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HEADER PROTEIN BINDING 07-OCT-24 9JU4
TITLE CRYSTAL STRUCTURE OF THE THERMOTOGA MARITIMA COLD SHOCK PROTEIN MUTANT
TITLE 2 EST#13 IN COMPLEX WITH AACEST
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD-3 DOMAIN PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: THE THERMOTOGA MARITIMA COLD SHOCK PROTEIN MUTANT BINDING
COMPND 7 TO AACEST;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ALICYCLOBACILLUS ACIDOCALDARIUS;
SOURCE 3 ORGANISM_TAXID: 405212;
SOURCE 4 GENE: AACI_2875;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 9 ORGANISM_TAXID: 2336;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ANTIBODY-MIMICS, COLD SHOCK PROTEIN, REFOLDING, HEAT STERILIZATION,
KEYWDS 2 FREEZE-DRYING, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.-I.TANAKA,H.AMESAKA
REVDAT 1 15-JAN-25 9JU4 0
JRNL AUTH H.AMESAKA,M.TACHIBANA,M.HARA,S.TOYA,H.NAKAGAWA,H.MATSUMURA,
JRNL AUTH 2 A.HIRATA,M.FUJIHASHI,K.TAKANO,S.I.TANAKA
JRNL TITL HEAT-STERILIZABLE ANTIBODY MIMICS DESIGNED ON THE COLD SHOCK
JRNL TITL 2 PROTEIN SCAFFOLD FROM HYPERTHERMOPHILE THERMOTOGA MARITIMA.
JRNL REF PROTEIN SCI. V. 34 70018 2025
JRNL REFN ESSN 1469-896X
JRNL PMID 39724358
JRNL DOI 10.1002/PRO.70018
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.17.1_3660: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 28793
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.080
REMARK 3 FREE R VALUE TEST SET COUNT : 886
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.6500 - 3.6300 0.97 4674 155 0.1568 0.1999
REMARK 3 2 3.6300 - 2.8800 0.99 4669 148 0.1736 0.1996
REMARK 3 3 2.8800 - 2.5200 0.99 4644 152 0.1823 0.2188
REMARK 3 4 2.5200 - 2.2900 0.99 4649 140 0.1777 0.2392
REMARK 3 5 2.2900 - 2.1300 0.99 4618 145 0.1774 0.2008
REMARK 3 6 2.1300 - 2.0000 1.00 4653 146 0.1709 0.2041
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2939
REMARK 3 ANGLE : 0.873 3995
REMARK 3 CHIRALITY : 0.055 424
REMARK 3 PLANARITY : 0.005 524
REMARK 3 DIHEDRAL : 7.288 400
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9JU4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-OCT-24.
REMARK 100 THE DEPOSITION ID IS D_1300052253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28793
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.520
REMARK 200 RESOLUTION RANGE LOW (A) : 46.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.380
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NEEDLE-LIKE CRYSTALS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, PH 5.0, AND 20%
REMARK 280 (W/V) PEG8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -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 -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 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: 2310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 621 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 LYS B 19
REMARK 465 ASP B 20
REMARK 465 GLU B 21
REMARK 465 GLY B 22
REMARK 465 GLY B 23
REMARK 465 MET B 34
REMARK 465 GLU B 35
REMARK 465 GLY B 36
REMARK 465 PHE B 37
REMARK 465 VAL B 54
REMARK 465 ALA B 55
REMARK 465 ASN B 56
REMARK 465 VAL B 65
REMARK 465 VAL B 66
REMARK 465 GLU B 67
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 ASP A 89 -169.34 -163.17
REMARK 500 SER A 155 -119.77 59.84
REMARK 500 PHE A 178 145.77 -171.24
REMARK 500 TYR A 183 65.85 27.22
REMARK 500 SER A 185 78.21 -102.64
REMARK 500 LEU A 205 -68.19 76.25
REMARK 500 SER A 231 78.94 -117.00
REMARK 500 SER A 289 -17.56 65.21
REMARK 500 SER B 52 33.20 -95.39
REMARK 500 HIS B 62 73.23 41.66
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9JU4 A 1 310 UNP C8WUR3 C8WUR3_ALIAD 1 310
DBREF 9JU4 B 2 67 PDB 9JU4 9JU4 2 67
SEQRES 1 A 310 MET PRO LEU ASP PRO VAL ILE GLN GLN VAL LEU ASP GLN
SEQRES 2 A 310 LEU ASN ARG MET PRO ALA PRO ASP TYR LYS HIS LEU SER
SEQRES 3 A 310 ALA GLN GLN PHE ARG SER GLN GLN SER LEU PHE PRO PRO
SEQRES 4 A 310 VAL LYS LYS GLU PRO VAL ALA GLU VAL ARG GLU PHE ASP
SEQRES 5 A 310 MET ASP LEU PRO GLY ARG THR LEU LYS VAL ARG MET TYR
SEQRES 6 A 310 ARG PRO GLU GLY VAL GLU PRO PRO TYR PRO ALA LEU VAL
SEQRES 7 A 310 TYR TYR HIS GLY GLY GLY TRP VAL VAL GLY ASP LEU GLU
SEQRES 8 A 310 THR HIS ASP PRO VAL CYS ARG VAL LEU ALA LYS ASP GLY
SEQRES 9 A 310 ARG ALA VAL VAL PHE SER VAL ASP TYR ARG LEU ALA PRO
SEQRES 10 A 310 GLU HIS LYS PHE PRO ALA ALA VAL GLU ASP ALA TYR ASP
SEQRES 11 A 310 ALA LEU GLN TRP ILE ALA GLU ARG ALA ALA ASP PHE HIS
SEQRES 12 A 310 LEU ASP PRO ALA ARG ILE ALA VAL GLY GLY ASP SER ALA
SEQRES 13 A 310 GLY GLY ASN LEU ALA ALA VAL THR SER ILE LEU ALA LYS
SEQRES 14 A 310 GLU ARG GLY GLY PRO ALA ILE ALA PHE GLN LEU LEU ILE
SEQRES 15 A 310 TYR PRO SER THR GLY TYR ASP PRO ALA HIS PRO PRO ALA
SEQRES 16 A 310 SER ILE GLU GLU ASN ALA GLU GLY TYR LEU LEU THR GLY
SEQRES 17 A 310 GLY MET MET LEU TRP PHE ARG ASP GLN TYR LEU ASN SER
SEQRES 18 A 310 LEU GLU GLU LEU THR HIS PRO TRP PHE SER PRO VAL LEU
SEQRES 19 A 310 TYR PRO ASP LEU SER GLY LEU PRO PRO ALA TYR ILE ALA
SEQRES 20 A 310 THR ALA GLN TYR ASP PRO LEU ARG ASP VAL GLY LYS LEU
SEQRES 21 A 310 TYR ALA GLU ALA LEU ASN LYS ALA GLY VAL LYS VAL GLU
SEQRES 22 A 310 ILE GLU ASN PHE GLU ASP LEU ILE HIS GLY PHE ALA GLN
SEQRES 23 A 310 PHE TYR SER LEU SER PRO GLY ALA THR LYS ALA LEU VAL
SEQRES 24 A 310 ARG ILE ALA GLU LYS LEU ARG ASP ALA LEU ALA
SEQRES 1 B 66 ARG GLY LYS VAL LYS TRP PHE HIS ASP TYR TYR GLY TYR
SEQRES 2 B 66 GLY PHE ILE THR LYS ASP GLU GLY GLY ASP VAL PHE VAL
SEQRES 3 B 66 ASN ALA ASP ALA ILE ASP MET GLU GLY PHE LYS THR LEU
SEQRES 4 B 66 LYS GLU GLY GLN VAL VAL GLU PHE GLU ILE ASP SER THR
SEQRES 5 B 66 VAL ALA ASN ALA PRO GLN ALA ALA HIS VAL LYS VAL VAL
SEQRES 6 B 66 GLU
HET PMS A 401 10
HET PEG A 402 7
HET GOL A 403 6
HETNAM PMS PHENYLMETHANESULFONIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 PMS C7 H8 O3 S
FORMUL 4 PEG C4 H10 O3
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *176(H2 O)
HELIX 1 AA1 ASP A 4 ASN A 15 1 12
HELIX 2 AA2 SER A 26 GLN A 33 1 8
HELIX 3 AA3 HIS A 93 ARG A 105 1 13
HELIX 4 AA4 PRO A 122 ARG A 138 1 17
HELIX 5 AA5 SER A 155 ARG A 171 1 17
HELIX 6 AA6 PRO A 194 ASN A 200 1 7
HELIX 7 AA7 THR A 207 LEU A 219 1 13
HELIX 8 AA8 SER A 221 HIS A 227 5 7
HELIX 9 AA9 SER A 231 TYR A 235 5 5
HELIX 10 AB1 LEU A 254 ALA A 268 1 15
HELIX 11 AB2 GLY A 283 TYR A 288 5 6
HELIX 12 AB3 SER A 291 ALA A 310 1 20
HELIX 13 AB4 ASP B 30 ILE B 32 5 3
SHEET 1 AA1 8 GLU A 47 LEU A 55 0
SHEET 2 AA1 8 ARG A 58 ARG A 66 -1 O LEU A 60 N MET A 53
SHEET 3 AA1 8 VAL A 107 VAL A 111 -1 O SER A 110 N ARG A 63
SHEET 4 AA1 8 TYR A 74 TYR A 80 1 N TYR A 79 O PHE A 109
SHEET 5 AA1 8 LEU A 144 ASP A 154 1 O ALA A 150 N ALA A 76
SHEET 6 AA1 8 GLN A 179 ILE A 182 1 O ILE A 182 N GLY A 153
SHEET 7 AA1 8 ALA A 244 ALA A 249 1 O TYR A 245 N LEU A 181
SHEET 8 AA1 8 VAL A 272 PHE A 277 1 O PHE A 277 N THR A 248
SHEET 1 AA2 6 GLY B 3 HIS B 9 0
SHEET 2 AA2 6 TYR B 14 THR B 18 -1 O TYR B 14 N HIS B 9
SHEET 3 AA2 6 VAL B 25 ASN B 28 -1 O VAL B 25 N ILE B 17
SHEET 4 AA2 6 GLN B 59 LYS B 64 1 O ALA B 60 N PHE B 26
SHEET 5 AA2 6 VAL B 45 ASP B 51 -1 N GLU B 49 O ALA B 61
SHEET 6 AA2 6 GLY B 3 HIS B 9 -1 N GLY B 3 O VAL B 46
LINK OG SER A 155 S PMS A 401 1555 1555 1.48
CISPEP 1 PRO A 72 PRO A 73 0 -5.15
CISPEP 2 ALA A 116 PRO A 117 0 1.27
CISPEP 3 PHE A 121 PRO A 122 0 3.03
CISPEP 4 GLY A 173 PRO A 174 0 0.58
CRYST1 45.820 46.650 101.260 90.00 93.99 90.00 P 1 2 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 0.021825 0.000000 0.001524 0.00000
SCALE2 0.000000 0.021436 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009900 0.00000
TER 2428 ALA A 310
TER 2841 LYS B 64
MASTER 246 0 3 13 14 0 0 6 3038 2 24 30
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