HEADER IMMUNE SYSTEM 29-FEB-24 8S73 TITLE CRYSTAL STRUCTURE OF FAB-ANTICD43 MONOCLONAL ANTIBODY COMPLEXED TO A TITLE 2 BIS-TN GLYCOPEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: G2D11(VH-CH1); COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: COMPND 6 QVQLQQSDAELVKPGASVKISCKASGYIFADHAIHWVKRKPEQGLEWIGYISPGNDDIKYNEKFKGKAT COMPND 7 LTADKSSSTAYMQLNSLTSEDSAVYFCKRSLPGTFDYWGQGTTLTVSSAKTTPPSVYPLAPGSAAQTNS COMPND 8 MVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHPASS COMPND 9 TKVDKKIVP; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: ANTICD43(VL-CL); COMPND 12 CHAIN: B, D; COMPND 13 ENGINEERED: YES; COMPND 14 OTHER_DETAILS: COMPND 15 DYKDIQMTQSPASLSASVGETVTITCRASENIYSYLAWYQQKQGKSPQLLVYNAKTLAEGVPSRFSGSG COMPND 16 SGTQFSLKINSLQPEDFGSYYCQHHYGTPYTFGGGTKLEIKR COMPND 17 ADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSS COMPND 18 TLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR; COMPND 19 MOL_ID: 3; COMPND 20 MOLECULE: BIS-TN GLYCOPEPTIDE; COMPND 21 CHAIN: M, N; COMPND 22 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606 KEYWDS MONOCLONAL ANTIBODIES, FAB-ANTICD43, ANTIGEN TN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.HURTADO-GUERRERO,J.MACIAS-LEON REVDAT 1 25-JUN-25 8S73 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. 2.20 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) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 88.7 REMARK 3 NUMBER OF REFLECTIONS : 49943 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) : 0.197 REMARK 3 R VALUE (WORKING SET) : 0.195 REMARK 3 FREE R VALUE : 0.237 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2093 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) : 2.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2364 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.09 REMARK 3 BIN R VALUE (WORKING SET) : 0.3750 REMARK 3 BIN FREE R VALUE SET COUNT : 79 REMARK 3 BIN FREE R VALUE : 0.4000 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 : 68 REMARK 3 SOLVENT ATOMS : 143 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.25 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.59000 REMARK 3 B22 (A**2) : 0.59000 REMARK 3 B33 (A**2) : -1.92000 REMARK 3 B12 (A**2) : 0.30000 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): 0.246 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.202 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.177 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.751 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6785 ; 0.010 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 6155 ; 0.002 ; 0.015 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9240 ; 1.680 ; 1.673 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14319 ; 1.315 ; 1.612 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 835 ; 8.218 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 274 ;35.617 ;23.942 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1072 ;19.159 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;19.287 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 929 ; 0.065 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7575 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1455 ; 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): 3364 ; 4.306 ; 5.212 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3363 ; 4.307 ; 5.212 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4191 ; 6.133 ; 7.804 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4192 ; 6.133 ; 7.804 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3416 ; 5.604 ; 5.828 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3417 ; 5.603 ; 5.828 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5046 ; 8.460 ; 8.479 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6981 ;11.314 ;60.342 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6973 ;11.317 ;60.336 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 1 212 C 1 212 6210 0.08 0.05 REMARK 3 2 B 4 211 D 4 211 6414 0.08 0.05 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 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 8S73 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1292136961. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-MAY-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALBA REMARK 200 BEAMLINE : XALOC REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 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 : 52037 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 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 (%) : 88.6 REMARK 200 DATA REDUNDANCY : 9.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32 REMARK 200 COMPLETENESS FOR SHELL (%) : 73.9 REMARK 200 DATA REDUNDANCY IN SHELL : 8.90 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.100 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 (%): 58.55 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM MALONATE DIBASIC MONOHYDRATE, REMARK 280 PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-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 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 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 APPLY THE FOLLOWING TO CHAINS: A, B, 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 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 B 440 LIES ON A SPECIAL POSITION. REMARK 375 HOH D 429 LIES ON A SPECIAL POSITION. REMARK 375 HOH D 440 LIES ON A SPECIAL POSITION. REMARK 375 HOH D 442 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 GLY A 127 REMARK 465 SER A 128 REMARK 465 ALA A 129 REMARK 465 ALA A 130 REMARK 465 GLN A 131 REMARK 465 THR A 132 REMARK 465 ASN A 133 REMARK 465 ASP B -2 REMARK 465 TYR B -1 REMARK 465 LYS B 0 REMARK 465 GLY C 127 REMARK 465 SER C 128 REMARK 465 ALA C 129 REMARK 465 ALA C 130 REMARK 465 GLN C 131 REMARK 465 THR C 132 REMARK 465 ASN C 133 REMARK 465 ASP D -2 REMARK 465 TYR D -1 REMARK 465 LYS D 0 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 GLY M 5 C GLY M 5 O 0.136 REMARK 500 PRO M 7 CA PRO M 7 C -0.121 REMARK 500 GLY N 5 C GLY N 5 O 0.128 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 B 211 CA - C - O ANGL. DEV. = -20.9 DEGREES REMARK 500 PRO M 7 N - CD - CG ANGL. DEV. = -10.9 DEGREES REMARK 500 SER N 3 N - CA - CB ANGL. DEV. = -9.5 DEGREES REMARK 500 PRO N 7 C - N - CA ANGL. DEV. = 9.1 DEGREES REMARK 500 PRO N 7 CA - N - CD ANGL. DEV. = -11.3 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 ALA A 88 172.03 178.06 REMARK 500 SER A 95 -173.03 65.40 REMARK 500 TYR B 30 -117.93 59.71 REMARK 500 ALA B 51 -41.81 72.98 REMARK 500 ASN B 138 60.03 65.87 REMARK 500 SER C 76 59.00 39.65 REMARK 500 SER C 95 -169.90 63.14 REMARK 500 SER C 160 -17.32 -140.33 REMARK 500 TYR D 30 -124.36 55.88 REMARK 500 ALA D 51 -37.52 68.50 REMARK 500 GLU D 56 123.09 -38.64 REMARK 500 SER D 77 73.68 47.88 REMARK 500 SER M 6 73.10 -117.35 REMARK 500 ALA N 2 -90.85 65.54 REMARK 500 REMARK 500 REMARK: NULL DBREF 8S73 A 1 212 PDB 8S73 8S73 1 212 DBREF 8S73 B -2 211 PDB 8S73 8S73 -2 211 DBREF 8S73 C 1 212 PDB 8S73 8S73 1 212 DBREF 8S73 D -2 211 PDB 8S73 8S73 -2 211 DBREF 8S73 M 1 7 PDB 8S73 8S73 1 7 DBREF 8S73 N 1 7 PDB 8S73 8S73 1 7 SEQRES 1 A 216 GLN VAL GLN LEU GLN GLN SER ASP ALA GLU LEU VAL LYS SEQRES 2 A 216 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 A 216 TYR ILE PHE ALA ASP HIS ALA ILE HIS TRP VAL LYS ARG SEQRES 4 A 216 LYS PRO GLU GLN GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 A 216 PRO GLY ASN ASP ASP ILE LYS TYR ASN GLU LYS PHE LYS SEQRES 6 A 216 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 A 216 ALA TYR MET GLN LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 A 216 ALA VAL TYR PHE CYS LYS ARG SER LEU PRO GLY THR PHE SEQRES 9 A 216 ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER SEQRES 10 A 216 ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO SEQRES 11 A 216 GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY SEQRES 12 A 216 CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 A 216 THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR SEQRES 14 A 216 PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SEQRES 15 A 216 SER SER VAL THR VAL PRO SER SER THR TRP PRO SER GLU SEQRES 16 A 216 THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR SEQRES 17 A 216 LYS VAL ASP LYS LYS ILE VAL PRO SEQRES 1 B 214 ASP TYR LYS ASP ILE GLN MET THR GLN SER PRO ALA SER SEQRES 2 B 214 LEU SER ALA SER VAL GLY GLU THR VAL THR ILE THR CYS SEQRES 3 B 214 ARG ALA SER GLU ASN ILE TYR SER TYR LEU ALA TRP TYR SEQRES 4 B 214 GLN GLN LYS GLN GLY LYS SER PRO GLN LEU LEU VAL TYR SEQRES 5 B 214 ASN ALA LYS THR LEU ALA GLU GLY VAL PRO SER ARG PHE SEQRES 6 B 214 SER GLY SER GLY SER GLY THR GLN PHE SER LEU LYS ILE SEQRES 7 B 214 ASN SER LEU GLN PRO GLU ASP PHE GLY SER TYR TYR CYS SEQRES 8 B 214 GLN HIS HIS TYR GLY THR PRO TYR THR PHE GLY GLY GLY SEQRES 9 B 214 THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR SEQRES 10 B 214 VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR SER SEQRES 11 B 214 GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR SEQRES 12 B 214 PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER SEQRES 13 B 214 GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN SEQRES 14 B 214 ASP SER LYS ASP SER THR TYR SER MET SER SER THR LEU SEQRES 15 B 214 THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR SEQRES 16 B 214 THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO ILE SEQRES 17 B 214 VAL LYS SER PHE ASN ARG SEQRES 1 C 216 GLN VAL GLN LEU GLN GLN SER ASP ALA GLU LEU VAL LYS SEQRES 2 C 216 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 C 216 TYR ILE PHE ALA ASP HIS ALA ILE HIS TRP VAL LYS ARG SEQRES 4 C 216 LYS PRO GLU GLN GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 C 216 PRO GLY ASN ASP ASP ILE LYS TYR ASN GLU LYS PHE LYS SEQRES 6 C 216 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 C 216 ALA TYR MET GLN LEU ASN SER LEU THR SER GLU ASP SER SEQRES 8 C 216 ALA VAL TYR PHE CYS LYS ARG SER LEU PRO GLY THR PHE SEQRES 9 C 216 ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER SEQRES 10 C 216 ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO SEQRES 11 C 216 GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY SEQRES 12 C 216 CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 C 216 THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR SEQRES 14 C 216 PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SEQRES 15 C 216 SER SER VAL THR VAL PRO SER SER THR TRP PRO SER GLU SEQRES 16 C 216 THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR SEQRES 17 C 216 LYS VAL ASP LYS LYS ILE VAL PRO SEQRES 1 D 214 ASP TYR LYS ASP ILE GLN MET THR GLN SER PRO ALA SER SEQRES 2 D 214 LEU SER ALA SER VAL GLY GLU THR VAL THR ILE THR CYS SEQRES 3 D 214 ARG ALA SER GLU ASN ILE TYR SER TYR LEU ALA TRP TYR SEQRES 4 D 214 GLN GLN LYS GLN GLY LYS SER PRO GLN LEU LEU VAL TYR SEQRES 5 D 214 ASN ALA LYS THR LEU ALA GLU GLY VAL PRO SER ARG PHE SEQRES 6 D 214 SER GLY SER GLY SER GLY THR GLN PHE SER LEU LYS ILE SEQRES 7 D 214 ASN SER LEU GLN PRO GLU ASP PHE GLY SER TYR TYR CYS SEQRES 8 D 214 GLN HIS HIS TYR GLY THR PRO TYR THR PHE GLY GLY GLY SEQRES 9 D 214 THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR SEQRES 10 D 214 VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR SER SEQRES 11 D 214 GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR SEQRES 12 D 214 PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER SEQRES 13 D 214 GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN SEQRES 14 D 214 ASP SER LYS ASP SER THR TYR SER MET SER SER THR LEU SEQRES 15 D 214 THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR SEQRES 16 D 214 THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO ILE SEQRES 17 D 214 VAL LYS SER PHE ASN ARG SEQRES 1 M 7 GLY ALA SER THR GLY SER PRO SEQRES 1 N 7 GLY ALA SER THR GLY SER PRO HET GOL B 301 6 HET GOL D 301 6 HET A2G M 101 14 HET A2G M 102 14 HET A2G N 101 14 HET A2G N 102 14 HETNAM GOL GLYCEROL HETNAM A2G 2-ACETAMIDO-2-DEOXY-ALPHA-D-GALACTOPYRANOSE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL 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 7 GOL 2(C3 H8 O3) FORMUL 9 A2G 4(C8 H15 N O6) FORMUL 13 HOH *143(H2 O) HELIX 1 AA1 ILE A 28 HIS A 32 5 5 HELIX 2 AA2 PRO A 53 ASP A 56 5 4 HELIX 3 AA3 GLU A 61 LYS A 64 5 4 HELIX 4 AA4 LYS A 73 SER A 75 5 3 HELIX 5 AA5 THR A 83 SER A 87 5 5 HELIX 6 AA6 SER A 156 SER A 158 5 3 HELIX 7 AA7 PRO A 200 SER A 203 5 4 HELIX 8 AA8 GLN B 79 PHE B 83 5 5 HELIX 9 AA9 SER B 121 SER B 127 1 7 HELIX 10 AB1 LYS B 183 GLU B 187 1 5 HELIX 11 AB2 ILE C 28 HIS C 32 5 5 HELIX 12 AB3 GLU C 61 LYS C 64 5 4 HELIX 13 AB4 LYS C 73 SER C 75 5 3 HELIX 14 AB5 THR C 83 SER C 87 5 5 HELIX 15 AB6 SER C 156 SER C 158 5 3 HELIX 16 AB7 PRO C 200 SER C 203 5 4 HELIX 17 AB8 GLN D 79 PHE D 83 5 5 HELIX 18 AB9 SER D 121 SER D 127 1 7 HELIX 19 AC1 LYS D 183 GLU D 187 1 5 SHEET 1 AA1 4 GLN A 3 GLN A 5 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 THR A 70 O TYR A 79 SHEET 1 AA2 6 ALA A 9 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 HIS A 35 O LYS A 93 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 ALA A 9 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 SER A 120 LEU A 124 0 SHEET 2 AA4 4 MET A 135 TYR A 145 -1 O LEU A 141 N TYR A 122 SHEET 3 AA4 4 LEU A 174 PRO A 184 -1 O VAL A 183 N VAL A 136 SHEET 4 AA4 4 VAL A 163 THR A 165 -1 N HIS A 164 O SER A 180 SHEET 1 AA5 4 SER A 120 LEU A 124 0 SHEET 2 AA5 4 MET A 135 TYR A 145 -1 O LEU A 141 N TYR A 122 SHEET 3 AA5 4 LEU A 174 PRO A 184 -1 O VAL A 183 N VAL A 136 SHEET 4 AA5 4 VAL A 169 GLN A 171 -1 N VAL A 169 O THR A 176 SHEET 1 AA6 3 THR A 151 TRP A 154 0 SHEET 2 AA6 3 THR A 194 HIS A 199 -1 O ASN A 196 N THR A 153 SHEET 3 AA6 3 THR A 204 LYS A 209 -1 O VAL A 206 N VAL A 197 SHEET 1 AA7 4 MET B 4 SER B 7 0 SHEET 2 AA7 4 VAL B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AA7 4 GLN B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AA7 4 PHE B 62 SER B 67 -1 N SER B 63 O LYS B 74 SHEET 1 AA8 6 SER B 10 SER B 14 0 SHEET 2 AA8 6 THR B 102 LYS B 107 1 O GLU B 105 N LEU B 11 SHEET 3 AA8 6 GLY B 84 HIS B 90 -1 N GLY B 84 O LEU B 104 SHEET 4 AA8 6 LEU B 33 GLN B 38 -1 N ALA B 34 O GLN B 89 SHEET 5 AA8 6 GLN B 45 TYR B 49 -1 O GLN B 45 N GLN B 37 SHEET 6 AA8 6 THR B 53 LEU B 54 -1 O THR B 53 N TYR B 49 SHEET 1 AA9 4 THR B 114 PHE B 118 0 SHEET 2 AA9 4 GLY B 129 PHE B 139 -1 O ASN B 137 N THR B 114 SHEET 3 AA9 4 TYR B 173 THR B 182 -1 O LEU B 181 N ALA B 130 SHEET 4 AA9 4 VAL B 159 TRP B 163 -1 N SER B 162 O SER B 176 SHEET 1 AB1 4 SER B 153 ARG B 155 0 SHEET 2 AB1 4 ASN B 145 ILE B 150 -1 N ILE B 150 O SER B 153 SHEET 3 AB1 4 SER B 191 THR B 197 -1 O THR B 193 N LYS B 149 SHEET 4 AB1 4 ILE B 205 ASN B 210 -1 O ILE B 205 N ALA B 196 SHEET 1 AB2 4 GLN C 3 GLN C 5 0 SHEET 2 AB2 4 VAL C 18 SER C 25 -1 O LYS C 23 N GLN C 5 SHEET 3 AB2 4 THR C 77 LEU C 82 -1 O ALA C 78 N CYS C 22 SHEET 4 AB2 4 ALA C 67 ASP C 72 -1 N THR C 70 O TYR C 79 SHEET 1 AB3 6 ALA C 9 VAL C 12 0 SHEET 2 AB3 6 THR C 107 VAL C 111 1 O THR C 110 N GLU C 10 SHEET 3 AB3 6 ALA C 88 ARG C 94 -1 N ALA C 88 O LEU C 109 SHEET 4 AB3 6 ILE C 34 ARG C 39 -1 N HIS C 35 O LYS C 93 SHEET 5 AB3 6 LEU C 45 SER C 52 -1 O ILE C 48 N TRP C 36 SHEET 6 AB3 6 ASP C 56A TYR C 59 -1 O ASP C 56A N SER C 52 SHEET 1 AB4 4 ALA C 9 VAL C 12 0 SHEET 2 AB4 4 THR C 107 VAL C 111 1 O THR C 110 N GLU C 10 SHEET 3 AB4 4 ALA C 88 ARG C 94 -1 N ALA C 88 O LEU C 109 SHEET 4 AB4 4 TYR C 102 TRP C 103 -1 O TYR C 102 N ARG C 94 SHEET 1 AB5 4 SER C 120 LEU C 124 0 SHEET 2 AB5 4 MET C 135 TYR C 145 -1 O LEU C 141 N TYR C 122 SHEET 3 AB5 4 LEU C 174 PRO C 184 -1 O VAL C 183 N VAL C 136 SHEET 4 AB5 4 VAL C 163 THR C 165 -1 N HIS C 164 O SER C 180 SHEET 1 AB6 4 SER C 120 LEU C 124 0 SHEET 2 AB6 4 MET C 135 TYR C 145 -1 O LEU C 141 N TYR C 122 SHEET 3 AB6 4 LEU C 174 PRO C 184 -1 O VAL C 183 N VAL C 136 SHEET 4 AB6 4 VAL C 169 GLN C 171 -1 N VAL C 169 O THR C 176 SHEET 1 AB7 3 THR C 151 TRP C 154 0 SHEET 2 AB7 3 THR C 194 HIS C 199 -1 O ASN C 196 N THR C 153 SHEET 3 AB7 3 THR C 204 LYS C 209 -1 O VAL C 206 N VAL C 197 SHEET 1 AB8 4 MET D 4 SER D 7 0 SHEET 2 AB8 4 VAL D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AB8 4 GLN D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 4 AB8 4 PHE D 62 SER D 67 -1 N SER D 63 O LYS D 74 SHEET 1 AB9 6 SER D 10 SER D 14 0 SHEET 2 AB9 6 THR D 102 LYS D 107 1 O GLU D 105 N LEU D 11 SHEET 3 AB9 6 GLY D 84 HIS D 90 -1 N GLY D 84 O LEU D 104 SHEET 4 AB9 6 LEU D 33 GLN D 38 -1 N ALA D 34 O GLN D 89 SHEET 5 AB9 6 GLN D 45 TYR D 49 -1 O GLN D 45 N GLN D 37 SHEET 6 AB9 6 THR D 53 LEU D 54 -1 O THR D 53 N TYR D 49 SHEET 1 AC1 4 THR D 114 PHE D 118 0 SHEET 2 AC1 4 GLY D 129 PHE D 139 -1 O ASN D 137 N THR D 114 SHEET 3 AC1 4 TYR D 173 THR D 182 -1 O LEU D 181 N ALA D 130 SHEET 4 AC1 4 VAL D 159 TRP D 163 -1 N SER D 162 O SER D 176 SHEET 1 AC2 4 SER D 153 ARG D 155 0 SHEET 2 AC2 4 ILE D 144 ILE D 150 -1 N ILE D 150 O SER D 153 SHEET 3 AC2 4 SER D 191 HIS D 198 -1 O THR D 193 N LYS D 149 SHEET 4 AC2 4 ILE D 205 ASN D 210 -1 O ILE D 205 N ALA D 196 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.08 SSBOND 2 CYS A 140 CYS A 195 1555 1555 2.00 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.16 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.01 SSBOND 5 CYS C 22 CYS C 92 1555 1555 2.07 SSBOND 6 CYS C 140 CYS C 195 1555 1555 2.03 SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.15 SSBOND 8 CYS D 134 CYS D 194 1555 1555 2.02 LINK OG SER M 3 C1 A2G M 101 1555 1555 1.49 LINK OG1 THR M 4 C1 A2G M 102 1555 1555 1.40 LINK OG SER N 3 C1 A2G N 101 1555 1555 1.43 LINK OG1 THR N 4 C1 A2G N 102 1555 1555 1.45 CISPEP 1 PHE A 146 PRO A 147 0 -10.64 CISPEP 2 GLU A 148 PRO A 149 0 -0.51 CISPEP 3 TRP A 188 PRO A 189 0 7.70 CISPEP 4 SER B 7 PRO B 8 0 -3.50 CISPEP 5 THR B 94 PRO B 95 0 -7.88 CISPEP 6 TYR B 140 PRO B 141 0 -0.02 CISPEP 7 PHE C 146 PRO C 147 0 -10.19 CISPEP 8 GLU C 148 PRO C 149 0 0.70 CISPEP 9 TRP C 188 PRO C 189 0 6.55 CISPEP 10 SER D 7 PRO D 8 0 -5.43 CISPEP 11 THR D 94 PRO D 95 0 -8.01 CISPEP 12 TYR D 140 PRO D 141 0 1.21 CISPEP 13 SER M 6 PRO M 7 0 -0.99 CRYST1 100.525 100.525 194.767 90.00 90.00 120.00 P 3 2 1 12 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 0.009948 0.005743 0.000000 0.00000 SCALE2 0.000000 0.011487 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005134 0.00000