HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 23-OCT-06 2NN5
TITLE STRUCTURE OF CONSERVED PROTEIN OF UNKNOWN FUNCTION EF2215 FROM
TITLE 2 ENTEROCOCCUS FAECALIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN EF_2215;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS;
SOURCE 3 ORGANISM_TAXID: 226185;
SOURCE 4 STRAIN: V583;
SOURCE 5 GENE: EF_2215;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, APC29336, HYPOTHETICAL PROTEIN, PSI-2, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG,
KEYWDS 3 UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,R.WU,S.MOY,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (MCSG)
REVDAT 4 27-DEC-23 2NN5 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 2NN5 1 VERSN
REVDAT 2 24-FEB-09 2NN5 1 VERSN
REVDAT 1 21-NOV-06 2NN5 0
JRNL AUTH J.OSIPIUK,R.WU,S.MOY,A.JOACHIMIAK
JRNL TITL X-RAY CRYSTAL STRUCTURE OF CONSERVED HYPOTHETICAL PROTEIN
JRNL TITL 2 EF_2215 FROM ENTEROCOCCUS FAECALIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 31125
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) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.700
REMARK 3 FREE R VALUE TEST SET COUNT : 2392
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2041
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2000
REMARK 3 BIN FREE R VALUE SET COUNT : 181
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1423
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 231
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.39000
REMARK 3 B22 (A**2) : 0.60000
REMARK 3 B33 (A**2) : -0.21000
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): 0.085
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.043
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.434
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1640 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2269 ; 1.900 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 221 ; 5.730 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;35.509 ;25.172
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 299 ;15.293 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;13.803 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 248 ; 0.180 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1294 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 777 ; 0.243 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1143 ; 0.324 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 178 ; 0.220 ; 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): 60 ; 0.299 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 37 ; 0.248 ; 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): 974 ; 1.891 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1570 ; 2.661 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 773 ; 4.322 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 671 ; 5.223 ; 4.500
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): 1747 ; 3.677 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 233 ; 6.817 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1572 ; 4.462 ; 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2NN5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000040065.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : STRUCTURESTUDIO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31303
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 34.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 17.00
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.58200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.070
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, MLPHARE, DM, SOLVE, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 0.1 M MES
REMARK 280 BUFFER, 30% PEG 4000, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 29.11350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.51500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 43.38300
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.11350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.51500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 43.38300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.11350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 34.51500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 43.38300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.11350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 34.51500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 43.38300
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC
REMARK 300 UNIT WHICH CONSISTS OF 1 CHAIN. THE AUTHOR STATES
REMARK 300 THAT THE BIOLOGICAL UNIT OF THIS PROTEIN IS UNKNOWN.
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 343 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 348 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 363 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 384 LIES ON A SPECIAL POSITION.
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 -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
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 A 519 O HOH A 533 1.95
REMARK 500 O HOH A 358 O HOH A 517 2.06
REMARK 500 O HOH A 386 O HOH A 503 2.07
REMARK 500 O HOH A 374 O HOH A 519 2.07
REMARK 500 O HOH A 374 O HOH A 533 2.09
REMARK 500 O HOH A 469 O HOH A 525 2.11
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 470 O HOH A 525 8455 2.07
REMARK 500 O HOH A 358 O HOH A 535 7545 2.08
REMARK 500 O HOH A 414 O HOH A 517 7555 2.19
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 THR A 4 OG1 - CB - CG2 ANGL. DEV. = 13.9 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 GLN A 10 -8.03 65.29
REMARK 500 GLN A 10 -7.97 65.23
REMARK 500 LYS A 75 -58.93 -131.34
REMARK 500 LYS A 75 -55.34 -132.81
REMARK 500 ASP A 82 -133.57 59.48
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 MG A 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 140 OE2
REMARK 620 2 EDO A 302 O1 91.9
REMARK 620 3 HOH A 340 O 90.7 176.4
REMARK 620 4 HOH A 341 O 87.0 91.2 91.5
REMARK 620 5 HOH A 356 O 90.2 88.6 88.9 177.2
REMARK 620 6 HOH A 390 O 177.5 89.7 87.8 91.0 91.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 304 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 337 O
REMARK 620 2 HOH A 366 O 90.7
REMARK 620 3 HOH A 447 O 177.1 87.4
REMARK 620 4 HOH A 496 O 89.3 92.0 88.7
REMARK 620 5 HOH A 514 O 92.0 95.0 90.2 172.9
REMARK 620 6 HOH A 524 O 87.6 174.6 94.2 82.9 90.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC29336 RELATED DB: TARGETDB
DBREF 2NN5 A 1 160 UNP Q832L1 Q832L1_ENTFA 1 160
SEQADV 2NN5 MSE A -23 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 HIS A -22 UNP Q832L1 EXPRESSION TAG
SEQADV 2NN5 HIS A -21 UNP Q832L1 EXPRESSION TAG
SEQADV 2NN5 HIS A -20 UNP Q832L1 EXPRESSION TAG
SEQADV 2NN5 HIS A -19 UNP Q832L1 EXPRESSION TAG
SEQADV 2NN5 HIS A -18 UNP Q832L1 EXPRESSION TAG
SEQADV 2NN5 HIS A -17 UNP Q832L1 EXPRESSION TAG
SEQADV 2NN5 SER A -16 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 SER A -15 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 GLY A -14 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 VAL A -13 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 ASP A -12 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 LEU A -11 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 GLY A -10 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 THR A -9 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 GLU A -8 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 ASN A -7 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 LEU A -6 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 TYR A -5 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 PHE A -4 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 GLN A -3 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 SER A -2 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 ASN A -1 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 ALA A 0 UNP Q832L1 CLONING ARTIFACT
SEQADV 2NN5 MSE A 1 UNP Q832L1 MET 1 MODIFIED RESIDUE
SEQADV 2NN5 MSE A 66 UNP Q832L1 MET 66 MODIFIED RESIDUE
SEQRES 1 A 184 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 184 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MSE LYS
SEQRES 3 A 184 ASP THR PHE ARG LEU GLU ASN GLN THR ILE TYR PHE GLY
SEQRES 4 A 184 THR GLU ARG ALA ILE SER ALA SER PRO GLN THR ILE TRP
SEQRES 5 A 184 ARG TYR LEU THR GLU THR ASP LYS LEU LYS GLN TRP PHE
SEQRES 6 A 184 PRO GLU LEU GLU ILE GLY GLU LEU GLY VAL ASN GLY PHE
SEQRES 7 A 184 TRP ARG PHE ILE LEU PRO ASP PHE GLU GLU THR MSE PRO
SEQRES 8 A 184 PHE THR ASP TYR ALA GLU GLU LYS TYR LEU GLY VAL THR
SEQRES 9 A 184 TRP ASP THR GLY ILE ILE TYR PHE ASP LEU LYS GLU GLN
SEQRES 10 A 184 ALA PRO HIS GLN THR LEU LEU VAL PHE SER GLU SER LEU
SEQRES 11 A 184 PRO GLU ASN PHE THR THR PRO ARG HIS LYS ASP ILE ALA
SEQRES 12 A 184 GLY TRP SER ILE VAL LEU ASN ARG LEU LYS GLN VAL VAL
SEQRES 13 A 184 GLU THR PRO ASP ALA ALA PRO GLU LYS ILE ASP PHE PRO
SEQRES 14 A 184 GLN ILE GLU ASN HIS TYR LEU GLU LYS LEU THR ASN LEU
SEQRES 15 A 184 GLU ASN
MODRES 2NN5 MSE A 1 MET SELENOMETHIONINE
MODRES 2NN5 MSE A 66 MET SELENOMETHIONINE
HET MSE A 1 13
HET MSE A 66 13
HET MG A 303 1
HET MG A 304 1
HET EDO A 301 4
HET EDO A 302 4
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 2(C5 H11 N O2 SE)
FORMUL 2 MG 2(MG 2+)
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 6 HOH *231(H2 O)
HELIX 1 1 THR A -9 ALA A 0 1 10
HELIX 2 2 SER A 23 GLU A 33 1 11
HELIX 3 3 GLU A 33 PHE A 41 1 9
HELIX 4 4 PRO A 113 THR A 134 1 22
HELIX 5 5 ASP A 143 GLU A 159 1 17
SHEET 1 A 8 THR A 4 GLU A 8 0
SHEET 2 A 8 THR A 11 ILE A 20 -1 O TYR A 13 N ARG A 6
SHEET 3 A 8 GLN A 97 LEU A 106 -1 O LEU A 106 N ILE A 12
SHEET 4 A 8 GLY A 84 ALA A 94 -1 N LYS A 91 O LEU A 99
SHEET 5 A 8 TYR A 76 TRP A 81 -1 N LEU A 77 O PHE A 88
SHEET 6 A 8 PHE A 62 ALA A 72 -1 N ALA A 72 O TYR A 76
SHEET 7 A 8 PHE A 54 LEU A 59 -1 N TRP A 55 O MSE A 66
SHEET 8 A 8 LEU A 44 GLU A 48 -1 N GLU A 45 O ARG A 56
LINK C ALA A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C THR A 65 N MSE A 66 1555 1555 1.34
LINK C MSE A 66 N PRO A 67 1555 1555 1.33
LINK OE2 GLU A 140 MG MG A 303 1555 1555 2.02
LINK O1 EDO A 302 MG MG A 303 1555 1555 2.17
LINK MG MG A 303 O HOH A 340 1555 1555 2.05
LINK MG MG A 303 O HOH A 341 1555 1555 2.11
LINK MG MG A 303 O HOH A 356 1555 1555 2.02
LINK MG MG A 303 O HOH A 390 1555 1555 2.14
LINK MG MG A 304 O HOH A 337 1555 1555 2.00
LINK MG MG A 304 O HOH A 366 1555 1555 2.02
LINK MG MG A 304 O HOH A 447 1555 1555 2.07
LINK MG MG A 304 O HOH A 496 1555 1555 2.13
LINK MG MG A 304 O HOH A 514 1555 1555 2.09
LINK MG MG A 304 O HOH A 524 1555 1555 2.16
SITE 1 AC1 6 GLU A 140 EDO A 302 HOH A 340 HOH A 341
SITE 2 AC1 6 HOH A 356 HOH A 390
SITE 1 AC2 6 HOH A 337 HOH A 366 HOH A 447 HOH A 496
SITE 2 AC2 6 HOH A 514 HOH A 524
SITE 1 AC3 4 ARG A 114 HIS A 115 HOH A 319 HOH A 345
SITE 1 AC4 9 GLU A 8 GLN A 130 ALA A 137 GLU A 140
SITE 2 AC4 9 MG A 303 HOH A 341 HOH A 356 HOH A 390
SITE 3 AC4 9 HOH A 445
CRYST1 58.227 69.030 86.766 90.00 90.00 90.00 I 2 2 2 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 0.017174 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014486 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011525 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
