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HEADER HYDROLASE 24-JUL-19 6SCD
TITLE POLYESTER HYDROLASE PE-H Y250S MUTANT OF PSEUDOMONAS AESTUSNIGRI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYESTER HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AESTUSNIGRI;
SOURCE 3 ORGANISM_TAXID: 857252;
SOURCE 4 GENE: B7O88_11480;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS POLYESTER DEGRADATION, PET HYDROLASE, MARINE BACTERIA, PSEUDOMONAS
KEYWDS 2 AESTUSNIGRI, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BOLLINGER,S.THIES,S.KOBUS,A.HOEPPNER,S.H.J.SMITS,K.-E.JAEGER
REVDAT 1 26-FEB-20 6SCD 0
JRNL AUTH A.BOLLINGER,S.THIES,S.KOBUS,A.HOEPPNER,S.H.J.SMITS,
JRNL AUTH 2 C.COSCOLIN,M.FERRER,K.-E.JAEGER
JRNL TITL A NOVEL POLYESTER HYDROLASE FROM THE MARINE BACTERIUM
JRNL TITL 2 PSEUDOMONAS AESTUSNIGRI - STRUCTURAL AND FUNCTIONAL INSIGHTS
JRNL REF FRONT MICROBIOL 2020
JRNL REFN ESSN 1664-302X
JRNL DOI 10.3389/FMICB.2020.00114
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 116011
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) : 0.115
REMARK 3 R VALUE (WORKING SET) : 0.113
REMARK 3 FREE R VALUE : 0.152
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 6011
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) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8523
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2000
REMARK 3 BIN FREE R VALUE SET COUNT : 417
REMARK 3 BIN FREE R VALUE : 0.2350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3995
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 493
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : 0.38000
REMARK 3 B33 (A**2) : -0.25000
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): 0.038
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.042
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.027
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.536
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.985
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.976
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4203 ; 0.026 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3770 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5736 ; 2.430 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8707 ; 1.336 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 556 ; 6.725 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 173 ;29.813 ;23.353
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 620 ;11.220 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;15.410 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 617 ; 0.149 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4866 ; 0.015 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 988 ; 0.006 ; 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): 7972 ; 5.799 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 155 ;39.352 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 8206 ;15.367 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6SCD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1292103437.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-19
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) : 0.950500
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 122029
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 77.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.050
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04300
REMARK 200 FOR THE DATA SET : 14.9800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
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) : 0.43900
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: PHASER
REMARK 200 STARTING MODEL: 6SBN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULPHATE, 0.1 M SODIUM
REMARK 280 CITRATE PH 3.5, 28 % (V/V) PEG 400, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-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 47.26300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.61650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.13400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.61650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.26300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.13400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 47.26300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.13400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 60.61650
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.13400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 47.26300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 60.61650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 1
REMARK 465 PRO A 2
REMARK 465 PHE A 3
REMARK 465 ASN A 4
REMARK 465 LYS A 5
REMARK 465 LYS A 6
REMARK 465 SER A 7
REMARK 465 VAL A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 LEU A 11
REMARK 465 CYS A 12
REMARK 465 GLY A 13
REMARK 465 ALA A 14
REMARK 465 GLY A 15
REMARK 465 ALA A 16
REMARK 465 LEU A 17
REMARK 465 LEU A 18
REMARK 465 PHE A 19
REMARK 465 SER A 20
REMARK 465 MET A 21
REMARK 465 SER A 22
REMARK 465 ALA A 23
REMARK 465 LEU A 24
REMARK 465 ALA A 25
REMARK 465 ASN A 26
REMARK 465 ASN A 27
REMARK 465 PRO A 28
REMARK 465 ALA A 29
REMARK 465 PRO A 30
REMARK 465 THR A 31
REMARK 465 ASP A 32
REMARK 465 PRO A 33
REMARK 465 GLY A 34
REMARK 465 ASP A 35
REMARK 465 SER A 36
REMARK 465 GLY A 37
REMARK 465 GLY A 38
REMARK 465 GLY A 39
REMARK 465 GLU A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 PHE B 3
REMARK 465 ASN B 4
REMARK 465 LYS B 5
REMARK 465 LYS B 6
REMARK 465 SER B 7
REMARK 465 VAL B 8
REMARK 465 LEU B 9
REMARK 465 ALA B 10
REMARK 465 LEU B 11
REMARK 465 CYS B 12
REMARK 465 GLY B 13
REMARK 465 ALA B 14
REMARK 465 GLY B 15
REMARK 465 ALA B 16
REMARK 465 LEU B 17
REMARK 465 LEU B 18
REMARK 465 PHE B 19
REMARK 465 SER B 20
REMARK 465 MET B 21
REMARK 465 SER B 22
REMARK 465 ALA B 23
REMARK 465 LEU B 24
REMARK 465 ALA B 25
REMARK 465 ASN B 26
REMARK 465 ASN B 27
REMARK 465 PRO B 28
REMARK 465 ALA B 29
REMARK 465 PRO B 30
REMARK 465 THR B 31
REMARK 465 ASP B 32
REMARK 465 PRO B 33
REMARK 465 GLY B 34
REMARK 465 ASP B 35
REMARK 465 SER B 36
REMARK 465 GLY B 37
REMARK 465 GLY B 38
REMARK 465 GLY B 39
REMARK 465 GLU B 306
REMARK 465 HIS B 307
REMARK 465 HIS B 308
REMARK 465 HIS B 309
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
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 63 NE CZ NH1 NH2
REMARK 470 LEU A 305 CG CD1 CD2
REMARK 470 SER B 40 OG
REMARK 470 ARG B 63 CD NE CZ NH1 NH2
REMARK 470 ARG B 66 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 98 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 157 CG CD NE CZ NH1 NH2
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 O HOH B 525 O HOH B 677 2.10
REMARK 500 OE1 GLN B 294 O HOH B 501 2.11
REMARK 500 O HOH A 511 O HOH A 690 2.12
REMARK 500 O HOH B 667 O HOH B 703 2.13
REMARK 500 O HOH A 676 O HOH A 696 2.14
REMARK 500 OE1 GLU A 243 O HOH A 501 2.15
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 GLU A 102 CB GLU A 102 CG -0.133
REMARK 500 GLU A 102 CD GLU A 102 OE2 -0.109
REMARK 500 SER A 152 CB SER A 152 OG -0.087
REMARK 500 GLU A 183 CD GLU A 183 OE1 0.094
REMARK 500 SER A 256 CB SER A 256 OG -0.212
REMARK 500 GLU A 276 CD GLU A 276 OE1 -0.080
REMARK 500 SER B 40 CA SER B 40 CB 0.155
REMARK 500 GLY B 97 N GLY B 97 CA 0.093
REMARK 500 GLU B 102 CB GLU B 102 CG -0.141
REMARK 500 GLU B 102 CD GLU B 102 OE1 -0.072
REMARK 500 GLU B 183 CD GLU B 183 OE2 -0.070
REMARK 500 GLU B 215 CD GLU B 215 OE2 0.080
REMARK 500 SER B 232 CA SER B 232 CB 0.092
REMARK 500 ASN B 288 N ASN B 288 CA 0.133
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 ARG A 66 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 66 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 GLU A 102 OE1 - CD - OE2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 GLU A 102 CG - CD - OE1 ANGL. DEV. = 12.5 DEGREES
REMARK 500 ASP A 106 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 106 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 PHE A 128 CB - CG - CD2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 136 NE - CZ - NH1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 GLU A 243 OE1 - CD - OE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP A 292 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG A 299 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 44 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU B 112 CB - CG - CD1 ANGL. DEV. = 13.6 DEGREES
REMARK 500 PHE B 117 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 PHE B 117 CZ - CE2 - CD2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 PHE B 128 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP B 143 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 TYR B 200 CZ - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP B 238 CB - CG - OD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ARG B 264 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP B 275 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 277 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 TYR B 280 CD1 - CE1 - CZ ANGL. DEV. = 6.5 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 SER A 171 -118.88 65.52
REMARK 500 HIS A 225 -87.27 -134.55
REMARK 500 SER A 256 -127.17 -125.81
REMARK 500 VAL B 99 22.04 45.24
REMARK 500 SER B 171 -122.95 67.43
REMARK 500 ALA B 220 70.69 -118.86
REMARK 500 HIS B 225 -89.51 -129.55
REMARK 500 SER B 256 -134.75 -126.76
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 ASP A 106 0.09 SIDE CHAIN
REMARK 500 ARG A 134 0.11 SIDE CHAIN
REMARK 500 ARG B 134 0.09 SIDE CHAIN
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 GLY B 58 -10.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 780 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A 781 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A 782 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A 783 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A 784 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH A 785 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH A 786 DISTANCE = 7.33 ANGSTROMS
REMARK 525 HOH A 787 DISTANCE = 7.90 ANGSTROMS
REMARK 525 HOH A 788 DISTANCE = 8.09 ANGSTROMS
REMARK 525 HOH B 705 DISTANCE = 6.42 ANGSTROMS
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 NA A 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 290 O
REMARK 620 2 ASP A 292 O 92.7
REMARK 620 3 ILE A 295 O 90.0 84.4
REMARK 620 4 HOH A 607 O 94.1 87.2 170.8
REMARK 620 5 HOH A 693 O 173.1 93.7 87.9 88.9
REMARK 620 6 HOH A 714 O 85.0 173.2 101.9 86.6 89.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 171 OG
REMARK 620 2 HOH B 606 O 63.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO B 194 O
REMARK 620 2 ALA B 220 O 109.9
REMARK 620 3 HOH B 607 O 134.3 77.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6SBN RELATED DB: PDB
REMARK 900 WILDTYPE
DBREF1 6SCD A 1 304 UNP A0A1H6AD45_9PSED
DBREF2 6SCD A A0A1H6AD45 1 304
DBREF1 6SCD B 1 304 UNP A0A1H6AD45_9PSED
DBREF2 6SCD B A0A1H6AD45 1 304
SEQADV 6SCD SER A 250 UNP A0A1H6AD4 TYR 250 ENGINEERED MUTATION
SEQADV 6SCD LEU A 305 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD GLU A 306 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD HIS A 307 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD HIS A 308 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD HIS A 309 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD HIS A 310 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD HIS A 311 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD HIS A 312 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD SER B 250 UNP A0A1H6AD4 TYR 250 ENGINEERED MUTATION
SEQADV 6SCD LEU B 305 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD GLU B 306 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD HIS B 307 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD HIS B 308 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD HIS B 309 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD HIS B 310 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD HIS B 311 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SCD HIS B 312 UNP A0A1H6AD4 EXPRESSION TAG
SEQRES 1 A 312 MET PRO PHE ASN LYS LYS SER VAL LEU ALA LEU CYS GLY
SEQRES 2 A 312 ALA GLY ALA LEU LEU PHE SER MET SER ALA LEU ALA ASN
SEQRES 3 A 312 ASN PRO ALA PRO THR ASP PRO GLY ASP SER GLY GLY GLY
SEQRES 4 A 312 SER ALA TYR GLN ARG GLY PRO ASP PRO SER VAL SER PHE
SEQRES 5 A 312 LEU GLU ALA ASP ARG GLY GLN TYR SER VAL ARG SER SER
SEQRES 6 A 312 ARG VAL SER SER LEU VAL SER GLY PHE GLY GLY GLY THR
SEQRES 7 A 312 ILE TYR TYR PRO THR GLY THR THR GLY THR MET GLY ALA
SEQRES 8 A 312 VAL VAL VAL ILE PRO GLY PHE VAL SER ALA GLU SER SER
SEQRES 9 A 312 ILE ASP TRP TRP GLY PRO LYS LEU ALA SER TYR GLY PHE
SEQRES 10 A 312 VAL VAL MET THR ILE ASP THR ASN THR GLY PHE ASP GLN
SEQRES 11 A 312 PRO PRO SER ARG ALA ARG GLN ILE ASN ASN ALA LEU ASP
SEQRES 12 A 312 TYR LEU VAL SER GLN ASN SER ARG SER SER SER PRO VAL
SEQRES 13 A 312 ARG GLY MET ILE ASP THR ASN ARG LEU GLY VAL ILE GLY
SEQRES 14 A 312 TRP SER MET GLY GLY GLY GLY THR LEU ARG VAL ALA SER
SEQRES 15 A 312 GLU GLY ARG ILE LYS ALA ALA ILE PRO LEU ALA PRO TRP
SEQRES 16 A 312 ASP THR THR SER TYR TYR ALA SER ARG SER GLN ALA PRO
SEQRES 17 A 312 THR LEU ILE PHE ALA CYS GLU SER ASP VAL ILE ALA PRO
SEQRES 18 A 312 VAL LEU GLN HIS ALA SER PRO PHE TYR ASN SER LEU PRO
SEQRES 19 A 312 SER SER ILE ASP LYS ALA PHE VAL GLU ILE ASN GLY GLY
SEQRES 20 A 312 SER HIS SER CYS GLY ASN GLY GLY SER ILE TYR ASN ASP
SEQRES 21 A 312 VAL LEU SER ARG PHE GLY VAL SER TRP MET LYS LEU HIS
SEQRES 22 A 312 LEU ASP GLU ASP SER ARG TYR LYS GLN PHE LEU CYS GLY
SEQRES 23 A 312 PRO ASN HIS THR SER ASP SER GLN ILE SER ASP TYR ARG
SEQRES 24 A 312 GLY ASN CYS PRO TYR LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 312 MET PRO PHE ASN LYS LYS SER VAL LEU ALA LEU CYS GLY
SEQRES 2 B 312 ALA GLY ALA LEU LEU PHE SER MET SER ALA LEU ALA ASN
SEQRES 3 B 312 ASN PRO ALA PRO THR ASP PRO GLY ASP SER GLY GLY GLY
SEQRES 4 B 312 SER ALA TYR GLN ARG GLY PRO ASP PRO SER VAL SER PHE
SEQRES 5 B 312 LEU GLU ALA ASP ARG GLY GLN TYR SER VAL ARG SER SER
SEQRES 6 B 312 ARG VAL SER SER LEU VAL SER GLY PHE GLY GLY GLY THR
SEQRES 7 B 312 ILE TYR TYR PRO THR GLY THR THR GLY THR MET GLY ALA
SEQRES 8 B 312 VAL VAL VAL ILE PRO GLY PHE VAL SER ALA GLU SER SER
SEQRES 9 B 312 ILE ASP TRP TRP GLY PRO LYS LEU ALA SER TYR GLY PHE
SEQRES 10 B 312 VAL VAL MET THR ILE ASP THR ASN THR GLY PHE ASP GLN
SEQRES 11 B 312 PRO PRO SER ARG ALA ARG GLN ILE ASN ASN ALA LEU ASP
SEQRES 12 B 312 TYR LEU VAL SER GLN ASN SER ARG SER SER SER PRO VAL
SEQRES 13 B 312 ARG GLY MET ILE ASP THR ASN ARG LEU GLY VAL ILE GLY
SEQRES 14 B 312 TRP SER MET GLY GLY GLY GLY THR LEU ARG VAL ALA SER
SEQRES 15 B 312 GLU GLY ARG ILE LYS ALA ALA ILE PRO LEU ALA PRO TRP
SEQRES 16 B 312 ASP THR THR SER TYR TYR ALA SER ARG SER GLN ALA PRO
SEQRES 17 B 312 THR LEU ILE PHE ALA CYS GLU SER ASP VAL ILE ALA PRO
SEQRES 18 B 312 VAL LEU GLN HIS ALA SER PRO PHE TYR ASN SER LEU PRO
SEQRES 19 B 312 SER SER ILE ASP LYS ALA PHE VAL GLU ILE ASN GLY GLY
SEQRES 20 B 312 SER HIS SER CYS GLY ASN GLY GLY SER ILE TYR ASN ASP
SEQRES 21 B 312 VAL LEU SER ARG PHE GLY VAL SER TRP MET LYS LEU HIS
SEQRES 22 B 312 LEU ASP GLU ASP SER ARG TYR LYS GLN PHE LEU CYS GLY
SEQRES 23 B 312 PRO ASN HIS THR SER ASP SER GLN ILE SER ASP TYR ARG
SEQRES 24 B 312 GLY ASN CYS PRO TYR LEU GLU HIS HIS HIS HIS HIS HIS
HET SO4 A 401 5
HET PO4 A 402 5
HET PO4 A 403 5
HET NA A 404 1
HET CL A 405 1
HET CL A 406 1
HET PEG A 407 7
HET GOL A 408 6
HET GOL A 409 6
HET ACT A 410 4
HET PO4 B 401 5
HET NA B 402 1
HET NA B 403 1
HET CL B 404 1
HETNAM SO4 SULFATE ION
HETNAM PO4 PHOSPHATE ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 O4 S 2-
FORMUL 4 PO4 3(O4 P 3-)
FORMUL 6 NA 3(NA 1+)
FORMUL 7 CL 3(CL 1-)
FORMUL 9 PEG C4 H10 O3
FORMUL 10 GOL 2(C3 H8 O3)
FORMUL 12 ACT C2 H3 O2 1-
FORMUL 17 HOH *493(H2 O)
HELIX 1 AA1 SER A 49 ALA A 55 1 7
HELIX 2 AA2 ALA A 101 ASP A 106 5 6
HELIX 3 AA3 TRP A 107 SER A 114 1 8
HELIX 4 AA4 GLN A 130 ASN A 149 1 20
HELIX 5 AA5 SER A 171 SER A 182 1 12
HELIX 6 AA6 TYR A 201 SER A 205 5 5
HELIX 7 AA7 HIS A 225 LEU A 233 1 9
HELIX 8 AA8 TYR A 258 ASP A 275 1 18
HELIX 9 AA9 ASP A 277 ARG A 279 5 3
HELIX 10 AB1 TYR A 280 CYS A 285 1 6
HELIX 11 AB2 ASN A 288 ASP A 292 5 5
HELIX 12 AB3 SER B 49 ALA B 55 1 7
HELIX 13 AB4 ALA B 101 ASP B 106 5 6
HELIX 14 AB5 TRP B 107 SER B 114 1 8
HELIX 15 AB6 GLN B 130 SER B 150 1 21
HELIX 16 AB7 SER B 171 SER B 182 1 12
HELIX 17 AB8 SER B 199 ARG B 204 1 6
HELIX 18 AB9 HIS B 225 LEU B 233 1 9
HELIX 19 AC1 TYR B 258 GLU B 276 1 19
HELIX 20 AC2 ASP B 277 ARG B 279 5 3
HELIX 21 AC3 TYR B 280 CYS B 285 1 6
HELIX 22 AC4 ASN B 288 ASP B 292 5 5
SHEET 1 AA1 6 VAL A 62 VAL A 67 0
SHEET 2 AA1 6 GLY A 77 PRO A 82 -1 O ILE A 79 N SER A 65
SHEET 3 AA1 6 PHE A 117 ILE A 122 -1 O VAL A 119 N TYR A 80
SHEET 4 AA1 6 MET A 89 ILE A 95 1 N VAL A 92 O MET A 120
SHEET 5 AA1 6 ILE A 160 TRP A 170 1 O ASP A 161 N MET A 89
SHEET 6 AA1 6 ALA A 188 LEU A 192 1 O LEU A 192 N GLY A 169
SHEET 1 AA2 3 THR A 209 CYS A 214 0
SHEET 2 AA2 3 LYS A 239 ILE A 244 1 O ILE A 244 N ALA A 213
SHEET 3 AA2 3 ILE A 295 GLY A 300 -1 O ASP A 297 N GLU A 243
SHEET 1 AA3 6 VAL B 62 VAL B 67 0
SHEET 2 AA3 6 GLY B 77 PRO B 82 -1 O ILE B 79 N SER B 65
SHEET 3 AA3 6 VAL B 118 ILE B 122 -1 O VAL B 119 N TYR B 80
SHEET 4 AA3 6 MET B 89 ILE B 95 1 N VAL B 94 O ILE B 122
SHEET 5 AA3 6 ILE B 160 TRP B 170 1 O GLY B 166 N ALA B 91
SHEET 6 AA3 6 ALA B 188 LEU B 192 1 O LEU B 192 N GLY B 169
SHEET 1 AA4 3 THR B 209 CYS B 214 0
SHEET 2 AA4 3 LYS B 239 ILE B 244 1 O ILE B 244 N ALA B 213
SHEET 3 AA4 3 ILE B 295 GLY B 300 -1 O ASP B 297 N GLU B 243
SSBOND 1 CYS A 214 CYS A 251 1555 1555 2.04
SSBOND 2 CYS A 285 CYS A 302 1555 1555 2.07
SSBOND 3 CYS B 214 CYS B 251 1555 1555 2.04
SSBOND 4 CYS B 285 CYS B 302 1555 1555 2.07
LINK O THR A 290 NA NA A 404 1555 1555 2.36
LINK O ASP A 292 NA NA A 404 1555 1555 2.45
LINK O ILE A 295 NA NA A 404 1555 1555 2.24
LINK OG SER B 171 NA NA B 402 1555 1555 2.87
LINK O PRO B 194 NA NA B 403 1555 1555 2.91
LINK O ALA B 220 NA NA B 403 1555 1555 2.76
LINK NA NA A 404 O HOH A 607 1555 1555 2.49
LINK NA NA A 404 O HOH A 693 1555 1555 2.41
LINK NA NA A 404 O HOH A 714 1555 1555 2.40
LINK NA NA B 402 O HOH B 606 1555 1555 3.18
LINK NA NA B 403 O HOH B 607 1555 1555 3.03
CISPEP 1 CYS A 302 PRO A 303 0 -2.97
CISPEP 2 CYS B 302 PRO B 303 0 -0.09
SITE 1 AC1 9 GLY A 73 ASN A 125 ASP A 129 SER A 133
SITE 2 AC1 9 ARG A 136 GLN A 137 HOH A 524 HOH A 553
SITE 3 AC1 9 HOH A 750
SITE 1 AC2 5 PRO A 132 ARG A 179 TYR A 201 HOH A 513
SITE 2 AC2 5 HOH A 571
SITE 1 AC3 4 ARG A 44 GLY A 45 GLN A 59 TYR A 60
SITE 1 AC4 6 THR A 290 ASP A 292 ILE A 295 HOH A 607
SITE 2 AC4 6 HOH A 693 HOH A 714
SITE 1 AC5 3 VAL A 218 HIS A 249 SER B 250
SITE 1 AC6 4 PHE A 98 SER A 171 MET A 172 HOH A 587
SITE 1 AC7 7 LEU A 70 VAL A 99 SER A 100 THR A 124
SITE 2 AC7 7 GLY A 127 HOH A 547 HOH A 580
SITE 1 AC8 7 SER A 235 LYS A 239 GLY A 300 ASN A 301
SITE 2 AC8 7 HOH A 548 HOH A 567 HOH A 779
SITE 1 AC9 5 GLU A 54 HOH A 534 HOH A 670 GLU B 215
SITE 2 AC9 5 SER B 216
SITE 1 AD1 5 SER A 235 SER A 236 ILE A 237 ASP A 238
SITE 2 AD1 5 ASN A 301
SITE 1 AD2 3 HOH A 786 ARG B 179 TYR B 201
SITE 1 AD3 3 PHE B 98 SER B 171 MET B 172
SITE 1 AD4 5 PRO B 194 ALA B 220 HIS B 225 ALA B 226
SITE 2 AD4 5 HOH B 607
SITE 1 AD5 5 HOH A 743 ASP B 217 VAL B 218 HIS B 249
SITE 2 AD5 5 HOH B 558
CRYST1 94.526 98.268 121.233 90.00 90.00 90.00 I 21 21 21 16
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 0.010579 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010176 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008249 0.00000
TER 2044 LEU A 305
TER 4050 LEU B 305
MASTER 628 0 14 22 18 0 24 6 4537 2 66 48
END |