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HEADER HYDROLASE 08-APR-19 6RB0
TITLE STRUCTURE OF ESTER-HYDROLASE EH1AB1 FROM THE METAGENOME OF LAKE ARREO
TITLE 2 COMPLEXED WITH A DERIVATIVE OF METHYL 4-NITROPHENYL HEXYLPHOSPHONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EH1AB1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-46 EK/LIC
KEYWDS ESTER HYDROLASE, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.CEA-RAMA,J.SANZ-APARICIO
REVDAT 1 25-DEC-19 6RB0 0
JRNL AUTH S.ALONSO,G.SANTIAGO,I.CEA-RAMA,L.FERNANDEZ-LOPEZ,C.COSCOLIN,
JRNL AUTH 2 J.MODREGGER,A.RESSMANN,M.MARTINEZ-MARTINEZ,H.MARRERO,
JRNL AUTH 3 R.BARGIELA,M.PITA,J.L.GONZALEZ-ALFONSO,M.BRIAND,D.ROJO,
JRNL AUTH 4 C.BARBAS,F.J.PLOU,P.N.GOLYSHIN,P.SHAHGALDIAN,
JRNL AUTH 5 J.SANZ-APARICIO,V.GUALLAR,M.FERRER
JRNL TITL GENETICALLY ENGINEERED PROTEINS WITH TWO ACTIVE SITES FOR
JRNL TITL 2 ENHANCED BIOCATALYSIS AND SYNERGISTIC CHEMO- AND
JRNL TITL 3 BIOCATALYSIS
JRNL REF NAT CATAL 2019
JRNL REFN ESSN 2520-1158
JRNL DOI 10.1038/S41929-019-0394-4
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 28255
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1460
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2077
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 110
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4770
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 162
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : -0.22000
REMARK 3 B33 (A**2) : -0.11000
REMARK 3 B12 (A**2) : 0.00000
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): 0.329
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.214
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.153
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.471
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4951 ; 0.006 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4534 ; 0.003 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6717 ; 1.492 ; 1.662
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10460 ; 1.372 ; 1.599
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 628 ; 6.723 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 272 ;30.254 ;20.515
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 714 ;13.963 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;20.471 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 632 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5688 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1122 ; 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): 2518 ; 1.658 ; 2.736
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2517 ; 1.658 ; 2.736
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3144 ; 2.729 ; 4.101
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3145 ; 2.728 ; 4.101
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2433 ; 2.313 ; 3.150
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2434 ; 2.312 ; 3.151
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3574 ; 3.870 ; 4.575
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5478 ; 6.020 ;33.135
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5464 ; 6.009 ;33.112
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 315 B 1 315 10356 0.08 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 6RB0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1292101703.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-18
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 : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97936
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL-CUT, CRYOCOOLED
REMARK 200 OPTICS : KB FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 1.11.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29764
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 43.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.14900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.64600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.6.04
REMARK 200 STARTING MODEL: 6I8F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG3350, 0.2M NAF, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 41.53850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.80550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.04500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.80550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.53850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.04500
REMARK 290 SMTRY3 4 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: 3080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 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 SER A 211 CB - CA - C ANGL. DEV. = 15.5 DEGREES
REMARK 500 SER B 211 CB - CA - C ANGL. DEV. = 17.7 DEGREES
REMARK 500 SER B 211 N - CA - CB ANGL. DEV. = -9.1 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 ASN A 95 -169.71 -170.87
REMARK 500 ASP A 118 79.46 -101.08
REMARK 500 PHE A 127 131.95 -34.99
REMARK 500 SER A 161 -113.31 47.29
REMARK 500 TYR A 189 62.96 30.72
REMARK 500 PHE A 209 -70.09 50.67
REMARK 500 TYR A 255 41.24 -105.01
REMARK 500 LEU A 291 49.37 -91.12
REMARK 500 ASN B 95 -170.18 -171.33
REMARK 500 PHE B 127 131.36 -33.60
REMARK 500 SER B 161 -112.84 47.92
REMARK 500 TYR B 189 62.17 31.97
REMARK 500 PHE B 209 -80.87 54.04
REMARK 500 TYR B 255 41.97 -105.33
REMARK 500 LEU B 291 48.57 -90.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MHH A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MHH A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MHH B 404 and SER B
REMARK 800 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MHH B 405 and SER B
REMARK 800 211
DBREF 6RB0 A 1 314 PDB 6RB0 6RB0 1 314
DBREF 6RB0 B 1 314 PDB 6RB0 6RB0 1 314
SEQRES 1 A 315 MET LEU LEU PRO GLU THR ARG ASN LEU LEU ASP LEU MET
SEQRES 2 A 315 ASP ALA ALA THR ARG GLY GLY ARG PRO GLY LEU ASP THR
SEQRES 3 A 315 LEU PRO HIS ALA VAL GLY ARG LYS ALA VAL ASP LYS MET
SEQRES 4 A 315 SER GLU ASP GLY GLU ALA ASP PRO PRO GLU VAL ALA GLU
SEQRES 5 A 315 VAL ALA ASN GLY GLY PHE ALA GLY PRO ALA SER GLU ILE
SEQRES 6 A 315 ARG PHE ARG ARG TYR ARG PRO LEU GLY GLU ALA ALA GLY
SEQRES 7 A 315 LEU LEU PRO THR LEU ILE TYR TYR HIS GLY GLY GLY PHE
SEQRES 8 A 315 VAL ILE GLY ASN ILE GLU THR HIS ASP SER THR CYS ARG
SEQRES 9 A 315 ARG LEU ALA ASN LYS SER ARG CYS GLN VAL ILE SER ILE
SEQRES 10 A 315 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA PRO
SEQRES 11 A 315 ILE ASP ASP GLY ILE ALA ALA PHE ARG HIS ILE ARG ASP
SEQRES 12 A 315 ASN ALA GLU SER PHE GLY ALA ASP ALA ALA ARG LEU ALA
SEQRES 13 A 315 VAL GLY GLY ASP SER ALA GLY GLY ALA MET ALA ALA VAL
SEQRES 14 A 315 VAL CYS GLN ALA CYS ARG ASP ALA GLY GLU THR GLY PRO
SEQRES 15 A 315 ALA PHE GLN MET LEU ILE TYR PRO ALA THR ASP SER SER
SEQRES 16 A 315 ARG GLU SER ALA SER ARG VAL ALA PHE ALA GLU GLY TYR
SEQRES 17 A 315 PHE LEU SER LYS ALA HIS MET ASP TRP PHE TRP GLU ALA
SEQRES 18 A 315 TYR VAL PRO GLU ASP THR ASP LEU THR ASP LEU ARG LEU
SEQRES 19 A 315 SER PRO LEU LEU ALA THR ASP PHE THR GLY LEU PRO PRO
SEQRES 20 A 315 ALA PHE VAL LEU THR ALA GLY TYR ASP PRO LEU ARG ASP
SEQRES 21 A 315 GLU GLY ARG ALA TYR ALA ASP ARG LEU ILE GLU ALA GLY
SEQRES 22 A 315 ILE LYS THR THR TYR VAL ASN TYR PRO GLY THR ILE HIS
SEQRES 23 A 315 GLY PHE PHE SER LEU THR ARG PHE LEU SER GLN GLY LEU
SEQRES 24 A 315 LYS ALA ASN ASP GLU ALA ALA ALA VAL MET GLY ALA HIS
SEQRES 25 A 315 PHE GLY THR
SEQRES 1 B 315 MET LEU LEU PRO GLU THR ARG ASN LEU LEU ASP LEU MET
SEQRES 2 B 315 ASP ALA ALA THR ARG GLY GLY ARG PRO GLY LEU ASP THR
SEQRES 3 B 315 LEU PRO HIS ALA VAL GLY ARG LYS ALA VAL ASP LYS MET
SEQRES 4 B 315 SER GLU ASP GLY GLU ALA ASP PRO PRO GLU VAL ALA GLU
SEQRES 5 B 315 VAL ALA ASN GLY GLY PHE ALA GLY PRO ALA SER GLU ILE
SEQRES 6 B 315 ARG PHE ARG ARG TYR ARG PRO LEU GLY GLU ALA ALA GLY
SEQRES 7 B 315 LEU LEU PRO THR LEU ILE TYR TYR HIS GLY GLY GLY PHE
SEQRES 8 B 315 VAL ILE GLY ASN ILE GLU THR HIS ASP SER THR CYS ARG
SEQRES 9 B 315 ARG LEU ALA ASN LYS SER ARG CYS GLN VAL ILE SER ILE
SEQRES 10 B 315 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA PRO
SEQRES 11 B 315 ILE ASP ASP GLY ILE ALA ALA PHE ARG HIS ILE ARG ASP
SEQRES 12 B 315 ASN ALA GLU SER PHE GLY ALA ASP ALA ALA ARG LEU ALA
SEQRES 13 B 315 VAL GLY GLY ASP SER ALA GLY GLY ALA MET ALA ALA VAL
SEQRES 14 B 315 VAL CYS GLN ALA CYS ARG ASP ALA GLY GLU THR GLY PRO
SEQRES 15 B 315 ALA PHE GLN MET LEU ILE TYR PRO ALA THR ASP SER SER
SEQRES 16 B 315 ARG GLU SER ALA SER ARG VAL ALA PHE ALA GLU GLY TYR
SEQRES 17 B 315 PHE LEU SER LYS ALA HIS MET ASP TRP PHE TRP GLU ALA
SEQRES 18 B 315 TYR VAL PRO GLU ASP THR ASP LEU THR ASP LEU ARG LEU
SEQRES 19 B 315 SER PRO LEU LEU ALA THR ASP PHE THR GLY LEU PRO PRO
SEQRES 20 B 315 ALA PHE VAL LEU THR ALA GLY TYR ASP PRO LEU ARG ASP
SEQRES 21 B 315 GLU GLY ARG ALA TYR ALA ASP ARG LEU ILE GLU ALA GLY
SEQRES 22 B 315 ILE LYS THR THR TYR VAL ASN TYR PRO GLY THR ILE HIS
SEQRES 23 B 315 GLY PHE PHE SER LEU THR ARG PHE LEU SER GLN GLY LEU
SEQRES 24 B 315 LYS ALA ASN ASP GLU ALA ALA ALA VAL MET GLY ALA HIS
SEQRES 25 B 315 PHE GLY THR
HET GOL A 401 6
HET GOL A 402 6
HET MHH A 403 10
HET MHH A 404 10
HET GOL B 401 6
HET GOL B 402 6
HET GOL B 403 6
HET MHH B 404 10
HET MHH B 405 10
HETNAM GOL GLYCEROL
HETNAM MHH METHYL HYDROGEN (R)-HEXYLPHOSPHONATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 5(C3 H8 O3)
FORMUL 5 MHH 4(C7 H17 O3 P)
FORMUL 12 HOH *162(H2 O)
HELIX 1 AA1 LEU A 3 GLY A 19 1 17
HELIX 2 AA2 GLY A 23 LEU A 27 5 5
HELIX 3 AA3 PRO A 28 GLU A 44 1 17
HELIX 4 AA4 ILE A 96 THR A 98 5 3
HELIX 5 AA5 HIS A 99 ARG A 111 1 13
HELIX 6 AA6 PRO A 128 ASN A 144 1 17
HELIX 7 AA7 ALA A 145 PHE A 148 5 4
HELIX 8 AA8 SER A 161 ALA A 177 1 17
HELIX 9 AA9 SER A 198 PHE A 204 1 7
HELIX 10 AB1 SER A 211 VAL A 223 1 13
HELIX 11 AB2 SER A 235 ALA A 239 5 5
HELIX 12 AB3 LEU A 258 ALA A 272 1 15
HELIX 13 AB4 LEU A 295 PHE A 313 1 19
HELIX 14 AB5 LEU B 3 ARG B 18 1 16
HELIX 15 AB6 GLY B 23 LEU B 27 5 5
HELIX 16 AB7 PRO B 28 GLU B 44 1 17
HELIX 17 AB8 ILE B 96 THR B 98 5 3
HELIX 18 AB9 HIS B 99 ARG B 111 1 13
HELIX 19 AC1 PRO B 128 ASN B 144 1 17
HELIX 20 AC2 ALA B 145 PHE B 148 5 4
HELIX 21 AC3 SER B 161 GLY B 178 1 18
HELIX 22 AC4 SER B 198 PHE B 204 1 7
HELIX 23 AC5 SER B 211 VAL B 223 1 13
HELIX 24 AC6 SER B 235 ALA B 239 5 5
HELIX 25 AC7 LEU B 258 ALA B 272 1 15
HELIX 26 AC8 LEU B 295 PHE B 313 1 19
SHEET 1 AA116 GLU A 52 ALA A 59 0
SHEET 2 AA116 GLU A 64 ARG A 71 -1 O ARG A 71 N GLU A 52
SHEET 3 AA116 GLN A 113 ASP A 118 -1 O SER A 116 N ARG A 68
SHEET 4 AA116 LEU A 80 TYR A 86 1 N LEU A 83 O GLN A 113
SHEET 5 AA116 ALA A 150 ASP A 160 1 O ALA A 156 N THR A 82
SHEET 6 AA116 PHE A 184 ILE A 188 1 O ILE A 188 N GLY A 159
SHEET 7 AA116 ALA A 248 ALA A 253 1 O PHE A 249 N LEU A 187
SHEET 8 AA116 THR A 276 TYR A 281 1 O THR A 277 N VAL A 250
SHEET 9 AA116 THR B 276 TYR B 281 -1 O TYR B 278 N TYR A 278
SHEET 10 AA116 ALA B 248 ALA B 253 1 N VAL B 250 O THR B 277
SHEET 11 AA116 PHE B 184 ILE B 188 1 N LEU B 187 O PHE B 249
SHEET 12 AA116 ALA B 150 ASP B 160 1 N GLY B 159 O ILE B 188
SHEET 13 AA116 LEU B 80 TYR B 86 1 N THR B 82 O ALA B 156
SHEET 14 AA116 GLN B 113 ASP B 118 1 O ILE B 115 N TYR B 85
SHEET 15 AA116 GLU B 64 ARG B 71 -1 N ARG B 68 O SER B 116
SHEET 16 AA116 GLU B 52 ALA B 59 -1 N GLU B 52 O ARG B 71
LINK OG SER A 161 P MHH A 403 1555 1555 1.63
LINK OG SER A 211 P MHH A 404 1555 1555 1.68
LINK OG SER B 161 P MHH B 404 1555 1555 1.64
LINK OG SER B 211 P MHH B 405 1555 1555 1.67
CISPEP 1 ALA A 122 PRO A 123 0 -2.09
CISPEP 2 PHE A 127 PRO A 128 0 4.30
CISPEP 3 ALA B 122 PRO B 123 0 -0.29
CISPEP 4 PHE B 127 PRO B 128 0 3.66
SITE 1 AC1 6 GLU A 49 VAL A 50 ARG A 104 HOH A 541
SITE 2 AC1 6 GLY B 56 ARG B 66
SITE 1 AC2 7 ASN A 55 GLY A 56 ARG A 66 HOH A 562
SITE 2 AC2 7 GLU B 49 VAL B 50 ARG B 104
SITE 1 AC3 6 GLY A 88 GLY A 89 GLY A 90 SER A 161
SITE 2 AC3 6 ALA A 162 HIS A 286
SITE 1 AC4 7 LEU A 10 ASP A 14 GLU A 206 GLY A 207
SITE 2 AC4 7 TYR A 208 PHE A 209 SER A 211
SITE 1 AC5 6 ARG A 263 ASP A 267 TYR A 278 ARG B 263
SITE 2 AC5 6 ASP B 267 ILE B 270
SITE 1 AC6 5 ALA B 173 ASP B 176 LEU B 232 ARG B 233
SITE 2 AC6 5 HOH B 509
SITE 1 AC7 8 ARG A 69 ARG A 71 GLY A 78 SER A 147
SITE 2 AC7 8 ARG B 69 ARG B 71 GLU B 146 SER B 147
SITE 1 AC8 13 GLY B 88 GLY B 89 GLY B 90 ASP B 160
SITE 2 AC8 13 ALA B 162 GLY B 163 GLY B 164 ALA B 165
SITE 3 AC8 13 ILE B 188 TYR B 189 PRO B 190 ALA B 191
SITE 4 AC8 13 HIS B 286
SITE 1 AC9 12 LEU B 10 ASP B 14 ALA B 205 GLU B 206
SITE 2 AC9 12 GLY B 207 TYR B 208 PHE B 209 LEU B 210
SITE 3 AC9 12 LYS B 212 ALA B 213 HIS B 214 MET B 215
CRYST1 83.077 86.090 97.611 90.00 90.00 90.00 P 21 21 21 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 0.012037 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011616 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010245 0.00000
TER 2386 THR A 315
TER 4772 THR B 315
MASTER 334 0 9 26 16 0 21 6 5002 2 74 50
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