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HEADER HYDROLASE 12-OCT-21 7PZJ
TITLE STRUCTURE OF A BACTEROIDETAL POLYETHYLENE TEREPHTHALATE (PET) ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHRYSEOBACTERIUM JEONII;
SOURCE 3 ORGANISM_TAXID: 266749;
SOURCE 4 GENE: OA86_11720;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASES, METAGENOME, METAGENOMIC SCREENING, PET DEGRADATION,
KEYWDS 2 POLYETHYLENE TEREPHTHALATE (PET), BACTEROIDETES, FLAVOBACTERIACEAE,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ZANG,R.DIERKES,P.PEREZ-GARCIA,S.WEIGERT,S.STERNAGEL,S.J.HALLAM,
AUTHOR 2 V.APPLEGATE,J.SCHUMACHER,T.SCHOTT,J.PLEISS,A.ALMEIDA,B.HOECKER,
AUTHOR 3 S.H.SMITS,R.A.SCHMITZ,J.CHOW,W.R.STREIT
REVDAT 1 02-MAR-22 7PZJ 0
JRNL AUTH H.ZHANG,P.PEREZ-GARCIA,R.F.DIERKES,V.APPLEGATE,J.SCHUMACHER,
JRNL AUTH 2 C.M.CHIBANI,S.STERNAGEL,L.PREUSS,S.WEIGERT,C.SCHMEISSER,
JRNL AUTH 3 D.DANSO,J.PLEISS,A.ALMEIDA,B.HOCKER,S.J.HALLAM,R.A.SCHMITZ,
JRNL AUTH 4 S.H.J.SMITS,J.CHOW,W.R.STREIT
JRNL TITL THE BACTEROIDETES AEQUORIVITA SP. AND KAISTELLA JEONII
JRNL TITL 2 PRODUCE PROMISCUOUS ESTERASES WITH PET-HYDROLYZING ACTIVITY.
JRNL REF FRONT MICROBIOL V. 12 03896 2021
JRNL REFN ESSN 1664-302X
JRNL PMID 35069509
JRNL DOI 10.3389/FMICB.2021.803896
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 15441
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.640
REMARK 3 FREE R VALUE TEST SET COUNT : 716
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 49.0800 - 3.5900 1.00 3132 134 0.1574 0.2050
REMARK 3 2 3.5900 - 2.8500 1.00 2935 153 0.1692 0.2126
REMARK 3 3 2.8500 - 2.4900 1.00 2928 122 0.1624 0.2243
REMARK 3 4 2.4900 - 2.2600 1.00 2862 161 0.1554 0.2112
REMARK 3 5 2.2600 - 2.1000 1.00 2868 146 0.1608 0.2290
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.15
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 7PZJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1292118697.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-AUG-21
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 : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15447
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 38.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 17.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.9500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
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 : 5.380
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: OWN MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM AETATE PH 4.6 AND 25%
REMARK 280 (W/V) PEG 4000, VAPOR DIFFUSION, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 20.90150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.87750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.87750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.35225
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.87750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.87750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 10.45075
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.87750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.87750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 31.35225
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.87750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.87750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 10.45075
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 20.90150
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 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 662 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 -21
REMARK 465 ARG A -20
REMARK 465 LYS A -19
REMARK 465 LEU A -18
REMARK 465 TYR A -17
REMARK 465 LEU A -16
REMARK 465 PHE A -15
REMARK 465 LEU A -14
REMARK 465 PHE A -13
REMARK 465 LEU A -12
REMARK 465 THR A -11
REMARK 465 LEU A -10
REMARK 465 ILE A -9
REMARK 465 SER A -8
REMARK 465 PRO A -7
REMARK 465 ILE A -6
REMARK 465 SER A -5
REMARK 465 ILE A -4
REMARK 465 SER A -3
REMARK 465 ILE A -2
REMARK 465 PHE A -1
REMARK 465 HIS A 0
REMARK 465 ALA A 1
REMARK 465 GLN A 2
REMARK 465 CYS A 3
REMARK 465 THR A 4
REMARK 465 GLY A 5
REMARK 465 TYR A 279
REMARK 465 PRO A 280
REMARK 465 ASN A 281
REMARK 465 PRO A 282
REMARK 465 THR A 283
REMARK 465 LYS A 284
REMARK 465 ASP A 285
REMARK 465 PHE A 286
REMARK 465 VAL A 287
REMARK 465 GLN A 288
REMARK 465 VAL A 289
REMARK 465 ASN A 290
REMARK 465 VAL A 291
REMARK 465 ARG A 292
REMARK 465 GLU A 293
REMARK 465 MET A 294
REMARK 465 ALA A 295
REMARK 465 SER A 296
REMARK 465 TYR A 297
REMARK 465 GLN A 298
REMARK 465 LEU A 299
REMARK 465 SER A 300
REMARK 465 SER A 301
REMARK 465 SER A 302
REMARK 465 THR A 303
REMARK 465 GLY A 304
REMARK 465 GLN A 305
REMARK 465 ILE A 306
REMARK 465 VAL A 307
REMARK 465 LEU A 308
REMARK 465 LYS A 309
REMARK 465 GLY A 310
REMARK 465 ILE A 311
REMARK 465 VAL A 312
REMARK 465 THR A 313
REMARK 465 SER A 314
REMARK 465 SER A 315
REMARK 465 LYS A 316
REMARK 465 ASN A 317
REMARK 465 GLN A 318
REMARK 465 ILE A 319
REMARK 465 ASP A 320
REMARK 465 LEU A 321
REMARK 465 SER A 322
REMARK 465 LYS A 323
REMARK 465 LEU A 324
REMARK 465 PRO A 325
REMARK 465 ALA A 326
REMARK 465 GLY A 327
REMARK 465 VAL A 328
REMARK 465 TYR A 329
REMARK 465 TYR A 330
REMARK 465 LEU A 331
REMARK 465 GLN A 332
REMARK 465 ILE A 333
REMARK 465 ASN A 334
REMARK 465 GLY A 335
REMARK 465 GLU A 336
REMARK 465 THR A 337
REMARK 465 ILE A 338
REMARK 465 LYS A 339
REMARK 465 VAL A 340
REMARK 465 ILE A 341
REMARK 465 LYS A 342
REMARK 465 LYS A 343
REMARK 465 GLN A 344
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 HE21 GLN A 262 OD1 ASP A 271 1.55
REMARK 500 O HOH A 647 O HOH A 675 1.94
REMARK 500 O HOH A 603 O HOH A 645 2.08
REMARK 500 O PRO A 56 NH1 ARG A 94 2.09
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 CYS A 263 CB CYS A 263 SG -0.238
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 PRO A 14 C - N - CD ANGL. DEV. = -25.6 DEGREES
REMARK 500 CYS A 263 CA - CB - SG ANGL. DEV. = 9.0 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 PRO A 14 120.38 26.63
REMARK 500 PRO A 47 -176.88 -58.42
REMARK 500 THR A 59 -21.39 83.80
REMARK 500 LEU A 87 -61.48 -126.33
REMARK 500 THR A 113 -10.04 80.41
REMARK 500 SER A 131 -122.20 58.37
REMARK 500 LEU A 157 119.13 -163.88
REMARK 500 SER A 159 59.67 -110.91
REMARK 500 HIS A 184 -89.22 -130.75
REMARK 500 SER A 260 72.94 -158.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 13 PRO A 14 -110.73
REMARK 500 PRO A 47 PRO A 48 -50.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PRO A 47 -13.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 403 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 24 OE2
REMARK 620 2 ARG A 29 O 94.6
REMARK 620 3 TYR A 34 OH 115.6 88.8
REMARK 620 4 SER A 37 OG 109.0 133.2 114.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 401 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 30 OD1
REMARK 620 2 GLY A 31 O 86.7
REMARK 620 3 TYR A 34 O 137.0 72.4
REMARK 620 4 HOH A 523 O 61.2 68.0 76.1
REMARK 620 5 HOH A 528 O 63.1 126.9 100.1 59.4
REMARK 620 6 HOH A 656 O 156.0 101.4 66.8 142.8 124.2
REMARK 620 7 HOH A 675 O 79.9 89.1 134.9 134.9 123.1 77.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 402 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 194 O
REMARK 620 2 THR A 196 O 92.0
REMARK 620 3 SER A 260 O 147.5 76.7
REMARK 620 4 SER A 260 OG 90.6 116.7 68.6
REMARK 620 5 HOH A 598 O 121.2 96.6 90.6 133.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 404 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 259 OE1
REMARK 620 2 TYR A 261 OH 95.3
REMARK 620 3 HOH A 573 O 115.8 131.5
REMARK 620 4 HOH A 677 O 117.9 102.3 95.0
REMARK 620 N 1 2 3
DBREF1 7PZJ A -21 344 UNP A0A0C1F4U8_9FLAO
DBREF2 7PZJ A A0A0C1F4U8 1 366
SEQRES 1 A 366 MET ARG LYS LEU TYR LEU PHE LEU PHE LEU THR LEU ILE
SEQRES 2 A 366 SER PRO ILE SER ILE SER ILE PHE HIS ALA GLN CYS THR
SEQRES 3 A 366 GLY ALA THR VAL GLU SER LEU THR ASN PRO GLY PRO TYR
SEQRES 4 A 366 THR VAL ALA THR LEU SER GLU ALA ASP GLY VAL ARG ASN
SEQRES 5 A 366 GLY PRO LYS TYR ALA GLY SER THR ILE TYR TYR PRO THR
SEQRES 6 A 366 ASN ALA THR PRO PRO TYR ALA SER ILE ALA ILE VAL PRO
SEQRES 7 A 366 GLY PHE THR ALA ALA PRO SER SER VAL GLN GLU TRP GLY
SEQRES 8 A 366 PRO PHE TYR ALA SER HIS GLY ILE VAL ALA ILE ILE ILE
SEQRES 9 A 366 GLY THR ASN SER LEU TYR ASP GLN PRO GLU ALA ARG ALA
SEQRES 10 A 366 LEU ALA LEU LEU ASP ALA LEU GLU THR ILE LYS GLN GLU
SEQRES 11 A 366 ASN GLY ARG ALA THR SER PRO LEU ILE GLY LYS LEU ASP
SEQRES 12 A 366 VAL THR LYS LEU ALA VAL SER GLY TRP SER MET GLY GLY
SEQRES 13 A 366 GLY GLY ALA GLN ARG ALA ALA VAL LEU ASP ASN THR ILE
SEQRES 14 A 366 SER ALA VAL VAL ALA LEU CYS PRO TYR LEU THR SER PRO
SEQRES 15 A 366 GLN LEU ASN HIS THR VAL PRO VAL LEU ILE PHE SER GLY
SEQRES 16 A 366 GLN SER ASP PRO THR ALA PRO PRO SER GLN HIS ALA ASN
SEQRES 17 A 366 VAL HIS TYR ASN THR THR PRO GLY THR THR ASN LYS LEU
SEQRES 18 A 366 LEU PHE GLU VAL LYS ASN GLY ASN HIS SER VAL ALA ASN
SEQRES 19 A 366 SER PRO THR GLY GLY GLY GLY ALA VAL GLY LYS LEU ALA
SEQRES 20 A 366 LEU SER TRP LEU LYS ILE TYR LEU GLU LYS ASN ASP CYS
SEQRES 21 A 366 TYR CYS SER VAL LEU ALA THR ALA ILE VAL ASN SER THR
SEQRES 22 A 366 THR VAL SER SER LYS ILE SER GLN SER TYR GLN CYS ASN
SEQRES 23 A 366 ASN ALA LEU GLY VAL VAL ASP SER LYS THR ARG PHE ASN
SEQRES 24 A 366 LEU TYR PRO ASN PRO THR LYS ASP PHE VAL GLN VAL ASN
SEQRES 25 A 366 VAL ARG GLU MET ALA SER TYR GLN LEU SER SER SER THR
SEQRES 26 A 366 GLY GLN ILE VAL LEU LYS GLY ILE VAL THR SER SER LYS
SEQRES 27 A 366 ASN GLN ILE ASP LEU SER LYS LEU PRO ALA GLY VAL TYR
SEQRES 28 A 366 TYR LEU GLN ILE ASN GLY GLU THR ILE LYS VAL ILE LYS
SEQRES 29 A 366 LYS GLN
HET K A 401 1
HET K A 402 1
HET K A 403 1
HET K A 404 1
HETNAM K POTASSIUM ION
FORMUL 2 K 4(K 1+)
FORMUL 6 HOH *196(H2 O)
HELIX 1 AA1 THR A 7 THR A 12 5 6
HELIX 2 AA2 ALA A 25 GLY A 27 5 3
HELIX 3 AA3 ALA A 61 GLN A 66 5 6
HELIX 4 AA4 GLU A 67 HIS A 75 1 9
HELIX 5 AA5 GLN A 90 ASN A 109 1 20
HELIX 6 AA6 SER A 131 ASP A 144 1 14
HELIX 7 AA7 HIS A 184 THR A 192 1 9
HELIX 8 AA8 THR A 215 GLY A 218 5 4
HELIX 9 AA9 GLY A 219 LEU A 233 1 15
HELIX 10 AB1 CYS A 238 THR A 251 1 14
SHEET 1 AA110 VAL A 19 SER A 23 0
SHEET 2 AA110 SER A 37 PRO A 42 -1 O ILE A 39 N LEU A 22
SHEET 3 AA110 VAL A 78 ILE A 82 -1 O ALA A 79 N TYR A 40
SHEET 4 AA110 TYR A 49 VAL A 55 1 N ILE A 54 O ILE A 80
SHEET 5 AA110 LEU A 120 TRP A 130 1 O ASP A 121 N TYR A 49
SHEET 6 AA110 ALA A 149 LEU A 153 1 O LEU A 153 N GLY A 129
SHEET 7 AA110 VAL A 168 GLY A 173 1 O LEU A 169 N ALA A 152
SHEET 8 AA110 LYS A 198 VAL A 203 1 O LEU A 199 N ILE A 170
SHEET 9 AA110 SER A 254 ASN A 264 -1 O LYS A 256 N GLU A 202
SHEET 10 AA110 VAL A 269 SER A 272 -1 O VAL A 270 N CYS A 263
SHEET 1 AA210 VAL A 19 SER A 23 0
SHEET 2 AA210 SER A 37 PRO A 42 -1 O ILE A 39 N LEU A 22
SHEET 3 AA210 VAL A 78 ILE A 82 -1 O ALA A 79 N TYR A 40
SHEET 4 AA210 TYR A 49 VAL A 55 1 N ILE A 54 O ILE A 80
SHEET 5 AA210 LEU A 120 TRP A 130 1 O ASP A 121 N TYR A 49
SHEET 6 AA210 ALA A 149 LEU A 153 1 O LEU A 153 N GLY A 129
SHEET 7 AA210 VAL A 168 GLY A 173 1 O LEU A 169 N ALA A 152
SHEET 8 AA210 LYS A 198 VAL A 203 1 O LEU A 199 N ILE A 170
SHEET 9 AA210 SER A 254 ASN A 264 -1 O LYS A 256 N GLU A 202
SHEET 10 AA210 ARG A 275 ASN A 277 -1 O PHE A 276 N ILE A 257
SSBOND 1 CYS A 240 CYS A 263 1555 1555 2.13
LINK OE2 GLU A 24 K K A 403 1555 1555 2.56
LINK O ARG A 29 K K A 403 1555 1555 2.66
LINK OD1 ASN A 30 K K A 401 1555 1555 2.57
LINK O GLY A 31 K K A 401 1555 1555 2.82
LINK O TYR A 34 K K A 401 1555 1555 2.60
LINK OH TYR A 34 K K A 403 1555 1555 2.75
LINK OG SER A 37 K K A 403 1555 1555 2.73
LINK O GLY A 194 K K A 402 1555 1555 2.52
LINK O THR A 196 K K A 402 1555 1555 2.75
LINK OE1 GLN A 259 K K A 404 1555 1555 2.63
LINK O SER A 260 K K A 402 1555 1555 2.72
LINK OG SER A 260 K K A 402 1555 1555 2.67
LINK OH TYR A 261 K K A 404 1555 1555 2.86
LINK K K A 401 O HOH A 523 1555 1555 2.48
LINK K K A 401 O HOH A 528 1555 1555 3.49
LINK K K A 401 O HOH A 656 1555 1555 3.08
LINK K K A 401 O HOH A 675 1555 1555 3.31
LINK K K A 402 O HOH A 598 1555 1555 2.85
LINK K K A 404 O HOH A 573 1555 1555 2.68
LINK K K A 404 O HOH A 677 1555 1555 2.56
CRYST1 109.755 109.755 41.803 90.00 90.00 90.00 P 43 21 2 8
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 0.009111 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009111 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023922 0.00000
TER 3989 LEU A 278
MASTER 470 0 4 10 20 0 0 6 2206 1 28 29
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