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HEADER HYDROLASE 16-NOV-24 9KMF
TITLE THE CRYSTAL STRUCTURE OF DSPETASE01 FROM BIORTUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ECTOPSEUDOMONAS MENDOCINA YMP;
SOURCE 3 ORGANISM_TAXID: 399739;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 561
KEYWDS POLYESTERASE-LIPASE-CUTINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.WAN,F.WANG,Z.LV,D.LIN,W.PAN,H.SHANG,J.SUN
REVDAT 1 19-NOV-25 9KMF 0
JRNL AUTH T.WAN,F.WANG,Z.LV,D.LIN,W.PAN,H.SHANG,J.SUN
JRNL TITL THE CRYSTAL STRUCTURE OF DSPETASE01 FROM BIORTUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0430
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 105278
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.129
REMARK 3 FREE R VALUE : 0.148
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.968
REMARK 3 FREE R VALUE TEST SET COUNT : 5230
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7195
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.1740
REMARK 3 BIN FREE R VALUE SET COUNT : 373
REMARK 3 BIN FREE R VALUE : 0.1970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3898
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 839
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.31100
REMARK 3 B22 (A**2) : -0.26600
REMARK 3 B33 (A**2) : -0.04500
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): 0.046
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.027
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.656
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.972
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4265 ; 0.012 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 3894 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5807 ; 1.897 ; 1.800
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8990 ; 0.644 ; 1.747
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 574 ; 6.181 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 45 ; 8.321 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 625 ;10.361 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 640 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5237 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1047 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 763 ; 0.222 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 56 ; 0.159 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2115 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 605 ; 0.229 ; 0.200
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): 2149 ; 1.142 ; 0.961
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2132 ; 1.073 ; 0.957
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2670 ; 1.626 ; 1.719
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2671 ; 1.628 ; 1.720
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2116 ; 1.989 ; 1.178
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2117 ; 1.990 ; 1.178
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3105 ; 3.013 ; 2.051
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3106 ; 3.013 ; 2.051
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 : 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 : MASK BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 9KMF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 19-NOV-24.
REMARK 100 THE DEPOSITION ID IS D_1300053836.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-24
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 : SPRING-8
REMARK 200 BEAMLINE : BL45XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105378
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 44.291
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
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) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MORDA
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH8.5, 20% PEG6,000,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 21.83500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.44800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.87400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.44800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.83500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.87400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
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 GLY A 1
REMARK 465 GLY A 2
REMARK 465 ALA A 3
REMARK 465 GLY B 1
REMARK 465 GLY B 2
REMARK 465 ALA B 3
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 497 O HOH B 552 1.65
REMARK 500 O HOH B 457 O HOH B 659 1.70
REMARK 500 O HOH B 549 O HOH B 725 1.81
REMARK 500 O HOH A 407 O HOH A 532 1.86
REMARK 500 O HOH A 407 O HOH A 658 1.90
REMARK 500 O HOH A 603 O HOH A 720 1.90
REMARK 500 O HOH B 576 O HOH B 713 1.92
REMARK 500 O HOH A 452 O HOH A 721 1.92
REMARK 500 O HOH A 492 O HOH A 600 1.95
REMARK 500 NH2 ARG B 38 O HOH B 401 1.95
REMARK 500 O HOH B 414 O HOH B 558 1.96
REMARK 500 O HOH A 470 O HOH A 497 1.98
REMARK 500 OG SER B 68 O HOH B 402 2.03
REMARK 500 OG SER A 68 O HOH A 401 2.03
REMARK 500 O HOH B 702 O HOH B 757 2.03
REMARK 500 O HOH B 422 O HOH B 430 2.04
REMARK 500 O HOH B 673 O HOH B 705 2.04
REMARK 500 NH2 ARG B 38 O HOH B 403 2.05
REMARK 500 O HOH B 429 O HOH B 762 2.09
REMARK 500 NH2 ARG B 207 O HOH B 404 2.10
REMARK 500 O HOH A 532 O HOH A 600 2.11
REMARK 500 O HOH B 567 O HOH B 762 2.14
REMARK 500 O HOH A 689 O HOH A 775 2.14
REMARK 500 O HOH A 429 O HOH A 767 2.14
REMARK 500 O HOH B 433 O HOH B 455 2.15
REMARK 500 O HOH B 760 O HOH B 765 2.15
REMARK 500 O HOH A 430 O HOH B 726 2.15
REMARK 500 O HOH B 410 O HOH B 414 2.15
REMARK 500 O HOH A 711 O HOH A 778 2.16
REMARK 500 NH1 ARG B 34 O HOH B 405 2.16
REMARK 500 O HOH B 589 O HOH B 726 2.16
REMARK 500 O HOH A 661 O HOH A 710 2.17
REMARK 500 NE ARG A 73 O HOH A 402 2.18
REMARK 500 OG SER A 186 O HOH A 403 2.19
REMARK 500 O HOH B 618 O HOH B 644 2.19
REMARK 500 O HOH B 619 O HOH B 682 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 651 O HOH A 655 4545 1.72
REMARK 500 O HOH A 751 O HOH B 691 1655 2.04
REMARK 500 O HOH A 450 O HOH B 592 1655 2.11
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 9 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 73 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 78 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 201 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 259 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TYR B 65 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 73 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 201 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 231 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 231 NE - CZ - NH2 ANGL. DEV. = -3.0 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 THR A 66 -5.81 78.35
REMARK 500 SER A 133 -129.51 65.63
REMARK 500 SER A 133 -127.03 61.91
REMARK 500 THR A 156 58.11 38.16
REMARK 500 HIS A 187 -87.05 -123.49
REMARK 500 THR B 66 -8.60 78.20
REMARK 500 SER B 133 -123.25 68.79
REMARK 500 THR B 156 57.94 38.74
REMARK 500 HIS B 187 -86.74 -121.35
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 A 101 0.10 SIDE CHAIN
REMARK 500 ARG B 101 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
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 CA A 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 150 OE1
REMARK 620 2 TYR A 232 O 102.2
REMARK 620 3 ASP A 235 OD1 155.5 81.4
REMARK 620 4 HOH A 425 O 84.5 149.6 81.1
REMARK 620 5 HOH A 447 O 120.3 120.4 76.0 78.7
REMARK 620 6 HOH A 448 O 76.2 79.8 128.1 130.3 73.0
REMARK 620 7 HOH A 615 O 76.3 78.1 80.9 74.7 147.0 139.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 306 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 161 OD1
REMARK 620 2 ASP A 161 OD2 52.7
REMARK 620 3 THR A 163 O 85.0 101.3
REMARK 620 4 THR A 163 OG1 77.4 130.0 68.4
REMARK 620 5 HOH A 516 O 115.7 72.4 74.8 139.7
REMARK 620 6 HOH A 618 O 157.9 149.4 89.2 80.6 83.0
REMARK 620 7 HOH A 678 O 116.5 76.4 146.4 138.4 72.6 79.1
REMARK 620 8 HOH A 693 O 82.7 97.5 144.2 76.2 140.4 89.8 67.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 307 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 150 OE1
REMARK 620 2 TYR B 232 O 102.6
REMARK 620 3 ASP B 235 OD1 157.2 81.6
REMARK 620 4 HOH B 435 O 113.8 125.8 79.7
REMARK 620 5 HOH B 448 O 75.5 78.4 127.0 73.7
REMARK 620 6 HOH B 461 O 84.0 148.7 81.5 76.4 132.4
REMARK 620 7 HOH B 588 O 77.9 78.5 81.1 145.7 139.8 72.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 308 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 161 OD1
REMARK 620 2 ASP B 161 OD2 52.8
REMARK 620 3 THR B 163 O 83.3 101.7
REMARK 620 4 THR B 163 OG1 75.2 128.0 69.3
REMARK 620 5 HOH B 498 O 156.1 151.1 89.0 80.9
REMARK 620 6 HOH B 513 O 116.5 76.3 71.5 137.2 81.9
REMARK 620 7 HOH B 631 O 117.3 76.2 147.3 137.6 80.4 76.5
REMARK 620 8 HOH B 661 O 79.4 93.8 142.6 74.3 93.7 145.8 69.3
REMARK 620 N 1 2 3 4 5 6 7
DBREF 9KMF A 1 261 PDB 9KMF 9KMF 1 261
DBREF 9KMF B 1 261 PDB 9KMF 9KMF 1 261
SEQRES 1 A 261 GLY GLY ALA GLU ASN ASP TYR GLU ARG GLY PRO ASP PRO
SEQRES 2 A 261 THR SER SER SER ILE GLU ALA SER ARG GLY PRO TYR ALA
SEQRES 3 A 261 VAL SER THR LYS SER ILE SER ARG PHE ALA ALA ARG GLY
SEQRES 4 A 261 PHE GLY GLY GLY THR ILE HIS TYR PRO THR THR THR ALA
SEQRES 5 A 261 ASP GLY THR PHE GLY VAL VAL ALA VAL SER PRO GLY TYR
SEQRES 6 A 261 THR ALA SER GLU SER THR ILE ARG TRP LEU GLY PRO ARG
SEQRES 7 A 261 LEU ALA SER PHE GLY PHE VAL VAL ILE THR PHE ASP THR
SEQRES 8 A 261 ASN SER ARG TYR ASP GLN PRO ARG ALA ARG GLY THR GLN
SEQRES 9 A 261 LEU LEU ALA ALA ILE ASP GLN ALA ILE GLY ASP SER THR
SEQRES 10 A 261 VAL GLY SER ARG ILE ASP PRO SER ARG GLN ALA VAL VAL
SEQRES 11 A 261 GLY HIS SER MET GLY GLY GLY GLY THR LEU GLU ALA ALA
SEQRES 12 A 261 LYS THR ARG PRO SER ILE GLU ALA ALA VAL GLY LEU THR
SEQRES 13 A 261 PRO TRP ASN LEU ASP LYS THR TRP PRO GLU VAL GLU ALA
SEQRES 14 A 261 ALA ALA LEU GLN ILE GLY ALA GLN ASN ASP SER VAL ALA
SEQRES 15 A 261 PRO PRO ARG SER HIS ALA VAL PRO PHE TYR GLY SER LEU
SEQRES 16 A 261 THR ASN ALA GLU ARG ARG ALA TYR LEU GLU LEU ARG GLY
SEQRES 17 A 261 ALA SER HIS PHE ALA PRO ASN THR SER ASN THR THR ILE
SEQRES 18 A 261 ALA LYS TYR THR LEU ALA TRP LEU LYS ARG TYR VAL ASP
SEQRES 19 A 261 ASP ASP THR ARG TYR GLU GLN PHE LEU ALA PRO GLY PRO
SEQRES 20 A 261 SER THR GLY PHE GLY SER ALA VAL SER ASP TYR ARG ILE
SEQRES 21 A 261 GLN
SEQRES 1 B 261 GLY GLY ALA GLU ASN ASP TYR GLU ARG GLY PRO ASP PRO
SEQRES 2 B 261 THR SER SER SER ILE GLU ALA SER ARG GLY PRO TYR ALA
SEQRES 3 B 261 VAL SER THR LYS SER ILE SER ARG PHE ALA ALA ARG GLY
SEQRES 4 B 261 PHE GLY GLY GLY THR ILE HIS TYR PRO THR THR THR ALA
SEQRES 5 B 261 ASP GLY THR PHE GLY VAL VAL ALA VAL SER PRO GLY TYR
SEQRES 6 B 261 THR ALA SER GLU SER THR ILE ARG TRP LEU GLY PRO ARG
SEQRES 7 B 261 LEU ALA SER PHE GLY PHE VAL VAL ILE THR PHE ASP THR
SEQRES 8 B 261 ASN SER ARG TYR ASP GLN PRO ARG ALA ARG GLY THR GLN
SEQRES 9 B 261 LEU LEU ALA ALA ILE ASP GLN ALA ILE GLY ASP SER THR
SEQRES 10 B 261 VAL GLY SER ARG ILE ASP PRO SER ARG GLN ALA VAL VAL
SEQRES 11 B 261 GLY HIS SER MET GLY GLY GLY GLY THR LEU GLU ALA ALA
SEQRES 12 B 261 LYS THR ARG PRO SER ILE GLU ALA ALA VAL GLY LEU THR
SEQRES 13 B 261 PRO TRP ASN LEU ASP LYS THR TRP PRO GLU VAL GLU ALA
SEQRES 14 B 261 ALA ALA LEU GLN ILE GLY ALA GLN ASN ASP SER VAL ALA
SEQRES 15 B 261 PRO PRO ARG SER HIS ALA VAL PRO PHE TYR GLY SER LEU
SEQRES 16 B 261 THR ASN ALA GLU ARG ARG ALA TYR LEU GLU LEU ARG GLY
SEQRES 17 B 261 ALA SER HIS PHE ALA PRO ASN THR SER ASN THR THR ILE
SEQRES 18 B 261 ALA LYS TYR THR LEU ALA TRP LEU LYS ARG TYR VAL ASP
SEQRES 19 B 261 ASP ASP THR ARG TYR GLU GLN PHE LEU ALA PRO GLY PRO
SEQRES 20 B 261 SER THR GLY PHE GLY SER ALA VAL SER ASP TYR ARG ILE
SEQRES 21 B 261 GLN
HET TRS A 301 8
HET TRS A 302 8
HET GOL A 303 6
HET GOL A 304 6
HET CA A 305 1
HET CA A 306 1
HET GOL B 301 6
HET GOL B 302 6
HET TRS B 303 8
HET GOL B 304 6
HET EDO B 305 4
HET GOL B 306 6
HET CA B 307 1
HET CA B 308 1
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM GOL GLYCEROL
HETNAM CA CALCIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN TRS TRIS BUFFER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 TRS 3(C4 H12 N O3 1+)
FORMUL 5 GOL 6(C3 H8 O3)
FORMUL 7 CA 4(CA 2+)
FORMUL 13 EDO C2 H6 O2
FORMUL 17 HOH *839(H2 O)
HELIX 1 AA1 THR A 14 ALA A 20 1 7
HELIX 2 AA2 SER A 68 ARG A 73 5 6
HELIX 3 AA3 TRP A 74 SER A 81 1 8
HELIX 4 AA4 GLN A 97 ASP A 115 1 19
HELIX 5 AA5 VAL A 118 SER A 120 5 3
HELIX 6 AA6 SER A 133 ARG A 146 1 14
HELIX 7 AA7 HIS A 187 LEU A 195 1 9
HELIX 8 AA8 PHE A 212 THR A 216 5 5
HELIX 9 AA9 ASN A 218 ASP A 234 1 17
HELIX 10 AB1 ASP A 236 LEU A 243 5 8
HELIX 11 AB2 THR B 14 ALA B 20 1 7
HELIX 12 AB3 SER B 33 ALA B 37 5 5
HELIX 13 AB4 SER B 68 ARG B 73 5 6
HELIX 14 AB5 TRP B 74 SER B 81 1 8
HELIX 15 AB6 GLN B 97 ASP B 115 1 19
HELIX 16 AB7 VAL B 118 SER B 120 5 3
HELIX 17 AB8 SER B 133 ARG B 146 1 14
HELIX 18 AB9 HIS B 187 LEU B 195 1 9
HELIX 19 AC1 PHE B 212 THR B 216 5 5
HELIX 20 AC2 ASN B 218 ASP B 234 1 17
HELIX 21 AC3 ASP B 236 ARG B 238 5 3
HELIX 22 AC4 TYR B 239 ALA B 244 1 6
SHEET 1 AA1 9 VAL A 27 ILE A 32 0
SHEET 2 AA1 9 GLY A 43 PRO A 48 -1 O TYR A 47 N SER A 28
SHEET 3 AA1 9 VAL A 85 PHE A 89 -1 O VAL A 86 N HIS A 46
SHEET 4 AA1 9 PHE A 56 SER A 62 1 N VAL A 59 O VAL A 85
SHEET 5 AA1 9 ILE A 122 HIS A 132 1 O VAL A 130 N ALA A 60
SHEET 6 AA1 9 ALA A 151 LEU A 155 1 O LEU A 155 N GLY A 131
SHEET 7 AA1 9 ALA A 170 ALA A 176 1 O ILE A 174 N GLY A 154
SHEET 8 AA1 9 ARG A 201 LEU A 206 1 O LEU A 206 N GLY A 175
SHEET 9 AA1 9 VAL A 255 GLN A 261 -1 O ASP A 257 N GLU A 205
SHEET 1 AA2 9 VAL B 27 ILE B 32 0
SHEET 2 AA2 9 GLY B 43 PRO B 48 -1 O GLY B 43 N ILE B 32
SHEET 3 AA2 9 VAL B 85 PHE B 89 -1 O VAL B 86 N HIS B 46
SHEET 4 AA2 9 PHE B 56 SER B 62 1 N VAL B 59 O ILE B 87
SHEET 5 AA2 9 ILE B 122 HIS B 132 1 O ASP B 123 N PHE B 56
SHEET 6 AA2 9 ALA B 151 LEU B 155 1 O LEU B 155 N GLY B 131
SHEET 7 AA2 9 ALA B 170 ALA B 176 1 O ILE B 174 N GLY B 154
SHEET 8 AA2 9 ARG B 201 LEU B 206 1 O LEU B 206 N GLY B 175
SHEET 9 AA2 9 VAL B 255 GLN B 261 -1 O ASP B 257 N GLU B 205
LINK OE1 GLU A 150 CA CA A 305 1555 1555 2.36
LINK OD1 ASP A 161 CA CA A 306 1555 1555 2.42
LINK OD2 ASP A 161 CA CA A 306 1555 1555 2.48
LINK O THR A 163 CA CA A 306 1555 1555 2.42
LINK OG1 THR A 163 CA CA A 306 1555 1555 2.62
LINK O TYR A 232 CA CA A 305 1555 1555 2.37
LINK OD1 ASP A 235 CA CA A 305 1555 1555 2.37
LINK CA CA A 305 O HOH A 425 1555 1555 2.40
LINK CA CA A 305 O HOH A 447 1555 1555 2.36
LINK CA CA A 305 O HOH A 448 1555 1555 2.46
LINK CA CA A 305 O HOH A 615 1555 1555 2.49
LINK CA CA A 306 O HOH A 516 1555 1555 2.47
LINK CA CA A 306 O HOH A 618 1555 1555 2.43
LINK CA CA A 306 O HOH A 678 1555 1555 2.43
LINK CA CA A 306 O HOH A 693 1555 1555 2.40
LINK OE1 GLU B 150 CA CA B 307 1555 1555 2.36
LINK OD1 ASP B 161 CA CA B 308 1555 1555 2.46
LINK OD2 ASP B 161 CA CA B 308 1555 1555 2.46
LINK O THR B 163 CA CA B 308 1555 1555 2.38
LINK OG1 THR B 163 CA CA B 308 1555 1555 2.52
LINK O TYR B 232 CA CA B 307 1555 1555 2.34
LINK OD1 ASP B 235 CA CA B 307 1555 1555 2.37
LINK CA CA B 307 O HOH B 435 1555 1555 2.39
LINK CA CA B 307 O HOH B 448 1555 1555 2.46
LINK CA CA B 307 O HOH B 461 1555 1555 2.41
LINK CA CA B 307 O HOH B 588 1555 1555 2.48
LINK CA CA B 308 O HOH B 498 1555 1555 2.40
LINK CA CA B 308 O HOH B 513 1555 1555 2.43
LINK CA CA B 308 O HOH B 631 1555 1555 2.47
LINK CA CA B 308 O HOH B 661 1555 1555 2.40
CISPEP 1 ALA A 244 PRO A 245 0 10.29
CISPEP 2 ALA B 244 PRO B 245 0 9.13
CRYST1 43.670 71.748 168.896 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 0.022899 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013938 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005921 0.00000
TER 2028 GLN A 261
TER 4053 GLN B 261
MASTER 456 0 14 22 18 0 0 6 4805 2 102 42
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