HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 25-MAR-09 3GRD
TITLE CRYSTAL STRUCTURE OF NTF2-SUPERFAMILY PROTEIN WITH UNKNOWN FUNCTION
TITLE 2 (NP_977240.1) FROM BACILLUS CEREUS ATCC 10987 AT 1.25 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED NTF2-SUPERFAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS ATCC 10987;
SOURCE 3 ORGANISM_TAXID: 222523;
SOURCE 4 ATCC: 10987;
SOURCE 5 GENE: BCE_0917, NP_977240.1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS NP_977240.1, NTF2-SUPERFAMILY PROTEIN WITH UNKNOWN FUNCTION,
KEYWDS 2 STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,
KEYWDS 3 PROTEIN STRUCTURE INITIATIVE, PSI-2, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 4 01-FEB-23 3GRD 1 REMARK SEQADV LINK
REVDAT 3 24-JUL-19 3GRD 1 REMARK LINK
REVDAT 2 25-OCT-17 3GRD 1 REMARK
REVDAT 1 07-APR-09 3GRD 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF NTF2-SUPERFAMILY PROTEIN WITH UNKNOWN
JRNL TITL 2 FUNCTION (NP_977240.1) FROM BACILLUS CEREUS ATCC 10987 AT
JRNL TITL 3 1.25 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 81659
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) : 0.135
REMARK 3 R VALUE (WORKING SET) : 0.133
REMARK 3 FREE R VALUE : 0.167
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4091
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) : 1.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5289
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE SET COUNT : 274
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2089
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 521
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : -0.20000
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): 0.040
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.041
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.025
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.289
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2440 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1608 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3328 ; 1.540 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3955 ; 0.893 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 326 ; 6.203 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 115 ;40.722 ;25.304
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 429 ;11.095 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;13.478 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 336 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2922 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 511 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 478 ; 0.267 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1726 ; 0.191 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1166 ; 0.186 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1293 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 389 ; 0.164 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.055 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 17 ; 0.265 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 27 ; 0.224 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 51 ; 0.192 ; 0.200
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): 1514 ; 2.362 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 615 ; 1.648 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2450 ; 3.164 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 965 ; 4.543 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 878 ; 6.066 ;11.000
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): 4257 ; 1.991 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 542 ; 9.093 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3974 ; 4.436 ; 3.000
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 : 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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 3. ACETATE (ACT) AND SODIUM (NA) IONS FROM
REMARK 3 CRYSTALLIZATION CONDITION ARE MODELED.
REMARK 4
REMARK 4 3GRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052218.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.29
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91162,0.97862
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 MONOCHROMATOR (HORIZONTAL
REMARK 200 FOCUSING)
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81747
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.250
REMARK 200 RESOLUTION RANGE LOW (A) : 29.566
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.46900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX, SHELXD, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 33.8000% POLYETHYLENE GLYCOL 4000,
REMARK 280 0.2000M SODIUM ACETATE, 0.1M TRIS PH 8.29, NANODROP, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 20.54500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.89500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.57000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.89500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.54500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.57000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A DIMER
REMARK 300 AS A SIGNIFICANT OLIGOMERIZATION STATE.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 0
REMARK 465 GLY B 0
REMARK 465 MSE B 1
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 LYS A 68 CD CE NZ
REMARK 470 LYS A 80 CE NZ
REMARK 470 LYS B 3 CD CE NZ
REMARK 470 LYS B 68 CD CE NZ
REMARK 470 LYS B 132 CE NZ
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 NH2 ARG A 10 O HOH A 495 2.14
REMARK 500 OG SER A 70 O HOH A 459 2.16
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 76 CD GLU A 76 OE2 0.069
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 56 -80.87 -120.99
REMARK 500 ASP A 81 59.54 -93.04
REMARK 500 VAL B 56 -74.91 -122.08
REMARK 500 ASP B 81 57.51 -98.66
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 NA A 135 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 61 O
REMARK 620 2 TRP A 64 O 83.5
REMARK 620 3 HOH A 158 O 77.5 98.4
REMARK 620 4 HOH A 253 O 99.0 78.8 175.8
REMARK 620 5 HOH A 297 O 164.9 101.9 87.8 95.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 135 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 222 O
REMARK 620 2 VAL B 77 O 89.4
REMARK 620 3 LYS B 80 O 172.5 83.8
REMARK 620 4 HOH B 158 O 93.3 99.8 84.8
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 ACT A 134
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 135
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 134
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 135
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 390498 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 3GRD A 1 133 UNP Q73CZ7 Q73CZ7_BACC1 1 133
DBREF 3GRD B 1 133 UNP Q73CZ7 Q73CZ7_BACC1 1 133
SEQADV 3GRD GLY A 0 UNP Q73CZ7 EXPRESSION TAG
SEQADV 3GRD GLY B 0 UNP Q73CZ7 EXPRESSION TAG
SEQRES 1 A 134 GLY MSE PRO LYS ALA ASN LEU GLU ILE ILE ARG SER THR
SEQRES 2 A 134 TYR GLU GLY SER ALA SER SER ASN ALA LYS HIS LEU ALA
SEQRES 3 A 134 GLU ALA LEU SER GLU LYS VAL GLU TRP THR GLU ALA GLU
SEQRES 4 A 134 GLY PHE PRO TYR GLY GLY THR TYR ILE GLY VAL GLU ALA
SEQRES 5 A 134 ILE MSE GLU ASN VAL PHE SER ARG LEU GLY SER GLU TRP
SEQRES 6 A 134 ASN ASP TYR LYS ALA SER VAL ASN MSE TYR HIS GLU VAL
SEQRES 7 A 134 SER GLY LYS ASP VAL ILE ILE ALA GLU GLY MSE TYR SER
SEQRES 8 A 134 GLY VAL TYR LYS ASP THR GLY LYS SER PHE GLU ALA GLU
SEQRES 9 A 134 PHE VAL HIS VAL TRP GLN LEU GLU ASN GLY LYS ILE VAL
SEQRES 10 A 134 LYS PHE LYS GLN TYR VAL ASP SER HIS LEU VAL ARG GLU
SEQRES 11 A 134 ALA MSE LYS SER
SEQRES 1 B 134 GLY MSE PRO LYS ALA ASN LEU GLU ILE ILE ARG SER THR
SEQRES 2 B 134 TYR GLU GLY SER ALA SER SER ASN ALA LYS HIS LEU ALA
SEQRES 3 B 134 GLU ALA LEU SER GLU LYS VAL GLU TRP THR GLU ALA GLU
SEQRES 4 B 134 GLY PHE PRO TYR GLY GLY THR TYR ILE GLY VAL GLU ALA
SEQRES 5 B 134 ILE MSE GLU ASN VAL PHE SER ARG LEU GLY SER GLU TRP
SEQRES 6 B 134 ASN ASP TYR LYS ALA SER VAL ASN MSE TYR HIS GLU VAL
SEQRES 7 B 134 SER GLY LYS ASP VAL ILE ILE ALA GLU GLY MSE TYR SER
SEQRES 8 B 134 GLY VAL TYR LYS ASP THR GLY LYS SER PHE GLU ALA GLU
SEQRES 9 B 134 PHE VAL HIS VAL TRP GLN LEU GLU ASN GLY LYS ILE VAL
SEQRES 10 B 134 LYS PHE LYS GLN TYR VAL ASP SER HIS LEU VAL ARG GLU
SEQRES 11 B 134 ALA MSE LYS SER
MODRES 3GRD MSE A 1 MET SELENOMETHIONINE
MODRES 3GRD MSE A 53 MET SELENOMETHIONINE
MODRES 3GRD MSE A 73 MET SELENOMETHIONINE
MODRES 3GRD MSE A 88 MET SELENOMETHIONINE
MODRES 3GRD MSE A 131 MET SELENOMETHIONINE
MODRES 3GRD MSE B 53 MET SELENOMETHIONINE
MODRES 3GRD MSE B 73 MET SELENOMETHIONINE
MODRES 3GRD MSE B 88 MET SELENOMETHIONINE
MODRES 3GRD MSE B 131 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 53 8
HET MSE A 73 16
HET MSE A 88 24
HET MSE A 131 8
HET MSE B 53 8
HET MSE B 73 16
HET MSE B 88 24
HET MSE B 131 8
HET ACT A 134 8
HET NA A 135 1
HET ACT B 134 8
HET NA B 135 1
HETNAM MSE SELENOMETHIONINE
HETNAM ACT ACETATE ION
HETNAM NA SODIUM ION
FORMUL 1 MSE 9(C5 H11 N O2 SE)
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 4 NA 2(NA 1+)
FORMUL 7 HOH *521(H2 O)
HELIX 1 1 ALA A 4 SER A 11 1 8
HELIX 2 2 SER A 16 ALA A 27 1 12
HELIX 3 3 GLY A 48 VAL A 56 1 9
HELIX 4 4 VAL A 56 GLU A 63 1 8
HELIX 5 5 ASP A 123 MSE A 131 1 9
HELIX 6 6 ALA B 4 SER B 11 1 8
HELIX 7 7 SER B 16 ALA B 27 1 12
HELIX 8 8 GLY B 48 VAL B 56 1 9
HELIX 9 9 VAL B 56 GLU B 63 1 8
HELIX 10 10 ASP B 123 MSE B 131 1 9
SHEET 1 A 6 GLY A 44 ILE A 47 0
SHEET 2 A 6 LEU A 28 GLU A 36 -1 N TRP A 34 O TYR A 46
SHEET 3 A 6 LYS A 114 VAL A 122 1 O PHE A 118 N THR A 35
SHEET 4 A 6 SER A 99 GLU A 111 -1 N VAL A 105 O TYR A 121
SHEET 5 A 6 VAL A 82 TYR A 93 -1 N TYR A 89 O ALA A 102
SHEET 6 A 6 TRP A 64 GLU A 76 -1 N ASN A 72 O GLU A 86
SHEET 1 B 6 GLY B 44 ILE B 47 0
SHEET 2 B 6 LEU B 28 GLU B 36 -1 N TRP B 34 O TYR B 46
SHEET 3 B 6 LYS B 114 VAL B 122 1 O PHE B 118 N THR B 35
SHEET 4 B 6 SER B 99 GLU B 111 -1 N VAL B 105 O TYR B 121
SHEET 5 B 6 VAL B 82 TYR B 93 -1 N TYR B 89 O ALA B 102
SHEET 6 B 6 TRP B 64 GLU B 76 -1 N SER B 70 O MSE B 88
LINK C MSE A 1 N PRO A 2 1555 1555 1.33
LINK C ILE A 52 N MSE A 53 1555 1555 1.33
LINK C MSE A 53 N GLU A 54 1555 1555 1.34
LINK C AASN A 72 N AMSE A 73 1555 1555 1.33
LINK C BASN A 72 N BMSE A 73 1555 1555 1.33
LINK C AMSE A 73 N TYR A 74 1555 1555 1.31
LINK C BMSE A 73 N TYR A 74 1555 1555 1.34
LINK C GLY A 87 N AMSE A 88 1555 1555 1.33
LINK C GLY A 87 N BMSE A 88 1555 1555 1.32
LINK C GLY A 87 N CMSE A 88 1555 1555 1.33
LINK C AMSE A 88 N TYR A 89 1555 1555 1.32
LINK C BMSE A 88 N TYR A 89 1555 1555 1.32
LINK C CMSE A 88 N TYR A 89 1555 1555 1.33
LINK C ALA A 130 N MSE A 131 1555 1555 1.33
LINK C MSE A 131 N LYS A 132 1555 1555 1.32
LINK C ILE B 52 N MSE B 53 1555 1555 1.33
LINK C MSE B 53 N GLU B 54 1555 1555 1.32
LINK C AASN B 72 N AMSE B 73 1555 1555 1.32
LINK C BASN B 72 N BMSE B 73 1555 1555 1.34
LINK C AMSE B 73 N TYR B 74 1555 1555 1.33
LINK C BMSE B 73 N TYR B 74 1555 1555 1.35
LINK C GLY B 87 N AMSE B 88 1555 1555 1.33
LINK C GLY B 87 N BMSE B 88 1555 1555 1.32
LINK C GLY B 87 N CMSE B 88 1555 1555 1.33
LINK C AMSE B 88 N TYR B 89 1555 1555 1.33
LINK C BMSE B 88 N TYR B 89 1555 1555 1.32
LINK C CMSE B 88 N TYR B 89 1555 1555 1.34
LINK C ALA B 130 N MSE B 131 1555 1555 1.31
LINK C MSE B 131 N LYS B 132 1555 1555 1.33
LINK O GLY A 61 NA NA A 135 1555 1555 2.39
LINK O TRP A 64 NA NA A 135 1555 1555 2.36
LINK NA NA A 135 O HOH A 158 1555 1555 2.42
LINK NA NA A 135 O HOH A 253 1555 1555 2.47
LINK NA NA A 135 O HOH A 297 1555 1555 2.38
LINK O HOH A 222 NA NA B 135 1555 1555 2.34
LINK O VAL B 77 NA NA B 135 1555 1555 2.31
LINK O LYS B 80 NA NA B 135 1555 1555 2.39
LINK NA NA B 135 O HOH B 158 1555 1555 2.46
SITE 1 AC1 8 GLU A 36 VAL A 56 PHE A 57 TYR A 89
SITE 2 AC1 8 HIS A 106 PHE A 118 GLN A 120 HOH A 171
SITE 1 AC2 6 GLY A 61 TRP A 64 HOH A 158 HOH A 253
SITE 2 AC2 6 HOH A 297 HOH A 323
SITE 1 AC3 7 GLU B 36 VAL B 56 PHE B 57 TYR B 89
SITE 2 AC3 7 PHE B 118 GLN B 120 HOH B 203
SITE 1 AC4 6 GLU A 14 HOH A 182 HOH A 222 VAL B 77
SITE 2 AC4 6 LYS B 80 HOH B 158
CRYST1 41.090 47.140 151.790 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 0.024337 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021213 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006588 0.00000
HETATM 1 N MSE A 1 -16.395 24.813 -12.784 1.00 29.09 N
ANISOU 1 N MSE A 1 3861 3887 3306 30 -349 324 N
HETATM 2 CA MSE A 1 -16.370 23.946 -11.562 1.00 24.95 C
ANISOU 2 CA MSE A 1 2968 3614 2897 62 -288 12 C
HETATM 3 C MSE A 1 -14.966 23.917 -10.952 1.00 21.15 C
ANISOU 3 C MSE A 1 2556 3331 2146 10 -297 -38 C
HETATM 4 O MSE A 1 -13.986 23.654 -11.643 1.00 20.45 O
ANISOU 4 O MSE A 1 2709 3108 1952 -61 -255 5 O
HETATM 5 CB MSE A 1 -16.726 22.527 -11.947 1.00 25.90 C
ANISOU 5 CB MSE A 1 3002 3699 3139 -148 -351 131 C
HETATM 6 CG MSE A 1 -16.776 21.581 -10.810 1.00 25.16 C
ANISOU 6 CG MSE A 1 3336 3080 3142 -292 -374 -227 C
HETATM 7 SE MSE A 1 -17.106 19.860 -11.513 0.75 28.97 SE
ANISOU 7 SE MSE A 1 3647 3035 4324 -292 -1494 -67 SE
HETATM 8 CE MSE A 1 -18.809 20.255 -12.201 1.00 23.63 C
ANISOU 8 CE MSE A 1 3007 3271 2700 -187 -670 -278 C
(ATOM LINES ARE NOT SHOWN.)
END
