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HEADER HYDROLASE 09-JAN-25 9HYD
TITLE PETASESM14 FROM MARINE-SPONGE STREPTOMYCES SP.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.74;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. SM14;
SOURCE 3 ORGANISM_TAXID: 1736045;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PETASE, POLYETHYLENE TEREPHTHALATE, SALT TOLERANCE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BHATTACHARYA,R.CASTAGNA,E.PARISINI
REVDAT 1 19-NOV-25 9HYD 0
JRNL AUTH A.CARLETTI,S.BHATTACHARYA,S.PEDRONI,M.BERTO,R.BONETTINI,
JRNL AUTH 2 R.CASTAGNA,E.PARISINI,G.DI ROCCO
JRNL TITL FUNCTIONAL AND STRUCTURAL CHARACTERIZATION OF PETASE SM14
JRNL TITL 2 FROM MARINE-SPONGE STREPTOMYCES SP. ACTIVE ON POLYETHYLENE
JRNL TITL 3 TEREPHTHALATE.
JRNL REF ACS SUSTAIN CHEM ENG V. 13 7460 2025
JRNL REFN ESSN 2168-0485
JRNL PMID 40443410
JRNL DOI 10.1021/ACSSUSCHEMENG.5C00737
REMARK 2
REMARK 2 RESOLUTION. 1.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0352
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) : 1.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 83.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 45061
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NONE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.058
REMARK 3 FREE R VALUE TEST SET COUNT : 2279
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) : 1.43
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3152
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3550
REMARK 3 BIN FREE R VALUE SET COUNT : 160
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1994
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 293
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16700
REMARK 3 B22 (A**2) : 0.16700
REMARK 3 B33 (A**2) : -0.54300
REMARK 3 B12 (A**2) : 0.08400
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): 0.065
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.069
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.998
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.986
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2097 ; 0.009 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 1832 ; 0.004 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2851 ; 1.623 ; 1.652
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4275 ; 0.575 ; 1.559
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 268 ; 6.789 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 23 ;10.196 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 313 ;13.218 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 307 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2493 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 439 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 400 ; 0.232 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 66 ; 0.221 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1031 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 239 ; 0.211 ; 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): 1054 ; 3.051 ; 2.341
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1053 ; 3.043 ; 2.340
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1322 ; 3.296 ; 3.515
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1323 ; 3.295 ; 3.516
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1043 ; 5.697 ; 2.652
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1044 ; 5.695 ; 2.653
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1527 ; 5.827 ; 3.862
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1528 ; 5.825 ; 3.863
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): 3929 ; 5.932 ; 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 9HYD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JAN-25.
REMARK 100 THE DEPOSITION ID IS D_1292144466.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JAN-24
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) : 0.7133
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45062
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.425
REMARK 200 RESOLUTION RANGE LOW (A) : 83.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 21.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
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: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M MES
REMARK 280 MONOHYDRATE PH 6.5, 30% W/V POLYETHYLENE GLYCOL MONOMETHYL ETHER
REMARK 280 5,000, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 14.93833
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 29.87667
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 22.40750
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 37.34583
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 7.46917
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: 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 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 21
REMARK 465 TRP A 22
REMARK 465 GLU A 23
REMARK 465 LEU A 24
REMARK 465 GLN A 25
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 GLY A 46 HG SER A 104 1.10
REMARK 500 HG1 THR A 114 H ASP A 115 1.25
REMARK 500 O HOH A 476 O HOH A 650 1.87
REMARK 500 O HOH A 510 O HOH A 628 1.88
REMARK 500 O HOH A 473 O HOH A 584 1.93
REMARK 500 O HOH A 607 O HOH A 688 2.05
REMARK 500 O HOH A 453 O HOH A 459 2.14
REMARK 500 O HOH A 645 O HOH A 676 2.15
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 ARG A 271 CZ ARG A 271 NH2 0.101
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 271 NE - CZ - NH1 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 ALA A 90 -19.53 89.39
REMARK 500 SER A 156 -127.42 69.72
REMARK 500 THR A 179 60.47 28.03
REMARK 500 HIS A 210 -86.65 -119.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 78 0.11 SIDE CHAIN
REMARK 500 ARG A 173 0.14 SIDE CHAIN
REMARK 500 ARG A 208 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9HYD A 26 284 UNP A0A679PDB4_9ACTN
DBREF2 9HYD A A0A679PDB4 26 284
SEQADV 9HYD GLY A 21 UNP A0A679PDB EXPRESSION TAG
SEQADV 9HYD TRP A 22 UNP A0A679PDB EXPRESSION TAG
SEQADV 9HYD GLU A 23 UNP A0A679PDB EXPRESSION TAG
SEQADV 9HYD LEU A 24 UNP A0A679PDB EXPRESSION TAG
SEQADV 9HYD GLN A 25 UNP A0A679PDB EXPRESSION TAG
SEQRES 1 A 264 GLY TRP GLU LEU GLN ALA GLN ASN PRO HIS GLU ARG GLY
SEQRES 2 A 264 PRO ASP PRO SER ASN SER TYR ILE GLU GLN ALA ARG GLY
SEQRES 3 A 264 SER TYR SER VAL SER GLN ARG SER ILE SER ARG LEU GLY
SEQRES 4 A 264 SER ASP GLY PHE ARG ASP GLY THR MET TYR TYR PRO THR
SEQRES 5 A 264 SER THR ALA ASP GLY ARG PHE GLY VAL VAL ALA ILE SER
SEQRES 6 A 264 PRO GLY TYR THR ALA SER GLU SER THR ILE ALA TRP LEU
SEQRES 7 A 264 GLY PRO ARG LEU ALA SER PHE GLY PHE VAL VAL VAL THR
SEQRES 8 A 264 ILE ASN THR ASP SER ARG TYR ASP GLN PRO ARG GLN ARG
SEQRES 9 A 264 ALA THR GLN LEU HIS ALA ALA LEU ASP HIS ALA ILE GLY
SEQRES 10 A 264 ASP SER VAL VAL GLY PRO ARG ILE ASP THR SER ARG GLN
SEQRES 11 A 264 ALA VAL MET GLY HIS SER MET GLY GLY GLY GLY ALA LEU
SEQRES 12 A 264 GLN ALA ALA GLU GLU ARG ASP GLU ILE ARG ALA ALA VAL
SEQRES 13 A 264 PRO LEU THR PRO TRP ASN LEU LYS LYS GLY TRP SER GLY
SEQRES 14 A 264 VAL ASP ALA ALA THR LEU VAL ILE GLY ALA GLU ASN ASP
SEQRES 15 A 264 ALA ILE ALA PRO VAL ARG SER HIS SER ILE PRO PHE TYR
SEQRES 16 A 264 GLU SER LEU THR ASN ALA GLU ARG ARG ALA TYR LEU GLU
SEQRES 17 A 264 LEU ARG ARG GLU GLY HIS PHE ALA PRO ASN SER SER ASN
SEQRES 18 A 264 THR LEU ILE ALA LYS TYR SER VAL SER TRP LEU LYS ARG
SEQRES 19 A 264 TYR VAL ASP ASN ASP LEU ARG TYR ASP GLN PHE ILE ASP
SEQRES 20 A 264 PRO GLY PRO ARG THR GLY ILE THR THR GLY VAL SER ASP
SEQRES 21 A 264 TYR ARG LEU GLY
HET GOL A 301 14
HET GOL A 302 14
HET GOL A 303 14
HET GOL A 304 14
HET GOL A 305 14
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 5(C3 H8 O3)
FORMUL 7 HOH *293(H2 O)
HELIX 1 AA1 SER A 37 GLU A 42 1 6
HELIX 2 AA2 SER A 91 ALA A 96 5 6
HELIX 3 AA3 TRP A 97 SER A 104 1 8
HELIX 4 AA4 ASP A 115 ASP A 119 5 5
HELIX 5 AA5 GLN A 120 GLY A 137 1 18
HELIX 6 AA6 VAL A 141 PRO A 143 5 3
HELIX 7 AA7 SER A 156 ARG A 169 1 14
HELIX 8 AA8 HIS A 210 LEU A 218 1 9
HELIX 9 AA9 PHE A 235 SER A 239 5 5
HELIX 10 AB1 ASN A 241 ASP A 257 1 17
HELIX 11 AB2 ASP A 259 ARG A 261 5 3
HELIX 12 AB3 TYR A 262 ASP A 267 1 6
SHEET 1 AA1 9 VAL A 50 SER A 56 0
SHEET 2 AA1 9 ASP A 65 PRO A 71 -1 O TYR A 70 N SER A 51
SHEET 3 AA1 9 VAL A 108 ASN A 113 -1 O VAL A 109 N TYR A 69
SHEET 4 AA1 9 PHE A 79 SER A 85 1 N VAL A 82 O VAL A 108
SHEET 5 AA1 9 ILE A 145 HIS A 155 1 O ASP A 146 N PHE A 79
SHEET 6 AA1 9 ILE A 172 LEU A 178 1 O LEU A 178 N GLY A 154
SHEET 7 AA1 9 ALA A 193 ALA A 199 1 O ILE A 197 N PRO A 177
SHEET 8 AA1 9 ARG A 224 LEU A 229 1 O LEU A 229 N GLY A 198
SHEET 9 AA1 9 VAL A 278 GLY A 284 -1 O GLY A 284 N ARG A 224
CISPEP 1 ASP A 267 PRO A 268 0 12.59
CRYST1 96.983 96.983 44.815 90.00 90.00 120.00 P 61 6
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 0.010311 0.005953 0.000000 0.00000
SCALE2 0.000000 0.011906 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022314 0.00000
TER 3973 GLY A 284
MASTER 349 0 5 12 9 0 0 6 2317 1 70 21
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