYS B 23 SHEET 4 AB9 4 PHE B 64 SER B 69 -1 N SER B 65 O THR B 76 SHEET 1 AC1 6 SER B 10 ALA B 14 0 SHEET 2 AC1 6 THR B 108 LYS B 113 1 O VAL B 111 N VAL B 11 SHEET 3 AC1 6 ALA B 86 GLU B 93 -1 N ALA B 86 O VAL B 110 SHEET 4 AC1 6 LEU B 35 GLN B 40 -1 N TYR B 38 O TYR B 89 SHEET 5 AC1 6 LYS B 47 TYR B 51 -1 O LEU B 49 N TRP B 37 SHEET 6 AC1 6 THR B 55 LEU B 56 -1 O THR B 55 N TYR B 51 SHEET 1 AC2 4 SER B 10 ALA B 14 0 SHEET 2 AC2 4 THR B 108 LYS B 113 1 O VAL B 111 N VAL B 11 SHEET 3 AC2 4 ALA B 86 GLU B 93 -1 N ALA B 86 O VAL B 110 SHEET 4 AC2 4 ASN B 102 PHE B 104 -1 O ALA B 103 N GLY B 92 SHEET 1 AC3 4 THR B 120 PHE B 124 0 SHEET 2 AC3 4 THR B 135 TYR B 145 -1 O ASN B 143 N THR B 120 SHEET 3 AC3 4 TYR B 178 THR B 187 -1 O LEU B 184 N ILE B 138 SHEET 4 AC3 4 ILE B 164 LYS B 168 -1 N SER B 167 O SER B 181 SHEET 1 AC4 4 THR B 158 THR B 159 0 SHEET 2 AC4 4 THR B 150 VAL B 155 -1 N VAL B 155 O THR B 158 SHEET 3 AC4 4 GLU B 196 GLN B 203 -1 O THR B 202 N THR B 150 SHEET 4 AC4 4 THR B 206 ASN B 213 -1 O VAL B 208 N VAL B 201 SSBOND 1 CYS H 21 CYS H 92 1555 1555 2.08 SSBOND 2 CYS H 133 CYS L 217 1555 1555 2.07 SSBOND 3 CYS H 146 CYS H 199 1555 1555 2.07 SSBOND 4 CYS L 23 CYS L 90 1555 1555 2.24 SSBOND 5 CYS L 82 CYS L 176 1555 1555 2.07 SSBOND 6 CYS L 96 CYS L 101 1555 1555 2.15 SSBOND 7 CYS L 140 CYS L 199 1555 1555 1.99 SSBOND 8 CYS A 21 CYS A 92 1555 1555 2.10 SSBOND 9 CYS A 133 CYS B 217 1555 1555 2.14 SSBOND 10 CYS A 146 CYS A 199 1555 1555 2.04 SSBOND 11 CYS B 23 CYS B 90 1555 1555 2.18 SSBOND 12 CYS B 82 CYS B 176 1555 1555 2.13 SSBOND 13 CYS B 96 CYS B 101 1555 1555 2.13 SSBOND 14 CYS B 140 CYS B 199 1555 1555 2.04 LINK C PHE C 7 N SEP C 8 1555 1555 1.34 LINK C SEP C 8 N TYR C 13 1555 1555 1.44 LINK C PHE D 7 N SEP D 8 1555 1555 1.34 LINK C SEP D 8 N TYR D 13 1555 1555 1.46 CISPEP 1 LEU H 152 PRO H 153 0 -13.03 CISPEP 2 GLU H 154 PRO H 155 0 -1.09 CISPEP 3 THR L 7 PRO L 8 0 -9.06 CISPEP 4 PHE L 146 PRO L 147 0 -0.45 CISPEP 5 PHE C 4 PRO C 5 0 -10.63 CISPEP 6 LEU A 152 PRO A 153 0 -12.66 CISPEP 7 GLU A 154 PRO A 155 0 -4.14 CISPEP 8 THR B 7 PRO B 8 0 -11.03 CISPEP 9 PHE B 146 PRO B 147 0 1.19 CISPEP 10 PHE D 4 PRO D 5 0 -13.04 CRYST1 54.351 67.841 71.341 112.54 104.99 98.31 P 1 2 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 0.018399 0.002688 0.006804 0.00000 SCALE2 0.000000 0.014897 0.007301 0.00000 SCALE3 0.000000 0.000000 0.016160 0.00000