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HEADER HYDROLASE 09-DEC-25 21DL
TITLE CRYSTAL STRUCTURE OF DE NOVO DESIGNED ESTERASE RPA1511-5221
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RPA1511_5221;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 3 ORGANISM_TAXID: 32644;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLYASE, DE NOVO DESIGNED, THERMOSTABLE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.WANG,R.LIU
REVDAT 1 01-APR-26 21DL 0
JRNL AUTH R.LIU,S.LI,P.ZHENG
JRNL TITL ENHANCED EFFICIENCY AND THERMOSTABILITY OF AN ESTERASE
JRNL TITL 2 RPA1511 FOR POLYLACTIC ACID DEPOLYMERIZATION BY PLACER AND
JRNL TITL 3 PROTEINMPNN.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21.2_5419
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 15373
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.680
REMARK 3 FREE R VALUE TEST SET COUNT : 720
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 48.3300 - 5.6400 1.00 3126 150 0.2140 0.2475
REMARK 3 2 5.6400 - 4.4800 1.00 2924 153 0.2037 0.2332
REMARK 3 3 4.4800 - 3.9100 1.00 2891 138 0.2015 0.2712
REMARK 3 4 3.9100 - 3.5500 1.00 2867 144 0.2386 0.3173
REMARK 3 5 3.5500 - 3.3000 1.00 2845 135 0.2684 0.3372
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.475
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 : 0.002 4674
REMARK 3 ANGLE : 0.510 6368
REMARK 3 CHIRALITY : 0.043 706
REMARK 3 PLANARITY : 0.006 840
REMARK 3 DIHEDRAL : 11.659 1748
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 : 1
REMARK 3 NCS GROUP : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : chain "A"
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : chain "B"
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 21DL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 17-DEC-25.
REMARK 100 THE DEPOSITION ID IS D_1300067016.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-25
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 : SSRF
REMARK 200 BEAMLINE : BL02U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : POINTLESS, AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15490
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 48.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 31.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.56
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 : 2.000
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 (%): 64.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M SUCCINC ACID PH 7.0, 0.1 M HEPES
REMARK 280 PH 7.0, 1% W/V PEG MONOMETHYL ETHER 2000, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 139.57400
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 69.78700
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 104.68050
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 34.89350
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 174.46750
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 139.57400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 69.78700
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 34.89350
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 104.68050
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 174.46750
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 B 415 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 MET A 1
REMARK 465 TRP A 2
REMARK 465 SER A 3
REMARK 465 HIS A 4
REMARK 465 PRO A 5
REMARK 465 GLN A 6
REMARK 465 PHE A 7
REMARK 465 GLU A 8
REMARK 465 LYS A 9
REMARK 465 GLY A 10
REMARK 465 SER A 11
REMARK 465 GLY A 12
REMARK 465 LEU A 308
REMARK 465 GLU A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 MET B 1
REMARK 465 TRP B 2
REMARK 465 SER B 3
REMARK 465 HIS B 4
REMARK 465 PRO B 5
REMARK 465 GLN B 6
REMARK 465 PHE B 7
REMARK 465 GLU B 8
REMARK 465 LYS B 9
REMARK 465 GLY B 10
REMARK 465 SER B 11
REMARK 465 GLY B 12
REMARK 465 LEU B 308
REMARK 465 GLU B 309
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
REMARK 465 HIS B 313
REMARK 465 HIS B 314
REMARK 465 HIS B 315
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 62 -160.30 -104.88
REMARK 500 SER A 63 -164.54 -162.37
REMARK 500 SER A 126 -120.21 56.55
REMARK 500 TYR A 156 100.19 58.28
REMARK 500 ALA A 163 99.60 74.05
REMARK 500 LEU A 283 59.26 -104.69
REMARK 500 ALA B 62 -160.01 -104.26
REMARK 500 SER B 63 -164.47 -162.15
REMARK 500 SER B 126 -121.82 56.22
REMARK 500 ALA B 168 -50.53 67.50
REMARK 500 LEU B 283 58.82 -104.75
REMARK 500
REMARK 500 REMARK: NULL
DBREF 21DL A 1 315 PDB 21DL 21DL 1 315
DBREF 21DL B 1 315 PDB 21DL 21DL 1 315
SEQRES 1 A 315 MET TRP SER HIS PRO GLN PHE GLU LYS GLY SER GLY SER
SEQRES 2 A 315 ARG ASP LEU ASP TRP ALA VAL ASP GLY GLN ASP TRP PRO
SEQRES 3 A 315 HIS ARG GLU ALA SER ARG PHE ILE GLU ALA GLY GLY ILE
SEQRES 4 A 315 ARG TRP HIS VAL GLN LEU LEU GLY SER PRO GLU ALA PRO
SEQRES 5 A 315 ALA LEU LEU LEU ILE HIS GLY THR GLY ALA SER SER HIS
SEQRES 6 A 315 SER TRP ARG GLY LEU ALA PRO LEU LEU SER LYS ARG TYR
SEQRES 7 A 315 HIS VAL VAL ALA PRO ASP LEU PRO GLY HIS GLY PHE THR
SEQRES 8 A 315 GLU THR PRO PRO GLU GLU ARG LEU SER LEU PRO GLY MET
SEQRES 9 A 315 ALA GLU LEU LEU ALA GLU LEU LEU ARG GLU LEU LYS VAL
SEQRES 10 A 315 GLN PRO GLU ILE VAL ILE GLY HIS SER ALA GLY ALA ALA
SEQRES 11 A 315 ILE ALA ALA ARG MET ALA LEU ASP GLY LEU ILE GLN PRO
SEQRES 12 A 315 GLN ILE ILE PHE ALA LEU ASN GLY ALA PHE LEU PRO TYR
SEQRES 13 A 315 GLY GLY GLU ALA TYR ALA ALA PHE LYS PRO ILE ALA ARG
SEQRES 14 A 315 ALA LEU ALA ALA ASN PRO GLU THR PRO ARG ARG PHE ALA
SEQRES 15 A 315 GLU ARG ALA ALA GLU PRO GLY ALA VAL GLU ARG LEU ILE
SEQRES 16 A 315 ALA SER THR GLY SER THR ILE ASP ALA GLU GLY LEU ALA
SEQRES 17 A 315 HIS TYR ARG LYS LEU TRP SER SER PRO ARG HIS VAL GLY
SEQRES 18 A 315 ALA ALA LEU THR MET MET ALA ASN TRP ASP LEU GLU PRO
SEQRES 19 A 315 LEU LEU GLU ARG LEU PRO GLU LEU LYS PRO LEU LEU VAL
SEQRES 20 A 315 LEU VAL ALA ALA GLU LYS ASP LYS ALA VAL PRO PRO GLU
SEQRES 21 A 315 VAL ALA GLU ARG VAL LYS GLU LEU LEU PRO ARG ALA GLU
SEQRES 22 A 315 ILE VAL ARG ILE PRO ALA LEU GLY HIS LEU ALA HIS GLU
SEQRES 23 A 315 GLU ASP PRO GLU LEU ILE ALA ARG LEU ILE GLU GLU HIS
SEQRES 24 A 315 VAL GLU ARG LEU GLU ALA GLN ARG LEU GLU HIS HIS HIS
SEQRES 25 A 315 HIS HIS HIS
SEQRES 1 B 315 MET TRP SER HIS PRO GLN PHE GLU LYS GLY SER GLY SER
SEQRES 2 B 315 ARG ASP LEU ASP TRP ALA VAL ASP GLY GLN ASP TRP PRO
SEQRES 3 B 315 HIS ARG GLU ALA SER ARG PHE ILE GLU ALA GLY GLY ILE
SEQRES 4 B 315 ARG TRP HIS VAL GLN LEU LEU GLY SER PRO GLU ALA PRO
SEQRES 5 B 315 ALA LEU LEU LEU ILE HIS GLY THR GLY ALA SER SER HIS
SEQRES 6 B 315 SER TRP ARG GLY LEU ALA PRO LEU LEU SER LYS ARG TYR
SEQRES 7 B 315 HIS VAL VAL ALA PRO ASP LEU PRO GLY HIS GLY PHE THR
SEQRES 8 B 315 GLU THR PRO PRO GLU GLU ARG LEU SER LEU PRO GLY MET
SEQRES 9 B 315 ALA GLU LEU LEU ALA GLU LEU LEU ARG GLU LEU LYS VAL
SEQRES 10 B 315 GLN PRO GLU ILE VAL ILE GLY HIS SER ALA GLY ALA ALA
SEQRES 11 B 315 ILE ALA ALA ARG MET ALA LEU ASP GLY LEU ILE GLN PRO
SEQRES 12 B 315 GLN ILE ILE PHE ALA LEU ASN GLY ALA PHE LEU PRO TYR
SEQRES 13 B 315 GLY GLY GLU ALA TYR ALA ALA PHE LYS PRO ILE ALA ARG
SEQRES 14 B 315 ALA LEU ALA ALA ASN PRO GLU THR PRO ARG ARG PHE ALA
SEQRES 15 B 315 GLU ARG ALA ALA GLU PRO GLY ALA VAL GLU ARG LEU ILE
SEQRES 16 B 315 ALA SER THR GLY SER THR ILE ASP ALA GLU GLY LEU ALA
SEQRES 17 B 315 HIS TYR ARG LYS LEU TRP SER SER PRO ARG HIS VAL GLY
SEQRES 18 B 315 ALA ALA LEU THR MET MET ALA ASN TRP ASP LEU GLU PRO
SEQRES 19 B 315 LEU LEU GLU ARG LEU PRO GLU LEU LYS PRO LEU LEU VAL
SEQRES 20 B 315 LEU VAL ALA ALA GLU LYS ASP LYS ALA VAL PRO PRO GLU
SEQRES 21 B 315 VAL ALA GLU ARG VAL LYS GLU LEU LEU PRO ARG ALA GLU
SEQRES 22 B 315 ILE VAL ARG ILE PRO ALA LEU GLY HIS LEU ALA HIS GLU
SEQRES 23 B 315 GLU ASP PRO GLU LEU ILE ALA ARG LEU ILE GLU GLU HIS
SEQRES 24 B 315 VAL GLU ARG LEU GLU ALA GLN ARG LEU GLU HIS HIS HIS
SEQRES 25 B 315 HIS HIS HIS
FORMUL 3 HOH *45(H2 O)
HELIX 1 AA1 ASP A 17 GLN A 23 1 7
HELIX 2 AA2 HIS A 27 GLU A 29 5 3
HELIX 3 AA3 SER A 63 ARG A 68 5 6
HELIX 4 AA4 GLY A 69 SER A 75 1 7
HELIX 5 AA5 PRO A 95 LEU A 99 5 5
HELIX 6 AA6 SER A 100 LYS A 116 1 17
HELIX 7 AA7 ALA A 127 ASP A 138 1 12
HELIX 8 AA8 PHE A 164 ALA A 172 1 9
HELIX 9 AA9 PRO A 175 ALA A 186 1 12
HELIX 10 AB1 GLY A 189 THR A 198 1 10
HELIX 11 AB2 ASP A 203 SER A 215 1 13
HELIX 12 AB3 SER A 216 ASN A 229 1 14
HELIX 13 AB4 LEU A 232 ARG A 238 1 7
HELIX 14 AB5 LEU A 239 LEU A 242 5 4
HELIX 15 AB6 PRO A 259 LEU A 269 1 11
HELIX 16 AB7 LEU A 283 ASP A 288 1 6
HELIX 17 AB8 ASP A 288 GLN A 306 1 19
HELIX 18 AB9 VAL B 20 TRP B 25 5 6
HELIX 19 AC1 HIS B 27 GLU B 29 5 3
HELIX 20 AC2 SER B 63 ARG B 68 5 6
HELIX 21 AC3 GLY B 69 SER B 75 1 7
HELIX 22 AC4 PRO B 95 LEU B 99 5 5
HELIX 23 AC5 SER B 100 LEU B 115 1 16
HELIX 24 AC6 ALA B 127 ASP B 138 1 12
HELIX 25 AC7 GLY B 158 ALA B 163 1 6
HELIX 26 AC8 ALA B 170 ASN B 174 5 5
HELIX 27 AC9 GLU B 176 ALA B 186 1 11
HELIX 28 AD1 GLY B 189 THR B 198 1 10
HELIX 29 AD2 ASP B 203 SER B 215 1 13
HELIX 30 AD3 SER B 216 ASN B 229 1 14
HELIX 31 AD4 LEU B 232 ARG B 238 1 7
HELIX 32 AD5 LEU B 239 LEU B 242 5 4
HELIX 33 AD6 PRO B 259 LEU B 269 1 11
HELIX 34 AD7 LEU B 283 ASP B 288 1 6
HELIX 35 AD8 ASP B 288 GLN B 306 1 19
SHEET 1 AA1 8 SER A 31 ALA A 36 0
SHEET 2 AA1 8 ILE A 39 LEU A 46 -1 O VAL A 43 N ARG A 32
SHEET 3 AA1 8 HIS A 79 PRO A 83 -1 O ALA A 82 N GLN A 44
SHEET 4 AA1 8 ALA A 53 ILE A 57 1 N LEU A 54 O HIS A 79
SHEET 5 AA1 8 ILE A 121 HIS A 125 1 O ILE A 123 N ILE A 57
SHEET 6 AA1 8 ILE A 145 LEU A 149 1 O PHE A 147 N GLY A 124
SHEET 7 AA1 8 LEU A 245 ALA A 251 1 O VAL A 247 N ALA A 148
SHEET 8 AA1 8 GLU A 273 ILE A 277 1 O GLU A 273 N LEU A 248
SHEET 1 AA2 8 SER B 31 ALA B 36 0
SHEET 2 AA2 8 ILE B 39 LEU B 46 -1 O VAL B 43 N ARG B 32
SHEET 3 AA2 8 HIS B 79 PRO B 83 -1 O ALA B 82 N GLN B 44
SHEET 4 AA2 8 ALA B 53 ILE B 57 1 N LEU B 54 O VAL B 81
SHEET 5 AA2 8 ILE B 121 HIS B 125 1 O ILE B 123 N ILE B 57
SHEET 6 AA2 8 ILE B 145 LEU B 149 1 O PHE B 147 N GLY B 124
SHEET 7 AA2 8 LEU B 245 ALA B 251 1 O LEU B 245 N ILE B 146
SHEET 8 AA2 8 GLU B 273 ILE B 277 1 O GLU B 273 N LEU B 248
CRYST1 125.827 125.827 209.361 90.00 90.00 120.00 P 65 2 2 24
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 0.007947 0.004588 0.000000 0.00000
SCALE2 0.000000 0.009177 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004776 0.00000
MTRIX1 1 -0.998921 0.023861 0.039831 -7.18138 1
MTRIX2 1 0.008595 0.938047 -0.346401 -8.66337 1
MTRIX3 1 -0.045629 -0.345685 -0.937240 -43.79683 1
TER 2280 ARG A 307
TER 4560 ARG B 307
MASTER 325 0 0 35 16 0 0 9 4603 2 0 50
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