| content |
HEADER HYDROLASE 04-JAN-13 3ZI7
TITLE STRUCTURE OF FAE SOLVED BY SAD FROM DATA COLLECTED BY DIRECT DATA
TITLE 2 COLLECTION (DDC) USING THE GROB ROBOT GONIOMETER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE Y;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: XYLANASE Y, 1\,4-BETA-D-XYLAN XYLANOHYDROLASE Y, XYLY,
COMPND 5 FERULOYL ESTERASE DOMAIN;
COMPND 6 EC: 3.2.1.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_TAXID: 1094188;
SOURCE 4 STRAIN: YS;
SOURCE 5 ATCC: 1515;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET21A
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.W.BOWLER
REVDAT 3 03-JUL-13 3ZI7 1 JRNL
REVDAT 2 22-MAY-13 3ZI7 1 JRNL REMARK
REVDAT 1 01-MAY-13 3ZI7 0
JRNL AUTH J.L.FERRER,N.A.LARIVE,M.W.BOWLER,D.NURIZZO
JRNL TITL RECENT PROGRESS IN ROBOT-BASED SYSTEMS FOR CRYSTALLOGRAPHY
JRNL TITL 2 AND THEIR CONTRIBUTION TO DRUG DISCOVERY.
JRNL REF EXPERT OPIN.DRUG DISCOV. V. 8 835 2013
JRNL REFN ISSN 1746-0441
JRNL PMID 23656378
JRNL DOI 10.1517/17460441.2013.793666
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.13
REMARK 3 NUMBER OF REFLECTIONS : 34580
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) : 0.12440
REMARK 3 R VALUE (WORKING SET) : 0.12253
REMARK 3 FREE R VALUE : 0.15951
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1820
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) : 2.300
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.359
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2308
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.114
REMARK 3 BIN FREE R VALUE SET COUNT : 126
REMARK 3 BIN FREE R VALUE : 0.158
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4493
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 166
REMARK 3 SOLVENT ATOMS : 754
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.277
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26
REMARK 3 B22 (A**2) : -0.01
REMARK 3 B33 (A**2) : 0.27
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.186
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.148
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.282
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4809 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4244 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6552 ; 1.881 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9781 ; 1.815 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 569 ; 6.144 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 254 ;37.546 ;23.937
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 666 ;13.486 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;20.373 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 653 ; 0.152 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5585 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1264 ; 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 3ZI7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JAN-13.
REMARK 100 THE PDBE ID CODE IS EBI-55322.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : DIAMOND001
REMARK 200 OPTICS : GALLIUM221
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52409
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.30
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 7.6
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 28.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.9
REMARK 200 R MERGE FOR SHELL (I) : 0.08
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 15.20
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXCDE
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: DATA WERE COLLECTED DIRECTLY USING THE GROB ROBOT
REMARK 200 GONIOMETER
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 32.80450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.65850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.31950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.65850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.80450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.31950
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 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 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 MSE A 789
REMARK 465 ALA A 790
REMARK 465 SER A 791
REMARK 465 ASP A 792
REMARK 465 LYS A 793
REMARK 465 PHE A 794
REMARK 465 PRO A 795
REMARK 465 VAL A 796
REMARK 465 ALA A 797
REMARK 465 GLU A 798
REMARK 465 ASN A 799
REMARK 465 PRO A 800
REMARK 465 SER A 801
REMARK 465 SER A 802
REMARK 465 MSE B 789
REMARK 465 ALA B 790
REMARK 465 SER B 791
REMARK 465 ASP B 792
REMARK 465 LYS B 793
REMARK 465 PHE B 794
REMARK 465 PRO B 795
REMARK 465 VAL B 796
REMARK 465 ALA B 797
REMARK 465 GLU B 798
REMARK 465 ASN B 799
REMARK 465 PRO B 800
REMARK 465 SER B 801
REMARK 465 SER B 802
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 ND2 ASN A 858 O HOH A 3128 1.92
REMARK 500 ND1 HIS A 1081 O HOH A 3356 2.11
REMARK 500 OH TYR B 819 OE2 GLU B 892 2.19
REMARK 500 ND1 HIS B 1081 O HOH B 3350 1.77
REMARK 500 CD2 HIS B 1081 O HOH B 3345 2.18
REMARK 500 CD CD A 2089 O HOH A 3237 1.57
REMARK 500 CD CD B 2089 O HOH B 3232 1.59
REMARK 500 O HOH A 3018 O HOH A 3094 2.18
REMARK 500 O HOH A 3054 O HOH A 3061 2.00
REMARK 500 O HOH A 3090 O HOH B 3206 2.13
REMARK 500 O HOH A 3106 O HOH A 3107 2.02
REMARK 500 O HOH A 3182 O HOH A 3357 2.07
REMARK 500 O HOH A 3183 O HOH A 3360 2.12
REMARK 500 O HOH A 3212 O HOH A 3213 1.84
REMARK 500 O HOH A 3290 O HOH A 3380 1.95
REMARK 500 O HOH A 3309 O HOH A 3316 2.19
REMARK 500 O HOH A 3339 O HOH A 3340 2.20
REMARK 500 O HOH A 3346 O HOH A 3347 2.11
REMARK 500 O HOH B 3012 O HOH B 3210 2.05
REMARK 500 O HOH B 3023 O HOH B 3110 2.00
REMARK 500 O HOH B 3046 O HOH B 3149 2.04
REMARK 500 O HOH B 3056 O HOH B 3183 1.95
REMARK 500 O HOH B 3101 O HOH A 3210 2.19
REMARK 500 O HOH B 3101 O HOH B 3102 2.18
REMARK 500 O HOH B 3116 O HOH B 3245 2.13
REMARK 500 O HOH B 3116 O HOH B 3234 1.80
REMARK 500 O HOH B 3120 O HOH B 3121 1.81
REMARK 500 O HOH B 3136 O HOH B 3247 1.92
REMARK 500 O HOH B 3173 O HOH B 3314 2.19
REMARK 500 O HOH B 3204 O HOH A 3270 1.95
REMARK 500 O HOH B 3270 O HOH B 3271 2.13
REMARK 500 O HOH B 3278 O HOH B 3279 1.91
REMARK 500 O HOH B 3291 O HOH B 3294 2.18
REMARK 500 O HOH B 3301 O HOH B 3309 2.06
REMARK 500 O HOH B 3301 O HOH B 3306 1.99
REMARK 500 O HOH B 3340 O HOH B 3341 2.06
REMARK 500 O HOH B 3349 O HOH B 3350 2.14
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 ND2A ASN B 854 O HOH A 3215 4555 2.20
REMARK 500 CG B ASN B 854 O HOH A 3216 4555 1.76
REMARK 500 CG B ASN B 854 O HOH A 3215 4555 2.20
REMARK 500 OD1B ASN B 854 O HOH A 3216 4555 2.17
REMARK 500 OD1B ASN B 854 O HOH A 3215 4555 1.12
REMARK 500 ND2B ASN B 854 O HOH A 3216 4555 1.34
REMARK 500 O HOH A 3059 O HOH B 3281 3545 1.76
REMARK 500 O HOH A 3103 O HOH B 3289 3545 1.37
REMARK 500 O HOH A 3104 O HOH B 3291 3545 1.53
REMARK 500 O HOH B 3050 O HOH A 3174 2564 2.02
REMARK 500 O HOH B 3128 O HOH A 3218 4555 1.99
REMARK 500 O HOH B 3131 O HOH A 3213 4555 1.99
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 SER A 927 CA SER A 927 CB 0.091
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 MSE A 964 CG - SE - CE ANGL. DEV. = -14.2 DEGREES
REMARK 500 ARG A1006 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A1006 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG B 813 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 828 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B1006 NE - CZ - NH2 ANGL. DEV. = -5.2 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 VAL A 878 -52.48 -131.99
REMARK 500 SEP A 954 -119.94 61.53
REMARK 500 CYS A 967 28.62 -140.93
REMARK 500 THR A1040 146.48 170.09
REMARK 500 ASN A1047 20.11 -153.31
REMARK 500 VAL B 878 -52.95 -136.08
REMARK 500 THR B 931 -166.57 -107.60
REMARK 500 SEP B 954 -120.94 63.73
REMARK 500 THR B1040 145.70 171.24
REMARK 500 ASN B1047 19.73 -153.97
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 CD A2086 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 823 SG
REMARK 620 2 HIS A 886 ND1 95.9
REMARK 620 3 GLU B1017 OE1 106.6 87.2
REMARK 620 4 GLU B1017 OE2 154.0 99.9 54.1
REMARK 620 5 HOH A3178 O 125.3 89.0 128.0 75.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A2087 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A1079 OE1
REMARK 620 2 GLU A1079 OE2 55.8
REMARK 620 3 HIS A1083 ND1 90.1 86.4
REMARK 620 4 GLU A 894 OE2 121.5 170.5 84.5
REMARK 620 5 HIS A1085 NE2 143.6 88.4 94.7 94.9
REMARK 620 6 GLU A 894 OE1 75.0 129.5 82.4 46.5 141.4
REMARK 620 7 HIS A1076 ND1 93.5 97.7 175.6 91.5 84.0 96.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A2088 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A1007 OE2
REMARK 620 2 HIS B1082 NE2 93.9
REMARK 620 3 HIS B1084 NE2 114.2 101.3
REMARK 620 4 GLU A1007 OE1 55.6 149.5 91.4
REMARK 620 5 HOH A3290 O 99.2 95.0 141.3 91.9
REMARK 620 6 HOH A3380 O 138.5 109.8 94.5 96.6 46.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A2089 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A3233 O
REMARK 620 2 HOH A3353 O 82.1
REMARK 620 3 HIS A 947 NE2 92.1 174.1
REMARK 620 4 HIS A1080 NE2 102.0 93.2 88.9
REMARK 620 5 HOH A3238 O 154.1 91.0 93.8 103.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A2091 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 933 O
REMARK 620 2 HOH A3225 O 89.3
REMARK 620 3 HOH A3217 O 89.1 162.5
REMARK 620 4 HOH A3221 O 102.1 89.1 108.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B2086 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 823 SG
REMARK 620 2 HIS B 886 ND1 93.5
REMARK 620 3 GLU A1017 OE1 108.3 90.3
REMARK 620 4 GLU A1017 OE2 156.0 101.0 53.1
REMARK 620 5 HOH B3185 O 126.4 89.4 125.2 73.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B2087 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B1079 OE1
REMARK 620 2 GLU B 894 OE1 77.5
REMARK 620 3 GLU B 894 OE2 123.9 46.3
REMARK 620 4 HIS B1076 ND1 94.9 93.1 89.7
REMARK 620 5 GLU B1079 OE2 55.6 132.7 173.5 96.7
REMARK 620 6 HIS B1083 ND1 86.8 85.0 87.4 177.1 86.2
REMARK 620 7 HIS B1085 NE2 145.2 137.3 91.0 84.2 89.8 95.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B2088 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B3278 O
REMARK 620 2 HOH B3279 O 46.3
REMARK 620 3 HIS A1084 NE2 141.1 94.9
REMARK 620 4 GLU B1007 OE1 91.4 94.9 89.5
REMARK 620 5 GLU B1007 OE2 96.9 135.2 115.1 55.4
REMARK 620 6 HIS A1082 NE2 92.9 106.1 102.5 154.6 99.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B2089 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B3228 O
REMARK 620 2 HOH B3347 O 78.5
REMARK 620 3 HIS B 947 NE2 96.3 169.8
REMARK 620 4 HIS B1080 NE2 106.8 98.1 91.8
REMARK 620 5 HOH B3233 O 151.0 90.3 90.3 101.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B2091 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 926 O
REMARK 620 2 TYR B 929 O 77.5
REMARK 620 3 HOH B3212 O 79.5 86.7
REMARK 620 4 HOH B3216 O 156.8 115.4 82.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A2086
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A2087
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A2088
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A2089
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A2090
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B2086
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B2087
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B2088
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B2089
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B2090
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A2091
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B2091
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZI6 RELATED DB: PDB
REMARK 900 STRUCTURE OF THERMOLYSIN SOLVED BY SAD FROM DATA
REMARK 900 COLLECTED BY DIRECT DATA COLLECTION (DDC) USING THE
REMARK 900 GROB ROBOT GONIOMETER
DBREF 3ZI7 A 792 1077 UNP P51584 XYNY_CLOTM 792 1077
DBREF 3ZI7 B 792 1077 UNP P51584 XYNY_CLOTM 792 1077
SEQADV 3ZI7 MSE A 789 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 ALA A 790 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 SER A 791 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 GLU A 1017 UNP P51584 ASP 1017 CONFLICT
SEQADV 3ZI7 ASP A 1018 UNP P51584 HIS 1018 CONFLICT
SEQADV 3ZI7 LEU A 1078 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 GLU A 1079 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 HIS A 1080 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 HIS A 1081 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 HIS A 1082 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 HIS A 1083 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 HIS A 1084 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 HIS A 1085 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 MSE B 789 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 ALA B 790 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 SER B 791 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 GLU B 1017 UNP P51584 ASP 1017 CONFLICT
SEQADV 3ZI7 ASP B 1018 UNP P51584 HIS 1018 CONFLICT
SEQADV 3ZI7 LEU B 1078 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 GLU B 1079 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 HIS B 1080 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 HIS B 1081 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 HIS B 1082 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 HIS B 1083 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 HIS B 1084 UNP P51584 EXPRESSION TAG
SEQADV 3ZI7 HIS B 1085 UNP P51584 EXPRESSION TAG
SEQRES 1 A 297 MSE ALA SER ASP LYS PHE PRO VAL ALA GLU ASN PRO SER
SEQRES 2 A 297 SER SER PHE LYS TYR GLU SER ALA VAL GLN TYR ARG PRO
SEQRES 3 A 297 ALA PRO ASP SER TYR LEU ASN PRO CYS PRO GLN ALA GLY
SEQRES 4 A 297 ARG ILE VAL LYS GLU THR TYR THR GLY ILE ASN GLY THR
SEQRES 5 A 297 LYS SER LEU ASN VAL TYR LEU PRO TYR GLY TYR ASP PRO
SEQRES 6 A 297 ASN LYS LYS TYR ASN ILE PHE TYR LEU MSE HIS GLY GLY
SEQRES 7 A 297 GLY GLU ASN GLU ASN THR ILE PHE SER ASN ASP VAL LYS
SEQRES 8 A 297 LEU GLN ASN ILE LEU ASP HIS ALA ILE MSE ASN GLY GLU
SEQRES 9 A 297 LEU GLU PRO LEU ILE VAL VAL THR PRO THR PHE ASN GLY
SEQRES 10 A 297 GLY ASN CYS THR ALA GLN ASN PHE TYR GLN GLU PHE ARG
SEQRES 11 A 297 GLN ASN VAL ILE PRO PHE VAL GLU SER LYS TYR SER THR
SEQRES 12 A 297 TYR ALA GLU SER THR THR PRO GLN GLY ILE ALA ALA SER
SEQRES 13 A 297 ARG MSE HIS ARG GLY PHE GLY GLY PHE SEP MSE GLY GLY
SEQRES 14 A 297 LEU THR THR TRP TYR VAL MSE VAL ASN CYS LEU ASP TYR
SEQRES 15 A 297 VAL ALA TYR PHE MSE PRO LEU SER GLY ASP TYR TRP TYR
SEQRES 16 A 297 GLY ASN SER PRO GLN ASP LYS ALA ASN SER ILE ALA GLU
SEQRES 17 A 297 ALA ILE ASN ARG SER GLY LEU SER LYS ARG GLU TYR PHE
SEQRES 18 A 297 VAL PHE ALA ALA THR GLY SER GLU ASP ILE ALA TYR ALA
SEQRES 19 A 297 ASN MSE ASN PRO GLN ILE GLU ALA MSE LYS ALA LEU PRO
SEQRES 20 A 297 HIS PHE ASP TYR THR SER ASP PHE SER LYS GLY ASN PHE
SEQRES 21 A 297 TYR PHE LEU VAL ALA PRO GLY ALA THR HIS TRP TRP GLY
SEQRES 22 A 297 TYR VAL ARG HIS TYR ILE TYR ASP ALA LEU PRO TYR PHE
SEQRES 23 A 297 PHE HIS GLU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 297 MSE ALA SER ASP LYS PHE PRO VAL ALA GLU ASN PRO SER
SEQRES 2 B 297 SER SER PHE LYS TYR GLU SER ALA VAL GLN TYR ARG PRO
SEQRES 3 B 297 ALA PRO ASP SER TYR LEU ASN PRO CYS PRO GLN ALA GLY
SEQRES 4 B 297 ARG ILE VAL LYS GLU THR TYR THR GLY ILE ASN GLY THR
SEQRES 5 B 297 LYS SER LEU ASN VAL TYR LEU PRO TYR GLY TYR ASP PRO
SEQRES 6 B 297 ASN LYS LYS TYR ASN ILE PHE TYR LEU MSE HIS GLY GLY
SEQRES 7 B 297 GLY GLU ASN GLU ASN THR ILE PHE SER ASN ASP VAL LYS
SEQRES 8 B 297 LEU GLN ASN ILE LEU ASP HIS ALA ILE MSE ASN GLY GLU
SEQRES 9 B 297 LEU GLU PRO LEU ILE VAL VAL THR PRO THR PHE ASN GLY
SEQRES 10 B 297 GLY ASN CYS THR ALA GLN ASN PHE TYR GLN GLU PHE ARG
SEQRES 11 B 297 GLN ASN VAL ILE PRO PHE VAL GLU SER LYS TYR SER THR
SEQRES 12 B 297 TYR ALA GLU SER THR THR PRO GLN GLY ILE ALA ALA SER
SEQRES 13 B 297 ARG MSE HIS ARG GLY PHE GLY GLY PHE SEP MSE GLY GLY
SEQRES 14 B 297 LEU THR THR TRP TYR VAL MSE VAL ASN CYS LEU ASP TYR
SEQRES 15 B 297 VAL ALA TYR PHE MSE PRO LEU SER GLY ASP TYR TRP TYR
SEQRES 16 B 297 GLY ASN SER PRO GLN ASP LYS ALA ASN SER ILE ALA GLU
SEQRES 17 B 297 ALA ILE ASN ARG SER GLY LEU SER LYS ARG GLU TYR PHE
SEQRES 18 B 297 VAL PHE ALA ALA THR GLY SER GLU ASP ILE ALA TYR ALA
SEQRES 19 B 297 ASN MSE ASN PRO GLN ILE GLU ALA MSE LYS ALA LEU PRO
SEQRES 20 B 297 HIS PHE ASP TYR THR SER ASP PHE SER LYS GLY ASN PHE
SEQRES 21 B 297 TYR PHE LEU VAL ALA PRO GLY ALA THR HIS TRP TRP GLY
SEQRES 22 B 297 TYR VAL ARG HIS TYR ILE TYR ASP ALA LEU PRO TYR PHE
SEQRES 23 B 297 PHE HIS GLU LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 3ZI7 MSE A 863 MET SELENOMETHIONINE
MODRES 3ZI7 MSE A 889 MET SELENOMETHIONINE
MODRES 3ZI7 MSE A 946 MET SELENOMETHIONINE
MODRES 3ZI7 SEP A 954 SER PHOSPHOSERINE
MODRES 3ZI7 MSE A 955 MET SELENOMETHIONINE
MODRES 3ZI7 MSE A 964 MET SELENOMETHIONINE
MODRES 3ZI7 MSE A 975 MET SELENOMETHIONINE
MODRES 3ZI7 MSE A 1024 MET SELENOMETHIONINE
MODRES 3ZI7 MSE A 1031 MET SELENOMETHIONINE
MODRES 3ZI7 MSE B 863 MET SELENOMETHIONINE
MODRES 3ZI7 MSE B 889 MET SELENOMETHIONINE
MODRES 3ZI7 MSE B 946 MET SELENOMETHIONINE
MODRES 3ZI7 SEP B 954 SER PHOSPHOSERINE
MODRES 3ZI7 MSE B 955 MET SELENOMETHIONINE
MODRES 3ZI7 MSE B 964 MET SELENOMETHIONINE
MODRES 3ZI7 MSE B 975 MET SELENOMETHIONINE
MODRES 3ZI7 MSE B 1024 MET SELENOMETHIONINE
MODRES 3ZI7 MSE B 1031 MET SELENOMETHIONINE
HET MSE A 863 8
HET MSE A 889 8
HET MSE A 946 8
HET SEP A 954 10
HET MSE A 955 11
HET MSE A 964 8
HET MSE A 975 8
HET MSE A1024 8
HET MSE A1031 8
HET CD A2086 1
HET CD A2087 1
HET CD A2088 1
HET CD A2089 1
HET CD A2090 1
HET MSE B 863 8
HET MSE B 889 8
HET MSE B 946 8
HET SEP B 954 10
HET MSE B 955 11
HET MSE B 964 8
HET MSE B 975 8
HET MSE B1024 8
HET MSE B1031 8
HET CD B2086 1
HET CD B2087 1
HET CD B2088 1
HET CD B2089 1
HET CD B2090 1
HET CD A2091 1
HET CD B2091 1
HETNAM CD CADMIUM ION
HETNAM SEP PHOSPHOSERINE
HETNAM MSE SELENOMETHIONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 3 CD 12(CD 2+)
FORMUL 4 SEP 2(C3 H8 N O6 P)
FORMUL 5 MSE 16(C5 H11 N O2 SE)
FORMUL 6 HOH *754(H2 O)
HELIX 1 1 PRO A 816 ASN A 821 5 6
HELIX 2 2 LYS A 879 ASN A 890 1 12
HELIX 3 3 ASN A 912 ASN A 920 1 9
HELIX 4 4 ASN A 920 TYR A 929 1 10
HELIX 5 5 THR A 937 ALA A 943 1 7
HELIX 6 6 SER A 944 MSE A 946 5 3
HELIX 7 7 SEP A 954 LEU A 968 1 15
HELIX 8 8 SER A 986 GLY A 1002 1 17
HELIX 9 9 ILE A 1019 ALA A 1033 1 15
HELIX 10 10 TRP A 1059 LEU A 1071 1 13
HELIX 11 11 PRO A 1072 PHE A 1074 5 3
HELIX 12 12 PRO B 816 ASN B 821 5 6
HELIX 13 13 LYS B 879 ASN B 890 1 12
HELIX 14 14 ASN B 912 ASN B 920 1 9
HELIX 15 15 ASN B 920 TYR B 929 1 10
HELIX 16 16 THR B 937 ALA B 943 1 7
HELIX 17 17 SER B 944 MSE B 946 5 3
HELIX 18 18 SEP B 954 LEU B 968 1 15
HELIX 19 19 SER B 986 GLY B 1002 1 17
HELIX 20 20 ALA B 1020 LEU B 1034 1 15
HELIX 21 21 TRP B 1059 LEU B 1071 1 13
HELIX 22 22 PRO B 1072 PHE B 1074 5 3
SHEET 1 AA 8 ARG A 828 GLY A 836 0
SHEET 2 AA 8 GLY A 839 LEU A 847 -1 O GLY A 839 N GLY A 836
SHEET 3 AA 8 LEU A 896 THR A 900 -1 O VAL A 898 N TYR A 846
SHEET 4 AA 8 ASN A 858 MSE A 863 1 O ASN A 858 N ILE A 897
SHEET 5 AA 8 ARG A 948 PHE A 953 1 O GLY A 949 N TYR A 861
SHEET 6 AA 8 TYR A 973 LEU A 977 1 O TYR A 973 N PHE A 950
SHEET 7 AA 8 PHE A1009 GLY A1015 1 O PHE A1009 N PHE A 974
SHEET 8 AA 8 PHE A1048 ALA A1053 1 O TYR A1049 N ALA A1012
SHEET 1 BA 8 ARG B 828 GLY B 836 0
SHEET 2 BA 8 GLY B 839 LEU B 847 -1 O GLY B 839 N GLY B 836
SHEET 3 BA 8 LEU B 896 THR B 900 -1 O VAL B 898 N TYR B 846
SHEET 4 BA 8 ASN B 858 MSE B 863 1 O ASN B 858 N ILE B 897
SHEET 5 BA 8 ARG B 948 PHE B 953 1 O GLY B 949 N TYR B 861
SHEET 6 BA 8 TYR B 973 LEU B 977 1 O TYR B 973 N PHE B 950
SHEET 7 BA 8 PHE B1009 GLY B1015 1 O PHE B1009 N PHE B 974
SHEET 8 BA 8 PHE B1048 ALA B1053 1 O TYR B1049 N ALA B1012
LINK N MSE A 863 C LEU A 862 1555 1555 1.34
LINK C MSE A 863 N HIS A 864 1555 1555 1.32
LINK N MSE A 889 C ILE A 888 1555 1555 1.32
LINK C MSE A 889 N ASN A 890 1555 1555 1.34
LINK N MSE A 946 C ARG A 945 1555 1555 1.33
LINK C MSE A 946 N HIS A 947 1555 1555 1.33
LINK N SEP A 954 C PHE A 953 1555 1555 1.34
LINK C SEP A 954 N MSE A 955 1555 1555 1.34
LINK C MSE A 955 N GLY A 956 1555 1555 1.34
LINK N MSE A 964 C VAL A 963 1555 1555 1.33
LINK C MSE A 964 N VAL A 965 1555 1555 1.31
LINK N MSE A 975 C PHE A 974 1555 1555 1.31
LINK C MSE A 975 N PRO A 976 1555 1555 1.36
LINK N MSE A1024 C ASN A1023 1555 1555 1.32
LINK C MSE A1024 N ASN A1025 1555 1555 1.30
LINK N MSE A1031 C ALA A1030 1555 1555 1.33
LINK C MSE A1031 N LYS A1032 1555 1555 1.31
LINK CD CD A2086 SG CYS A 823 1555 1555 2.53
LINK CD CD A2086 ND1 HIS A 886 1555 1555 2.33
LINK CD CD A2086 OE1 GLU B1017 1555 3545 2.38
LINK CD CD A2086 OE2 GLU B1017 1555 3545 2.48
LINK CD CD A2086 O HOH A3178 1555 1555 2.20
LINK CD CD A2087 ND1 HIS A1076 1555 1555 2.46
LINK CD CD A2087 OE1 GLU A 894 1555 1555 3.10
LINK CD CD A2087 OE2 GLU A 894 1555 1555 2.16
LINK CD CD A2087 OE1 GLU A1079 1555 1555 2.26
LINK CD CD A2087 NE2 HIS A1085 1555 1555 2.28
LINK CD CD A2087 OE2 GLU A1079 1555 1555 2.41
LINK CD CD A2087 ND1 HIS A1083 1555 1555 2.29
LINK CD CD A2088 OE1 GLU A1007 1555 1555 2.54
LINK CD CD A2088 NE2 HIS B1084 1555 1455 2.27
LINK CD CD A2088 NE2 HIS B1082 1555 1455 2.32
LINK CD CD A2088 OE2 GLU A1007 1555 1555 2.13
LINK CD CD A2088 O HOH A3290 1555 1555 2.49
LINK CD CD A2088 O HOH A3380 1555 1555 2.42
LINK CD CD A2089 NE2 HIS A 947 1555 1555 2.39
LINK CD CD A2089 O HOH A3353 1555 1555 2.68
LINK CD CD A2089 O HOH A3238 1555 1555 2.37
LINK CD CD A2089 O HOH A3233 1555 1555 2.37
LINK CD CD A2089 NE2 HIS A1080 1555 1555 2.11
LINK CD CD A2090 O HOH A3382 1555 1555 2.45
LINK CD CD A2091 O HOH A3225 1555 1555 2.66
LINK CD CD A2091 O HOH A3221 1555 1555 2.60
LINK CD CD A2091 O HOH A3217 1555 1555 2.55
LINK CD CD A2091 O ALA A 933 1555 1555 2.51
LINK N MSE B 863 C LEU B 862 1555 1555 1.32
LINK C MSE B 863 N HIS B 864 1555 1555 1.32
LINK N MSE B 889 C ILE B 888 1555 1555 1.34
LINK C MSE B 889 N ASN B 890 1555 1555 1.32
LINK C MSE B 946 N HIS B 947 1555 1555 1.30
LINK N MSE B 946 C ARG B 945 1555 1555 1.32
LINK C SEP B 954 N MSE B 955 1555 1555 1.34
LINK N SEP B 954 C PHE B 953 1555 1555 1.32
LINK C MSE B 955 N GLY B 956 1555 1555 1.34
LINK N MSE B 964 C VAL B 963 1555 1555 1.33
LINK C MSE B 964 N VAL B 965 1555 1555 1.33
LINK C MSE B 975 N PRO B 976 1555 1555 1.37
LINK N MSE B 975 C PHE B 974 1555 1555 1.32
LINK N MSE B1024 C ASN B1023 1555 1555 1.34
LINK C MSE B1024 N ASN B1025 1555 1555 1.32
LINK N MSE B1031 C ALA B1030 1555 1555 1.32
LINK C MSE B1031 N LYS B1032 1555 1555 1.32
LINK CD CD B2086 O HOH B3185 1555 1555 2.21
LINK CD CD B2086 OE2 GLU A1017 1555 2564 2.48
LINK CD CD B2086 OE1 GLU A1017 1555 2564 2.47
LINK CD CD B2086 ND1 HIS B 886 1555 1555 2.34
LINK CD CD B2086 SG CYS B 823 1555 1555 2.46
LINK CD CD B2087 NE2 HIS B1085 1555 1555 2.31
LINK CD CD B2087 ND1 HIS B1083 1555 1555 2.37
LINK CD CD B2087 OE2 GLU B1079 1555 1555 2.39
LINK CD CD B2087 ND1 HIS B1076 1555 1555 2.47
LINK CD CD B2087 OE2 GLU B 894 1555 1555 2.32
LINK CD CD B2087 OE1 GLU B 894 1555 1555 2.94
LINK CD CD B2087 OE1 GLU B1079 1555 1555 2.15
LINK CD CD B2088 NE2 HIS A1082 1555 1655 2.24
LINK CD CD B2088 OE2 GLU B1007 1555 1555 2.17
LINK CD CD B2088 OE1 GLU B1007 1555 1555 2.48
LINK CD CD B2088 NE2 HIS A1084 1555 1655 2.22
LINK CD CD B2088 O HOH B3279 1555 1555 2.37
LINK CD CD B2088 O HOH B3278 1555 1555 2.48
LINK CD CD B2089 O HOH B3233 1555 1555 2.23
LINK CD CD B2089 NE2 HIS B1080 1555 1555 2.07
LINK CD CD B2089 NE2 HIS B 947 1555 1555 2.43
LINK CD CD B2089 O HOH B3347 1555 1555 2.64
LINK CD CD B2089 O HOH B3228 1555 1555 2.39
LINK CD CD B2090 O HOH B3367 1555 1555 2.97
LINK CD CD B2091 O HOH B3216 1555 1555 2.63
LINK CD CD B2091 O HOH B3212 1555 1555 2.56
LINK CD CD B2091 O TYR B 929 1555 1555 2.56
LINK CD CD B2091 O GLU B 926 1555 1555 2.52
SITE 1 AC1 5 CYS A 823 HIS A 886 MSE A 889 HOH A3178
SITE 2 AC1 5 GLU B1017
SITE 1 AC2 5 GLU A 894 HIS A1076 GLU A1079 HIS A1083
SITE 2 AC2 5 HIS A1085
SITE 1 AC3 5 GLU A1007 HOH A3290 HOH A3380 HIS B1082
SITE 2 AC3 5 HIS B1084
SITE 1 AC4 6 HIS A 947 HIS A1080 HOH A3233 HOH A3237
SITE 2 AC4 6 HOH A3238 HOH A3353
SITE 1 AC5 2 HIS A1081 HOH A3382
SITE 1 AC6 5 GLU A1017 CYS B 823 HIS B 886 MSE B 889
SITE 2 AC6 5 HOH B3185
SITE 1 AC7 5 GLU B 894 HIS B1076 GLU B1079 HIS B1083
SITE 2 AC7 5 HIS B1085
SITE 1 AC8 5 HIS A1082 HIS A1084 GLU B1007 HOH B3278
SITE 2 AC8 5 HOH B3279
SITE 1 AC9 6 HIS B 947 HIS B1080 HOH B3228 HOH B3232
SITE 2 AC9 6 HOH B3233 HOH B3347
SITE 1 BC1 2 HIS B1081 HOH B3367
SITE 1 BC2 4 ALA A 933 HOH A3217 HOH A3221 HOH A3225
SITE 1 BC3 4 GLU B 926 TYR B 929 HOH B3212 HOH B3216
CRYST1 65.609 108.639 113.317 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 0.015242 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009205 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008825 0.00000
TER 2323 HIS A1085
TER 4649 HIS B1085
MASTER 584 0 30 22 16 0 20 6 5413 2 250 46
END |