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HEADER HYDROLASE 03-MAY-22 7ZR3
TITLE STRUCTURE OF ESTER-HYDROLASE EH0 FROM THE METAGENOME OF SORGHUM
TITLE 2 BICOLOR RHIZOSPHERE FROM THE HENFAES RESEARCH CENTRE (GWYNEDD, WALES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EH0;
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(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: P15TV-L
KEYWDS ESTER HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.CEA-RAMA,J.SANZ-APARICIO
REVDAT 1 28-DEC-22 7ZR3 0
JRNL AUTH I.CEA-RAMA,J.SANZ-APARICIO
JRNL TITL STRUCTURE OF ESTER-HYDROLASE EH0 FROM THE METAGENOME OF
JRNL TITL 2 SORGHUM BICOLOR RHIZOSPHERE FROM THE HENFAES RESEARCH CENTRE
JRNL TITL 3 (GWYNEDD, WALES)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 61522
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3250
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4485
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 220
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4741
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 432
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.70000
REMARK 3 B22 (A**2) : -0.38000
REMARK 3 B33 (A**2) : 1.08000
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): 0.126
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.121
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.145
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4942 ; 0.010 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4685 ; 0.003 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6740 ; 1.484 ; 1.641
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10818 ; 1.384 ; 1.572
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 646 ; 6.297 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 236 ;25.345 ;21.271
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 727 ;13.878 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;15.263 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 627 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5639 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1069 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 16 4
REMARK 3 1 B 3 B 16 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 240 ; 1.890 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 240 ;10.910 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 37 A 317 4
REMARK 3 1 B 37 B 317 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 4110 ; 0.390 ; 0.500
REMARK 3 MEDIUM THERMAL 2 A (A**2): 4110 ; 9.000 ; 2.000
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7ZR3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAY-22.
REMARK 100 THE DEPOSITION ID IS D_1292122542.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-17
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) : 1.07218
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 0.5.32
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64849
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 64.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.40
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.60
REMARK 200 R MERGE FOR SHELL (I) : 0.67700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.5.02
REMARK 200 STARTING MODEL: 4YPV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG8000, 100MM BIS-TRIS PH 5.5,
REMARK 280 100MM AMMONIUM ACETATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 31.97900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.27850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.33300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.27850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.97900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.33300
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 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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ALA A 322
REMARK 465 ALA A 323
REMARK 465 ALA A 324
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 ARG B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 318
REMARK 465 MET B 319
REMARK 465 ALA B 320
REMARK 465 GLN B 321
REMARK 465 ALA B 322
REMARK 465 ALA B 323
REMARK 465 ALA B 324
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 31 N - CA - CB ANGL. DEV. = -7.8 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 LYS A 24 -19.84 -49.28
REMARK 500 GLU A 27 -78.92 -67.52
REMARK 500 LEU A 28 -134.22 49.72
REMARK 500 ASP A 95 -162.20 -164.69
REMARK 500 PRO A 128 39.91 -99.61
REMARK 500 SER A 161 -118.91 56.92
REMARK 500 TYR A 190 60.82 29.73
REMARK 500 THR A 212 151.34 79.92
REMARK 500 PHE B 5 -64.66 77.57
REMARK 500 ASP B 95 -166.90 -165.26
REMARK 500 SER B 161 -121.79 56.70
REMARK 500 TYR B 190 57.37 33.40
REMARK 500 THR B 212 154.31 84.30
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7ZR3 A -20 324 PDB 7ZR3 7ZR3 -20 324
DBREF 7ZR3 B -20 324 PDB 7ZR3 7ZR3 -20 324
SEQRES 1 A 345 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 345 ARG GLU ASN LEU TYR PHE GLN GLY MET THR GLU LEU PHE
SEQRES 3 A 345 VAL ARG PRO ASP VAL ARG GLY PHE LEU ASP PHE LEU ASN
SEQRES 4 A 345 ASN LEU PRO GLY PRO LYS MET HIS GLU LEU ASP ALA PRO
SEQRES 5 A 345 THR ALA ARG GLN MET TYR VAL ALA MET LYS ASP VAL GLY
SEQRES 6 A 345 ASP PRO PRO VAL GLY GLU LEU GLY THR LEU LEU ASP LEU
SEQRES 7 A 345 SER ILE PRO GLY PRO GLY GLY ASP ILE PRO ALA ARG LEU
SEQRES 8 A 345 TYR ASP PRO ARG ALA SER ARG GLU PRO GLY PRO ALA ILE
SEQRES 9 A 345 VAL PHE PHE HIS GLY GLY GLY PHE VAL ILE GLY ASP LEU
SEQRES 10 A 345 GLU SER HIS GLY SER PHE THR ALA GLU MET ALA ARG VAL
SEQRES 11 A 345 LEU ASP LEU PRO VAL ILE ALA VAL ASP TYR ARG LEU ALA
SEQRES 12 A 345 PRO GLU PHE PRO TRP PRO ALA ALA PRO ASP ASP CYS GLU
SEQRES 13 A 345 ALA ALA ALA ARG TRP VAL ALA ASN SER PRO ALA GLU LEU
SEQRES 14 A 345 GLY ARG SER VAL THR SER LEU VAL LEU CYS GLY ASP SER
SEQRES 15 A 345 ALA GLY GLY ASN LEU VAL ILE VAL THR ALA ALA ALA LEU
SEQRES 16 A 345 ARG ASP GLN PRO ALA LYS VAL PRO VAL ILE ALA GLN LEU
SEQRES 17 A 345 PRO PHE TYR PRO ALA THR ASP ALA SER LYS GLU TYR PRO
SEQRES 18 A 345 SER TYR ALA GLU PHE ALA GLU GLY TYR LEU LEU THR ARG
SEQRES 19 A 345 ASP SER MET GLU TRP PHE MET ALA ALA TYR LYS SER GLU
SEQRES 20 A 345 ALA ASP HIS ILE ARG SER SER PRO LEU LEU GLY ASP LEU
SEQRES 21 A 345 ALA GLY MET PRO PRO ALA VAL VAL VAL THR GLY GLY LEU
SEQRES 22 A 345 ASP PRO ILE ARG ASP GLN GLY ARG ALA TYR ALA ALA ALA
SEQRES 23 A 345 LEU ALA LEU ALA GLY VAL PRO VAL VAL PHE ARG GLU ALA
SEQRES 24 A 345 LYS GLY ASN ILE HIS GLY PHE ILE THR LEU ARG LYS ALA
SEQRES 25 A 345 ILE PRO SER SER VAL GLY ASP VAL MET GLY ALA PHE ALA
SEQRES 26 A 345 ALA LEU LYS ASP ILE ILE VAL GLU ALA GLU GLY ASP ARG
SEQRES 27 A 345 ALA MET ALA GLN ALA ALA ALA
SEQRES 1 B 345 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 345 ARG GLU ASN LEU TYR PHE GLN GLY MET THR GLU LEU PHE
SEQRES 3 B 345 VAL ARG PRO ASP VAL ARG GLY PHE LEU ASP PHE LEU ASN
SEQRES 4 B 345 ASN LEU PRO GLY PRO LYS MET HIS GLU LEU ASP ALA PRO
SEQRES 5 B 345 THR ALA ARG GLN MET TYR VAL ALA MET LYS ASP VAL GLY
SEQRES 6 B 345 ASP PRO PRO VAL GLY GLU LEU GLY THR LEU LEU ASP LEU
SEQRES 7 B 345 SER ILE PRO GLY PRO GLY GLY ASP ILE PRO ALA ARG LEU
SEQRES 8 B 345 TYR ASP PRO ARG ALA SER ARG GLU PRO GLY PRO ALA ILE
SEQRES 9 B 345 VAL PHE PHE HIS GLY GLY GLY PHE VAL ILE GLY ASP LEU
SEQRES 10 B 345 GLU SER HIS GLY SER PHE THR ALA GLU MET ALA ARG VAL
SEQRES 11 B 345 LEU ASP LEU PRO VAL ILE ALA VAL ASP TYR ARG LEU ALA
SEQRES 12 B 345 PRO GLU PHE PRO TRP PRO ALA ALA PRO ASP ASP CYS GLU
SEQRES 13 B 345 ALA ALA ALA ARG TRP VAL ALA ASN SER PRO ALA GLU LEU
SEQRES 14 B 345 GLY ARG SER VAL THR SER LEU VAL LEU CYS GLY ASP SER
SEQRES 15 B 345 ALA GLY GLY ASN LEU VAL ILE VAL THR ALA ALA ALA LEU
SEQRES 16 B 345 ARG ASP GLN PRO ALA LYS VAL PRO VAL ILE ALA GLN LEU
SEQRES 17 B 345 PRO PHE TYR PRO ALA THR ASP ALA SER LYS GLU TYR PRO
SEQRES 18 B 345 SER TYR ALA GLU PHE ALA GLU GLY TYR LEU LEU THR ARG
SEQRES 19 B 345 ASP SER MET GLU TRP PHE MET ALA ALA TYR LYS SER GLU
SEQRES 20 B 345 ALA ASP HIS ILE ARG SER SER PRO LEU LEU GLY ASP LEU
SEQRES 21 B 345 ALA GLY MET PRO PRO ALA VAL VAL VAL THR GLY GLY LEU
SEQRES 22 B 345 ASP PRO ILE ARG ASP GLN GLY ARG ALA TYR ALA ALA ALA
SEQRES 23 B 345 LEU ALA LEU ALA GLY VAL PRO VAL VAL PHE ARG GLU ALA
SEQRES 24 B 345 LYS GLY ASN ILE HIS GLY PHE ILE THR LEU ARG LYS ALA
SEQRES 25 B 345 ILE PRO SER SER VAL GLY ASP VAL MET GLY ALA PHE ALA
SEQRES 26 B 345 ALA LEU LYS ASP ILE ILE VAL GLU ALA GLU GLY ASP ARG
SEQRES 27 B 345 ALA MET ALA GLN ALA ALA ALA
HET ACT A 401 4
HET ACT A 402 4
HET CL A 403 1
HET GOL A 404 6
HET GOL A 405 6
HET GOL A 406 6
HET PEG A 407 7
HET GOL B 601 6
HETNAM ACT ACETATE ION
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 5 CL CL 1-
FORMUL 6 GOL 4(C3 H8 O3)
FORMUL 9 PEG C4 H10 O3
FORMUL 11 HOH *432(H2 O)
HELIX 1 AA1 ARG A 7 ASN A 19 1 13
HELIX 2 AA2 THR A 32 GLY A 44 1 13
HELIX 3 AA3 HIS A 99 ASP A 111 1 13
HELIX 4 AA4 PRO A 128 ASN A 143 1 16
HELIX 5 AA5 SER A 144 GLY A 149 5 6
HELIX 6 AA6 ALA A 162 GLN A 177 1 16
HELIX 7 AA7 SER A 201 PHE A 205 5 5
HELIX 8 AA8 GLU A 207 THR A 212 1 6
HELIX 9 AA9 THR A 212 ILE A 230 1 19
HELIX 10 AB1 ILE A 255 ALA A 269 1 15
HELIX 11 AB2 GLY A 284 LEU A 288 5 5
HELIX 12 AB3 SER A 294 GLN A 321 1 28
HELIX 13 AB4 ARG B 7 LEU B 20 1 14
HELIX 14 AB5 ASP B 29 GLY B 44 1 16
HELIX 15 AB6 HIS B 99 ASP B 111 1 13
HELIX 16 AB7 PRO B 128 ASN B 143 1 16
HELIX 17 AB8 ALA B 162 GLN B 177 1 16
HELIX 18 AB9 GLU B 207 THR B 212 1 6
HELIX 19 AC1 THR B 212 ILE B 230 1 19
HELIX 20 AC2 ILE B 255 ALA B 269 1 15
HELIX 21 AC3 GLY B 284 LEU B 288 5 5
HELIX 22 AC4 SER B 294 ASP B 316 1 23
SHEET 1 AA1 6 THR A 53 ILE A 59 0
SHEET 2 AA1 6 ILE A 66 ASP A 72 -1 O LEU A 70 N LEU A 55
SHEET 3 AA1 6 VAL A 114 VAL A 117 -1 O VAL A 114 N TYR A 71
SHEET 4 AA1 6 GLY A 80 PHE A 86 1 N ILE A 83 O ILE A 115
SHEET 5 AA1 6 VAL A 152 ASP A 160 1 O VAL A 156 N VAL A 84
SHEET 6 AA1 6 VAL A 183 PHE A 189 1 O LEU A 187 N LEU A 157
SHEET 1 AA2 4 ALA A 245 GLY A 250 0
SHEET 2 AA2 4 VAL A 273 ALA A 278 1 O ALA A 278 N THR A 249
SHEET 3 AA2 4 VAL B 273 ALA B 278 -1 O PHE B 275 N VAL A 273
SHEET 4 AA2 4 ALA B 245 GLY B 250 1 N VAL B 247 O VAL B 274
SHEET 1 AA3 6 THR B 53 GLY B 61 0
SHEET 2 AA3 6 GLY B 64 ASP B 72 -1 O ILE B 66 N ILE B 59
SHEET 3 AA3 6 VAL B 114 VAL B 117 -1 O VAL B 114 N TYR B 71
SHEET 4 AA3 6 GLY B 80 PHE B 86 1 N ILE B 83 O ILE B 115
SHEET 5 AA3 6 VAL B 152 ASP B 160 1 O VAL B 156 N VAL B 84
SHEET 6 AA3 6 VAL B 183 PHE B 189 1 O PHE B 189 N GLY B 159
CISPEP 1 ALA A 122 PRO A 123 0 4.16
CISPEP 2 TRP A 127 PRO A 128 0 4.20
CISPEP 3 ALA B 122 PRO B 123 0 3.02
CISPEP 4 TRP B 127 PRO B 128 0 2.94
CRYST1 63.958 116.666 128.557 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 0.015635 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008571 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007779 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.574761 -0.011867 0.818236 4.53399 1
MTRIX2 2 -0.005299 -0.999820 -0.018223 -23.67794 1
MTRIX3 2 0.818304 -0.014810 0.574594 -6.52646 1
MTRIX1 3 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 3 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 3 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 4 -0.602634 -0.114632 0.789742 6.04181 1
MTRIX2 4 -0.054180 -0.981468 -0.183805 -20.28413 1
MTRIX3 4 0.796177 -0.153555 0.585255 -5.17277 1
TER 2410 GLN A 321
TER 4781 ARG B 317
MASTER 367 0 8 22 16 0 0 18 5213 2 39 54
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