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HEADER HYDROLASE 31-AUG-23 8QEF
TITLE A CARBOHYDRATE ESTERASE FAMILY 15 (CE15) GLUCURONOYL ESTERASE FROM
TITLE 2 PHOCAEICOLA ATCC 8482 BOUND TO NOVEL LIGAND.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHOCAEICOLA VULGATUS ATCC 8482;
SOURCE 3 ORGANISM_TAXID: 435590;
SOURCE 4 GENE: BVU_0175;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET28-A
KEYWDS ESTERASE, CE15, GLUCURONOYL ESTERASE, BACTEROIDOTA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BANERJEE,J.N.POULSEN,S.MAZURKEWICH,A.SEVESO,J.LARSBRINK,L.LO LEGGIO
REVDAT 1 13-DEC-23 8QEF 0
JRNL AUTH S.BANERJEE,J.N.POULSEN,S.MAZURKEWICH,A.SEVESO,J.LARSBRINK,
JRNL AUTH 2 L.LO LEGGIO
JRNL TITL A CARBOHYDRATE ESTERASE FAMILY 15 (CE15) GLUCURONOYL
JRNL TITL 2 ESTERASE FROM PHOCAEICOLA ATCC 8482 BOUND TO NOVEL LIGAND.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
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) : 2.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 85.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 70.6
REMARK 3 NUMBER OF REFLECTIONS : 26881
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1367
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) : 2.16
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.22
REMARK 3 REFLECTION IN BIN (WORKING SET) : 131
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 4.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 2
REMARK 3 BIN FREE R VALUE : 0.0610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6226
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 95
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : -0.14000
REMARK 3 B33 (A**2) : 0.18000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.20000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.993
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.303
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.218
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.007
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6503 ; 0.008 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 5747 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8840 ; 1.483 ; 1.650
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13401 ; 1.246 ; 1.581
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 794 ; 7.657 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 353 ;33.735 ;22.918
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1028 ;17.195 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;19.777 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 795 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7364 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1412 ; 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): 3140 ; 2.333 ; 3.372
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3139 ; 2.333 ; 3.372
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3928 ; 3.615 ; 5.052
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3929 ; 3.615 ; 5.052
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3363 ; 2.741 ; 3.660
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3364 ; 2.741 ; 3.660
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4907 ; 4.417 ; 5.358
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7448 ; 6.210 ;38.763
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7445 ; 6.210 ;38.770
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 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : NULL
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 5811 ; 0.46 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 5811 ; 7.40 ; 2.00
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 8QEF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1292133094.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-22
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 : MAX IV
REMARK 200 BEAMLINE : BIOMAX
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28249
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.160
REMARK 200 RESOLUTION RANGE LOW (A) : 85.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
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 (%): 35.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.0, 20 MM NACL, AND 20
REMARK 280 -24% (W/V) PEG 6000, SOAKED IN 0.25 M NEUTRALISED GALACTURONIC
REMARK 280 ACID., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 29.58150
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: 3140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 11.0 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 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 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 SER A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 SER A 12
REMARK 465 SER A 13
REMARK 465 GLU A 14
REMARK 465 ASN A 15
REMARK 465 LEU A 16
REMARK 465 TYR A 17
REMARK 465 PHE A 18
REMARK 465 GLN A 19
REMARK 465 GLY A 20
REMARK 465 HIS A 21
REMARK 465 SER A 22
REMARK 465 LYS A 23
REMARK 465 SER A 24
REMARK 465 PRO A 25
REMARK 465 PRO A 161
REMARK 465 GLU A 162
REMARK 465 ILE A 163
REMARK 465 THR A 164
REMARK 465 ASP A 165
REMARK 465 GLU A 166
REMARK 465 LYS A 167
REMARK 465 MET A 168
REMARK 465 LYS A 169
REMARK 465 LYS A 170
REMARK 465 ARG A 171
REMARK 465 LYS A 427
REMARK 465 MET B 2
REMARK 465 GLY B 3
REMARK 465 SER B 4
REMARK 465 SER B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 SER B 12
REMARK 465 SER B 13
REMARK 465 GLU B 14
REMARK 465 ASN B 15
REMARK 465 LEU B 16
REMARK 465 TYR B 17
REMARK 465 PHE B 18
REMARK 465 GLN B 19
REMARK 465 GLY B 20
REMARK 465 HIS B 21
REMARK 465 SER B 22
REMARK 465 LYS B 23
REMARK 465 SER B 24
REMARK 465 PRO B 25
REMARK 465 ARG B 26
REMARK 465 PRO B 161
REMARK 465 GLU B 162
REMARK 465 ILE B 163
REMARK 465 THR B 164
REMARK 465 ASP B 165
REMARK 465 GLU B 166
REMARK 465 LYS B 167
REMARK 465 MET B 168
REMARK 465 LYS B 169
REMARK 465 LYS B 170
REMARK 465 ARG B 171
REMARK 465 ASN B 426
REMARK 465 LYS B 427
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 26 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 31 CG CD CE NZ
REMARK 470 ASN B 223 CG OD1 ND2
REMARK 470 LYS B 251 CG CD CE NZ
REMARK 470 LYS B 252 CG CD CE NZ
REMARK 470 LYS B 327 CE NZ
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 MET A 79 -63.32 -128.06
REMARK 500 ASP A 154 76.48 -63.56
REMARK 500 PRO A 156 0.22 -68.82
REMARK 500 ASP A 208 28.59 49.92
REMARK 500 SER A 264 -120.38 59.48
REMARK 500 SER A 264 -118.78 56.87
REMARK 500 ASP A 353 58.53 -99.67
REMARK 500 ASP A 357 82.58 66.03
REMARK 500 ASP A 357 82.58 66.06
REMARK 500 HIS A 406 100.25 -43.94
REMARK 500 LYS B 66 -60.40 -133.63
REMARK 500 MET B 79 -65.74 -120.78
REMARK 500 LYS B 89 171.43 -57.77
REMARK 500 ARG B 96 125.03 164.29
REMARK 500 ASP B 178 -47.94 -27.18
REMARK 500 LYS B 257 48.83 -147.06
REMARK 500 SER B 264 -124.23 67.02
REMARK 500 ARG B 325 38.35 -142.77
REMARK 500 LYS B 327 -37.60 -39.70
REMARK 500 ASP B 357 79.57 60.88
REMARK 500 TYR B 375 31.79 -98.20
REMARK 500 MET B 393 28.39 -150.92
REMARK 500 ALA B 407 169.27 174.08
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 GLY A 136 LYS A 137 149.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8QCL RELATED DB: PDB
REMARK 900 RELATED ID: 8Q6S RELATED DB: PDB
DBREF 8QEF A 30 427 UNP A6KWT9 A6KWT9_PHOV8 30 427
DBREF 8QEF B 30 427 UNP A6KWT9 A6KWT9_PHOV8 30 427
SEQADV 8QEF MET A 2 UNP A6KWT9 INITIATING METHIONINE
SEQADV 8QEF GLY A 3 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF SER A 4 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF SER A 5 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS A 6 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS A 7 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS A 8 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS A 9 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS A 10 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS A 11 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF SER A 12 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF SER A 13 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF GLU A 14 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF ASN A 15 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF LEU A 16 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF TYR A 17 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF PHE A 18 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF GLN A 19 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF GLY A 20 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS A 21 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF SER A 22 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF LYS A 23 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF SER A 24 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF PRO A 25 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF ARG A 26 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF LYS A 27 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF ASP A 28 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF TYR A 29 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF MET B 2 UNP A6KWT9 INITIATING METHIONINE
SEQADV 8QEF GLY B 3 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF SER B 4 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF SER B 5 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS B 6 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS B 7 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS B 8 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS B 9 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS B 10 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS B 11 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF SER B 12 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF SER B 13 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF GLU B 14 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF ASN B 15 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF LEU B 16 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF TYR B 17 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF PHE B 18 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF GLN B 19 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF GLY B 20 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF HIS B 21 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF SER B 22 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF LYS B 23 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF SER B 24 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF PRO B 25 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF ARG B 26 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF LYS B 27 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF ASP B 28 UNP A6KWT9 EXPRESSION TAG
SEQADV 8QEF TYR B 29 UNP A6KWT9 EXPRESSION TAG
SEQRES 1 A 426 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 A 426 ASN LEU TYR PHE GLN GLY HIS SER LYS SER PRO ARG LYS
SEQRES 3 A 426 ASP TYR ALA LYS LEU ALA ASN TYR ASP GLU SER LYS VAL
SEQRES 4 A 426 PRO GLN TYR THR LEU PRO SER VAL LEU MET CYS HIS ASP
SEQRES 5 A 426 GLY GLU MET VAL GLN THR LYS GLU GLN TRP GLU GLN LYS
SEQRES 6 A 426 ARG ARG PRO GLU ILE LEU ASN LEU PHE THR THR TYR MET
SEQRES 7 A 426 PHE GLY LYS ALA PRO VAL LEU LYS HIS LYS LEU PRO CYS
SEQRES 8 A 426 THR VAL SER ARG ILE ASN GLU LYS ALA LEU ASN GLY ARG
SEQRES 9 A 426 ALA THR ARG LYS GLU ILE THR ILE GLN LEU THR ASP ASP
SEQRES 10 A 426 PRO GLN GLY PRO HIS ILE ASP LEU GLN LEU TYR LEU PRO
SEQRES 11 A 426 ASN HIS VAL SER GLY LYS ILE PRO VAL PHE LEU GLY ILE
SEQRES 12 A 426 SER PHE MET PRO ASN TYR THR ILE TYR ASP ASP PRO ASP
SEQRES 13 A 426 LEU SER VAL PRO GLU ILE THR ASP GLU LYS MET LYS LYS
SEQRES 14 A 426 ARG SER PHE ARG GLY SER MET ASP LYS SER TRP GLN LEU
SEQRES 15 A 426 ASP LYS ILE LEU GLU HIS GLY TYR GLY LEU ALA THR PHE
SEQRES 16 A 426 CYS TYR ASN ASP VAL ASP PRO ASP PHE ASP ASP ASP PHE
SEQRES 17 A 426 GLN ASN GLY VAL HIS PRO TYR TYR TYR GLU LYS GLY GLN
SEQRES 18 A 426 ASN PHE PRO ASP PRO ASP GLN TRP GLY SER ILE ALA ALA
SEQRES 19 A 426 TRP ALA TRP GLY MET SER ARG ALA MET ASP TYR LEU GLU
SEQRES 20 A 426 THR ASP LYS LYS VAL ASP ALA LYS LYS VAL ALA VAL ILE
SEQRES 21 A 426 GLY HIS SER ARG LEU GLY LYS THR ALA VAL TRP ALA GLY
SEQRES 22 A 426 ALA SER ASP PRO ARG PHE ALA LEU VAL ILE SER GLY ASN
SEQRES 23 A 426 SER GLY CYS CYS GLY VAL ALA ILE SER ARG ARG CYS PHE
SEQRES 24 A 426 GLY GLU THR VAL GLU ALA MET ASN VAL ARG PHE PRO HIS
SEQRES 25 A 426 TRP PHE CYS GLY ASN TYR LYS GLN PHE ASN ASP ARG GLU
SEQRES 26 A 426 LYS TYR LEU PRO PHE ASP GLN HIS GLU LEU VAL ALA LEU
SEQRES 27 A 426 ILE ALA PRO ARG PRO ILE TYR ILE ALA SER ALA GLU GLU
SEQRES 28 A 426 ASP ASN TRP SER ASP GLN LYS GLY GLU PHE LEU GLY GLY
SEQRES 29 A 426 LYS GLY ALA GLU PRO VAL TYR ALA LEU TYR GLY LEU GLY
SEQRES 30 A 426 GLY ILE GLY CYS GLU GLU MET PRO PRO VAL ASP THR PRO
SEQRES 31 A 426 TYR MET ASN GLY PRO ILE ALA TYR HIS ASN ARG LYS GLY
SEQRES 32 A 426 PRO HIS ALA VAL LEU PRO TYR ASP TRP GLU GLN PHE LEU
SEQRES 33 A 426 ARG PHE ALA ASP LYS TYR PHE LYS ASN LYS
SEQRES 1 B 426 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 B 426 ASN LEU TYR PHE GLN GLY HIS SER LYS SER PRO ARG LYS
SEQRES 3 B 426 ASP TYR ALA LYS LEU ALA ASN TYR ASP GLU SER LYS VAL
SEQRES 4 B 426 PRO GLN TYR THR LEU PRO SER VAL LEU MET CYS HIS ASP
SEQRES 5 B 426 GLY GLU MET VAL GLN THR LYS GLU GLN TRP GLU GLN LYS
SEQRES 6 B 426 ARG ARG PRO GLU ILE LEU ASN LEU PHE THR THR TYR MET
SEQRES 7 B 426 PHE GLY LYS ALA PRO VAL LEU LYS HIS LYS LEU PRO CYS
SEQRES 8 B 426 THR VAL SER ARG ILE ASN GLU LYS ALA LEU ASN GLY ARG
SEQRES 9 B 426 ALA THR ARG LYS GLU ILE THR ILE GLN LEU THR ASP ASP
SEQRES 10 B 426 PRO GLN GLY PRO HIS ILE ASP LEU GLN LEU TYR LEU PRO
SEQRES 11 B 426 ASN HIS VAL SER GLY LYS ILE PRO VAL PHE LEU GLY ILE
SEQRES 12 B 426 SER PHE MET PRO ASN TYR THR ILE TYR ASP ASP PRO ASP
SEQRES 13 B 426 LEU SER VAL PRO GLU ILE THR ASP GLU LYS MET LYS LYS
SEQRES 14 B 426 ARG SER PHE ARG GLY SER MET ASP LYS SER TRP GLN LEU
SEQRES 15 B 426 ASP LYS ILE LEU GLU HIS GLY TYR GLY LEU ALA THR PHE
SEQRES 16 B 426 CYS TYR ASN ASP VAL ASP PRO ASP PHE ASP ASP ASP PHE
SEQRES 17 B 426 GLN ASN GLY VAL HIS PRO TYR TYR TYR GLU LYS GLY GLN
SEQRES 18 B 426 ASN PHE PRO ASP PRO ASP GLN TRP GLY SER ILE ALA ALA
SEQRES 19 B 426 TRP ALA TRP GLY MET SER ARG ALA MET ASP TYR LEU GLU
SEQRES 20 B 426 THR ASP LYS LYS VAL ASP ALA LYS LYS VAL ALA VAL ILE
SEQRES 21 B 426 GLY HIS SER ARG LEU GLY LYS THR ALA VAL TRP ALA GLY
SEQRES 22 B 426 ALA SER ASP PRO ARG PHE ALA LEU VAL ILE SER GLY ASN
SEQRES 23 B 426 SER GLY CYS CYS GLY VAL ALA ILE SER ARG ARG CYS PHE
SEQRES 24 B 426 GLY GLU THR VAL GLU ALA MET ASN VAL ARG PHE PRO HIS
SEQRES 25 B 426 TRP PHE CYS GLY ASN TYR LYS GLN PHE ASN ASP ARG GLU
SEQRES 26 B 426 LYS TYR LEU PRO PHE ASP GLN HIS GLU LEU VAL ALA LEU
SEQRES 27 B 426 ILE ALA PRO ARG PRO ILE TYR ILE ALA SER ALA GLU GLU
SEQRES 28 B 426 ASP ASN TRP SER ASP GLN LYS GLY GLU PHE LEU GLY GLY
SEQRES 29 B 426 LYS GLY ALA GLU PRO VAL TYR ALA LEU TYR GLY LEU GLY
SEQRES 30 B 426 GLY ILE GLY CYS GLU GLU MET PRO PRO VAL ASP THR PRO
SEQRES 31 B 426 TYR MET ASN GLY PRO ILE ALA TYR HIS ASN ARG LYS GLY
SEQRES 32 B 426 PRO HIS ALA VAL LEU PRO TYR ASP TRP GLU GLN PHE LEU
SEQRES 33 B 426 ARG PHE ALA ASP LYS TYR PHE LYS ASN LYS
HET EDO A 501 4
HET EDO A 502 4
HET EDO A 503 4
HET GTR B 501 13
HET EDO B 502 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GTR BETA-D-GALACTOPYRANURONIC ACID
HETSYN EDO ETHYLENE GLYCOL
HETSYN GTR BETA-D-GALACTURONIC ACID; D-GALACTURONIC ACID;
HETSYN 2 GTR GALACTURONIC ACID
FORMUL 3 EDO 4(C2 H6 O2)
FORMUL 6 GTR C6 H10 O7
FORMUL 8 HOH *95(H2 O)
HELIX 1 AA1 ASP A 28 ALA A 33 1 6
HELIX 2 AA2 ASP A 36 VAL A 40 5 5
HELIX 3 AA3 THR A 59 LYS A 66 1 8
HELIX 4 AA4 LYS A 66 MET A 79 1 14
HELIX 5 AA5 PRO A 148 ILE A 152 5 5
HELIX 6 AA6 MET A 177 TRP A 181 5 5
HELIX 7 AA7 GLN A 182 HIS A 189 1 8
HELIX 8 AA8 ASN A 199 VAL A 201 5 3
HELIX 9 AA9 VAL A 213 TYR A 218 1 6
HELIX 10 AB1 GLY A 231 GLU A 248 1 18
HELIX 11 AB2 SER A 264 ASP A 277 1 14
HELIX 12 AB3 ILE A 295 CYS A 299 5 5
HELIX 13 AB4 THR A 303 PHE A 311 1 9
HELIX 14 AB5 GLY A 317 ASN A 323 5 7
HELIX 15 AB6 ARG A 325 LEU A 329 5 5
HELIX 16 AB7 GLN A 333 LEU A 339 1 7
HELIX 17 AB8 ASP A 353 SER A 356 5 4
HELIX 18 AB9 ASP A 357 LEU A 374 1 18
HELIX 19 AC1 LEU A 409 LYS A 425 1 17
HELIX 20 AC2 TYR B 29 ALA B 33 5 5
HELIX 21 AC3 ASP B 36 VAL B 40 5 5
HELIX 22 AC4 THR B 59 LYS B 66 1 8
HELIX 23 AC5 LYS B 66 MET B 79 1 14
HELIX 24 AC6 PRO B 148 ILE B 152 5 5
HELIX 25 AC7 MET B 177 GLN B 182 1 6
HELIX 26 AC8 GLN B 182 HIS B 189 1 8
HELIX 27 AC9 ASN B 199 VAL B 201 5 3
HELIX 28 AD1 VAL B 213 TYR B 218 5 6
HELIX 29 AD2 GLY B 231 ASP B 250 1 20
HELIX 30 AD3 SER B 264 ASP B 277 1 14
HELIX 31 AD4 ILE B 295 CYS B 299 5 5
HELIX 32 AD5 THR B 303 PHE B 311 1 9
HELIX 33 AD6 GLY B 317 ASN B 323 5 7
HELIX 34 AD7 ARG B 325 LEU B 329 5 5
HELIX 35 AD8 ASP B 332 LEU B 339 1 8
HELIX 36 AD9 ASP B 353 SER B 356 5 4
HELIX 37 AE1 ASP B 357 GLY B 367 1 11
HELIX 38 AE2 ALA B 368 ALA B 373 1 6
HELIX 39 AE3 LEU B 374 GLY B 376 5 3
HELIX 40 AE4 LEU B 409 LYS B 425 1 17
SHEET 1 AA1 9 CYS A 92 ASN A 98 0
SHEET 2 AA1 9 ALA A 106 GLN A 114 -1 O ARG A 108 N ASN A 98
SHEET 3 AA1 9 HIS A 123 PRO A 131 -1 O LEU A 126 N ILE A 111
SHEET 4 AA1 9 GLY A 192 CYS A 197 -1 O THR A 195 N GLN A 127
SHEET 5 AA1 9 ILE A 138 SER A 145 1 N PHE A 141 O ALA A 194
SHEET 6 AA1 9 VAL A 253 HIS A 263 1 O ALA A 259 N LEU A 142
SHEET 7 AA1 9 LEU A 282 GLY A 286 1 O ILE A 284 N VAL A 260
SHEET 8 AA1 9 ILE A 345 ALA A 350 1 O ALA A 348 N SER A 285
SHEET 9 AA1 9 ILE A 397 ARG A 402 1 O HIS A 400 N SER A 349
SHEET 1 AA2 9 CYS B 92 ASN B 98 0
SHEET 2 AA2 9 ALA B 106 GLN B 114 -1 O THR B 112 N THR B 93
SHEET 3 AA2 9 HIS B 123 PRO B 131 -1 O LEU B 128 N LYS B 109
SHEET 4 AA2 9 GLY B 192 CYS B 197 -1 O THR B 195 N GLN B 127
SHEET 5 AA2 9 ILE B 138 SER B 145 1 N GLY B 143 O ALA B 194
SHEET 6 AA2 9 VAL B 253 HIS B 263 1 O ALA B 259 N LEU B 142
SHEET 7 AA2 9 LEU B 282 GLY B 286 1 O ILE B 284 N VAL B 260
SHEET 8 AA2 9 ILE B 345 ALA B 350 1 O TYR B 346 N SER B 285
SHEET 9 AA2 9 ILE B 397 ARG B 402 1 O HIS B 400 N SER B 349
CISPEP 1 ALA A 341 PRO A 342 0 2.34
CISPEP 2 ALA B 341 PRO B 342 0 3.94
CRYST1 74.215 59.163 87.163 90.00 101.44 90.00 P 1 21 1 4
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 0.013474 0.000000 0.002727 0.00000
SCALE2 0.000000 0.016902 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011705 0.00000
TER 3162 ASN A 426
TER 6280 LYS B 425
MASTER 389 0 5 40 18 0 0 6 6350 2 29 66
END |