| content |
HEADER HYDROLASE 20-NOV-18 6I8D
TITLE STRUCTURE OF ESTER-HYDROLASE EH1AB1 FROM THE METAGENOME OF LAKE ARREO
TITLE 2 COMPLEXED WITH A DERIVATIVE OF BUTYL 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;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 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 27-NOV-19 6I8D 0
JRNL AUTH I.CEA-RAMA,J.SANZ-APARICIO
JRNL TITL STRUCTURE OF ESTER-HYDROLASE EH1AB1 FROM THE METAGENOME OF
JRNL TITL 2 LAKE ARREO COMPLEXED WITH A DERIVATIVE OF BUTYL
JRNL TITL 3 4-NITROPHENYL HEXYLPHOSPHONATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0222
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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 11539
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) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 622
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 865
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.3850
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 : 79
REMARK 3 SOLVENT ATOMS : 41
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.85000
REMARK 3 B22 (A**2) : -3.76000
REMARK 3 B33 (A**2) : 0.91000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.594
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.491
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.224
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.887
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.815
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4962 ; 0.005 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 4379 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6722 ; 1.057 ; 1.680
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10255 ; 1.014 ; 1.675
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 628 ; 6.188 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 272 ;27.232 ;20.515
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 714 ;13.342 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;17.248 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 634 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5710 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 938 ; 0.002 ; 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 ; 1.587 ; 4.049
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2517 ; 1.583 ; 4.049
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3144 ; 2.786 ; 6.072
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3145 ; 2.786 ; 6.072
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2444 ; 1.857 ; 4.294
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2444 ; 1.857 ; 4.294
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3579 ; 3.195 ; 6.360
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5289 ; 6.139 ;48.501
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5289 ; 6.139 ;48.497
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 9928 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 6I8D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1200012933.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.97924
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 1.11.12
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12184
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 49.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.21800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.52500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.6.02
REMARK 200 STARTING MODEL: 5JD4
REMARK 200
REMARK 200 REMARK: THIN BARS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 45 % PEG P400, 0.1 M BIS-TRIS PH 6.5,
REMARK 280 VAPOR 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 42.62500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.24900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.08050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.24900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.62500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.08050
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: 3230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 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 SER A 160A
REMARK 465 SER A 210A
REMARK 465 SER B 160A
REMARK 465 SER B 210A
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 OG SER A 161 P1 H7N A 401 1.39
REMARK 500 OG SER B 161 P1 H7N B 401 1.40
REMARK 500 O LEU B 27 N HIS B 29 2.16
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 SER A 161 CB - CA - C ANGL. DEV. = 15.8 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 ARG A 21 60.95 -117.48
REMARK 500 VAL A 92 -48.24 -141.85
REMARK 500 ASN A 95 -173.13 -172.77
REMARK 500 SER A 161 -120.36 58.75
REMARK 500 TYR A 189 58.04 29.62
REMARK 500 PHE A 209 -121.12 58.72
REMARK 500 LEU A 210 124.30 -36.57
REMARK 500 TYR A 255 57.56 -113.09
REMARK 500 LEU A 291 56.92 -93.01
REMARK 500 LEU B 24 -25.20 66.87
REMARK 500 PRO B 28 75.27 -68.17
REMARK 500 VAL B 92 -48.28 -141.52
REMARK 500 ASN B 95 -172.92 -172.79
REMARK 500 SER B 161 -126.91 62.68
REMARK 500 TYR B 189 55.10 35.20
REMARK 500 PHE B 209 -121.37 58.34
REMARK 500 LEU B 210 119.77 -37.43
REMARK 500 TYR B 255 57.33 -112.28
REMARK 500 LEU B 291 56.35 -92.29
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 B 18 0.18 SIDE CHAIN
REMARK 500 ARG B 21 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 H7N A 401
REMARK 610 H7N B 401
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H7N A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H7N A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H7N B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide H7N B 402 and SER B
REMARK 800 211
DBREF 6I8D A 1 315 PDB 6I8D 6I8D 1 315
DBREF 6I8D B 1 315 PDB 6I8D 6I8D 1 315
SEQRES 1 A 317 MET LEU LEU PRO GLU THR ARG ASN LEU LEU ASP LEU MET
SEQRES 2 A 317 ASP ALA ALA THR ARG GLY GLY ARG PRO GLY LEU ASP THR
SEQRES 3 A 317 LEU PRO HIS ALA VAL GLY ARG LYS ALA VAL ASP LYS MET
SEQRES 4 A 317 SER GLU ASP GLY GLU ALA ASP PRO PRO GLU VAL ALA GLU
SEQRES 5 A 317 VAL ALA ASN GLY GLY PHE ALA GLY PRO ALA SER GLU ILE
SEQRES 6 A 317 ARG PHE ARG ARG TYR ARG PRO LEU GLY GLU ALA ALA GLY
SEQRES 7 A 317 LEU LEU PRO THR LEU ILE TYR TYR HIS GLY GLY GLY PHE
SEQRES 8 A 317 VAL ILE GLY ASN ILE GLU THR HIS ASP SER THR CYS ARG
SEQRES 9 A 317 ARG LEU ALA ASN LYS SER ARG CYS GLN VAL ILE SER ILE
SEQRES 10 A 317 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA PRO
SEQRES 11 A 317 ILE ASP ASP GLY ILE ALA ALA PHE ARG HIS ILE ARG ASP
SEQRES 12 A 317 ASN ALA GLU SER PHE GLY ALA ASP ALA ALA ARG LEU ALA
SEQRES 13 A 317 VAL GLY GLY ASP SER SER ALA GLY GLY ALA MET ALA ALA
SEQRES 14 A 317 VAL VAL CYS GLN ALA CYS ARG ASP ALA GLY GLU THR GLY
SEQRES 15 A 317 PRO ALA PHE GLN MET LEU ILE TYR PRO ALA THR ASP SER
SEQRES 16 A 317 SER ARG GLU SER ALA SER ARG VAL ALA PHE ALA GLU GLY
SEQRES 17 A 317 TYR PHE LEU SER SER LYS ALA HIS MET ASP TRP PHE TRP
SEQRES 18 A 317 GLU ALA TYR VAL PRO GLU ASP THR ASP LEU THR ASP LEU
SEQRES 19 A 317 ARG LEU SER PRO LEU LEU ALA THR ASP PHE THR GLY LEU
SEQRES 20 A 317 PRO PRO ALA PHE VAL LEU THR ALA GLY TYR ASP PRO LEU
SEQRES 21 A 317 ARG ASP GLU GLY ARG ALA TYR ALA ASP ARG LEU ILE GLU
SEQRES 22 A 317 ALA GLY ILE LYS THR THR TYR VAL ASN TYR PRO GLY THR
SEQRES 23 A 317 ILE HIS GLY PHE PHE SER LEU THR ARG PHE LEU SER GLN
SEQRES 24 A 317 GLY LEU LYS ALA ASN ASP GLU ALA ALA ALA VAL MET GLY
SEQRES 25 A 317 ALA HIS PHE GLY THR
SEQRES 1 B 317 MET LEU LEU PRO GLU THR ARG ASN LEU LEU ASP LEU MET
SEQRES 2 B 317 ASP ALA ALA THR ARG GLY GLY ARG PRO GLY LEU ASP THR
SEQRES 3 B 317 LEU PRO HIS ALA VAL GLY ARG LYS ALA VAL ASP LYS MET
SEQRES 4 B 317 SER GLU ASP GLY GLU ALA ASP PRO PRO GLU VAL ALA GLU
SEQRES 5 B 317 VAL ALA ASN GLY GLY PHE ALA GLY PRO ALA SER GLU ILE
SEQRES 6 B 317 ARG PHE ARG ARG TYR ARG PRO LEU GLY GLU ALA ALA GLY
SEQRES 7 B 317 LEU LEU PRO THR LEU ILE TYR TYR HIS GLY GLY GLY PHE
SEQRES 8 B 317 VAL ILE GLY ASN ILE GLU THR HIS ASP SER THR CYS ARG
SEQRES 9 B 317 ARG LEU ALA ASN LYS SER ARG CYS GLN VAL ILE SER ILE
SEQRES 10 B 317 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA PRO
SEQRES 11 B 317 ILE ASP ASP GLY ILE ALA ALA PHE ARG HIS ILE ARG ASP
SEQRES 12 B 317 ASN ALA GLU SER PHE GLY ALA ASP ALA ALA ARG LEU ALA
SEQRES 13 B 317 VAL GLY GLY ASP SER SER ALA GLY GLY ALA MET ALA ALA
SEQRES 14 B 317 VAL VAL CYS GLN ALA CYS ARG ASP ALA GLY GLU THR GLY
SEQRES 15 B 317 PRO ALA PHE GLN MET LEU ILE TYR PRO ALA THR ASP SER
SEQRES 16 B 317 SER ARG GLU SER ALA SER ARG VAL ALA PHE ALA GLU GLY
SEQRES 17 B 317 TYR PHE LEU SER SER LYS ALA HIS MET ASP TRP PHE TRP
SEQRES 18 B 317 GLU ALA TYR VAL PRO GLU ASP THR ASP LEU THR ASP LEU
SEQRES 19 B 317 ARG LEU SER PRO LEU LEU ALA THR ASP PHE THR GLY LEU
SEQRES 20 B 317 PRO PRO ALA PHE VAL LEU THR ALA GLY TYR ASP PRO LEU
SEQRES 21 B 317 ARG ASP GLU GLY ARG ALA TYR ALA ASP ARG LEU ILE GLU
SEQRES 22 B 317 ALA GLY ILE LYS THR THR TYR VAL ASN TYR PRO GLY THR
SEQRES 23 B 317 ILE HIS GLY PHE PHE SER LEU THR ARG PHE LEU SER GLN
SEQRES 24 B 317 GLY LEU LYS ALA ASN ASP GLU ALA ALA ALA VAL MET GLY
SEQRES 25 B 317 ALA HIS PHE GLY THR
HET H7N A 401 13
HET H7N A 402 13
HET PEG A 403 7
HET PEG A 404 7
HET GOL A 405 6
HET H7N B 401 13
HET H7N B 402 13
HET PEG B 403 7
HETNAM H7N BUTOXY(HEXYL)PHOSPHINIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 H7N 4(C10 H23 O3 P)
FORMUL 5 PEG 3(C4 H10 O3)
FORMUL 7 GOL C3 H8 O3
FORMUL 11 HOH *41(H2 O)
HELIX 1 AA1 LEU A 3 GLY A 20 1 18
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 ASN A 95 THR A 98 5 4
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 ARG A 259 ALA A 272 1 14
HELIX 13 AB4 LEU A 295 GLY A 314 1 20
HELIX 14 AB5 LEU B 3 ARG B 18 1 16
HELIX 15 AB6 PRO B 28 GLU B 44 1 17
HELIX 16 AB7 ASN B 95 THR B 98 5 4
HELIX 17 AB8 HIS B 99 ARG B 111 1 13
HELIX 18 AB9 PRO B 128 ASN B 144 1 17
HELIX 19 AC1 ALA B 145 PHE B 148 5 4
HELIX 20 AC2 SER B 161 ALA B 177 1 17
HELIX 21 AC3 SER B 198 PHE B 204 1 7
HELIX 22 AC4 SER B 211 VAL B 223 1 13
HELIX 23 AC5 SER B 235 ALA B 239 5 5
HELIX 24 AC6 ARG B 259 ALA B 272 1 14
HELIX 25 AC7 LEU B 295 GLY B 314 1 20
SHEET 1 AA116 GLU A 52 ALA A 59 0
SHEET 2 AA116 GLU A 64 ARG A 71 -1 O ARG A 69 N ALA A 54
SHEET 3 AA116 GLN A 113 ASP A 118 -1 O VAL A 114 N TYR A 70
SHEET 4 AA116 LEU A 80 TYR A 86 1 N LEU A 83 O ILE A 115
SHEET 5 AA116 ALA A 150 ASP A 160 1 O ALA A 156 N THR A 82
SHEET 6 AA116 GLN A 185 ILE A 188 1 O MET A 186 N VAL A 157
SHEET 7 AA116 ALA A 248 TYR A 255 1 O PHE A 249 N LEU A 187
SHEET 8 AA116 THR A 276 ILE A 285 1 O THR A 277 N VAL A 250
SHEET 9 AA116 THR B 276 ILE B 285 -1 O TYR B 278 N TYR A 278
SHEET 10 AA116 ALA B 248 TYR B 255 1 N VAL B 250 O THR B 277
SHEET 11 AA116 GLN B 185 ILE B 188 1 N LEU B 187 O PHE B 249
SHEET 12 AA116 ALA B 150 ASP B 160 1 N VAL B 157 O MET B 186
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 LEU B 83
SHEET 15 AA116 GLU B 64 ARG B 71 -1 N TYR B 70 O VAL B 114
SHEET 16 AA116 GLU B 52 ALA B 59 -1 N PHE B 58 O ILE B 65
LINK OG SER A 211 P1 H7N A 402 1555 1555 1.44
LINK OG SER B 211 P1 H7N B 402 1555 1555 1.45
CISPEP 1 ALA A 122 PRO A 123 0 5.33
CISPEP 2 PHE A 127 PRO A 128 0 5.97
CISPEP 3 ALA B 122 PRO B 123 0 5.79
CISPEP 4 PHE B 127 PRO B 128 0 5.90
SITE 1 AC1 6 GLY A 89 GLY A 90 SER A 161 ALA A 162
SITE 2 AC1 6 PHE A 209 HIS A 286
SITE 1 AC2 7 ASP A 14 GLU A 206 GLY A 207 TYR A 208
SITE 2 AC2 7 PHE A 209 LEU A 210 SER A 211
SITE 1 AC3 5 ARG A 259 ASP A 260 ARG A 263 ASN A 280
SITE 2 AC3 5 ILE B 270
SITE 1 AC4 6 GLU A 52 GLY B 57 PHE B 67 HIS B 140
SITE 2 AC4 6 SER B 147 PHE B 148
SITE 1 AC5 4 SER A 194 ARG A 201 LYS A 212 TRP A 219
SITE 1 AC6 7 GLY B 89 GLY B 90 SER B 161 ALA B 162
SITE 2 AC6 7 PHE B 209 LEU B 210 HIS B 286
SITE 1 AC7 5 ILE A 270 ARG B 259 ASP B 260 ARG B 263
SITE 2 AC7 5 ASN B 280
SITE 1 AC8 11 ASP B 14 ALA B 205 GLU B 206 GLY B 207
SITE 2 AC8 11 TYR B 208 PHE B 209 LEU B 210 LYS B 212
SITE 3 AC8 11 ALA B 213 HIS B 214 MET B 215
CRYST1 85.250 88.161 98.498 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 0.011730 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011343 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010152 0.00000
TER 2386 THR A 315
TER 4772 THR B 315
MASTER 379 0 8 25 16 0 16 6 4890 2 81 50
END |