HEADER HYDROLASE 31-OCT-05 2EVR
TITLE CRYSTAL STRUCTURE OF A PUTATIVE GAMMA-D-GLUTAMYL-L-DIAMINO ACID
TITLE 2 ENDOPEPTIDASE (NPUN_R0659) FROM NOSTOC PUNCTIFORME PCC 73102 AT 1.60
TITLE 3 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COG0791: CELL WALL-ASSOCIATED HYDROLASES (INVASION-
COMPND 3 ASSOCIATED PROTEINS);
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC PUNCTIFORME;
SOURCE 3 ORGANISM_TAXID: 63737;
SOURCE 4 STRAIN: PCC 73102;
SOURCE 5 GENE: 53686717;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PUTATIVE GAMMA-D-GLUTAMYL-L-DIAMINO ACID ENDOPEPTIDASE, STRUCTURAL
KEYWDS 2 GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, PSI-2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 6 25-JAN-23 2EVR 1 REMARK SEQADV LINK
REVDAT 5 13-JUL-11 2EVR 1 VERSN
REVDAT 4 28-JUL-10 2EVR 1 HEADER TITLE KEYWDS
REVDAT 3 10-MAR-09 2EVR 1 JRNL
REVDAT 2 24-FEB-09 2EVR 1 VERSN
REVDAT 1 22-NOV-05 2EVR 0
JRNL AUTH Q.XU,S.SUDEK,D.MCMULLAN,M.D.MILLER,B.GEIERSTANGER,D.H.JONES,
JRNL AUTH 2 S.S.KRISHNA,G.SPRAGGON,B.BURSALAY,P.ABDUBEK,C.ACOSTA,
JRNL AUTH 3 E.AMBING,T.ASTAKHOVA,H.L.AXELROD,D.CARLTON,J.CARUTHERS,
JRNL AUTH 4 H.J.CHIU,T.CLAYTON,M.C.DELLER,L.DUAN,Y.ELIAS,M.A.ELSLIGER,
JRNL AUTH 5 J.FEUERHELM,S.K.GRZECHNIK,J.HALE,G.WON HAN,J.HAUGEN,
JRNL AUTH 6 L.JAROSZEWSKI,K.K.JIN,H.E.KLOCK,M.W.KNUTH,P.KOZBIAL,A.KUMAR,
JRNL AUTH 7 D.MARCIANO,A.T.MORSE,E.NIGOGHOSSIAN,L.OKACH,S.OOMMACHEN,
JRNL AUTH 8 J.PAULSEN,R.REYES,C.L.RIFE,C.V.TROUT,H.VAN DEN BEDEM,
JRNL AUTH 9 D.WEEKES,A.WHITE,G.WOLF,C.ZUBIETA,K.O.HODGSON,J.WOOLEY,
JRNL AUTH10 A.M.DEACON,A.GODZIK,S.A.LESLEY,I.A.WILSON
JRNL TITL STRUCTURAL BASIS OF MUREIN PEPTIDE SPECIFICITY OF A
JRNL TITL 2 GAMMA-D-GLUTAMYL-L-DIAMINO ACID ENDOPEPTIDASE.
JRNL REF STRUCTURE V. 17 303 2009
JRNL REFN ISSN 0969-2126
JRNL PMID 19217401
JRNL DOI 10.1016/J.STR.2008.12.008
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 48970
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2624
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3466
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 212
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1714
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.12000
REMARK 3 B22 (A**2) : -0.12000
REMARK 3 B33 (A**2) : 0.24000
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): 0.060
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.060
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.042
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.435
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1905 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1661 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2614 ; 1.508 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3887 ; 0.818 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 259 ; 5.766 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 93 ;35.234 ;24.839
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 298 ;11.752 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;15.317 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 281 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2222 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 402 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 336 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1691 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 957 ; 0.189 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1192 ; 0.090 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 214 ; 0.182 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.231 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 18 ; 0.267 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 52 ; 0.241 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 29 ; 0.189 ; 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): 1171 ; 1.817 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 482 ; 0.498 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1891 ; 3.153 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 765 ; 4.409 ; 7.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 706 ; 6.192 ; 7.000
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): 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 13 A 90
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5811 20.4375 46.6320
REMARK 3 T TENSOR
REMARK 3 T11: 0.0207 T22: -0.0500
REMARK 3 T33: -0.0518 T12: 0.0229
REMARK 3 T13: -0.0212 T23: -0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 2.5040 L22: 0.4152
REMARK 3 L33: 1.0822 L12: -0.0337
REMARK 3 L13: 0.6070 L23: 0.0957
REMARK 3 S TENSOR
REMARK 3 S11: -0.0533 S12: -0.2022 S13: 0.1257
REMARK 3 S21: 0.2303 S22: 0.0386 S23: -0.0724
REMARK 3 S31: -0.0269 S32: -0.0029 S33: 0.0147
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 91 A 234
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5041 -0.2780 36.4309
REMARK 3 T TENSOR
REMARK 3 T11: 0.0018 T22: -0.0526
REMARK 3 T33: -0.0435 T12: 0.0081
REMARK 3 T13: -0.0304 T23: -0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 1.4912 L22: 1.8081
REMARK 3 L33: 0.6580 L12: -0.1298
REMARK 3 L13: 0.1426 L23: 0.5367
REMARK 3 S TENSOR
REMARK 3 S11: 0.0395 S12: -0.0469 S13: -0.1182
REMARK 3 S21: 0.2586 S22: 0.0300 S23: -0.1091
REMARK 3 S31: 0.1542 S32: 0.0093 S33: -0.0695
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 0.7
REMARK 3 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 3. TENTATIVE MODELS WERE BUILT FOR THE FOLLOWING
REMARK 3 AREAS WITH POOR DENSITIES: N-TERMINAL A13; C-TERMINAL A233-234.
REMARK 3 4. THERE ARE SOME UNUSUAL DENSITIES FEATURES NEAR A114, A116
REMARK 3 AREA THAT WERE LEFT UNINTERPRETED.
REMARK 4
REMARK 4 2EVR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035151.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-05
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 : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0163, 0.9797
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51615
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 28.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 4.310
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.33
REMARK 200 R MERGE FOR SHELL (I) : 0.82100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.150
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M NACL, 10.0% PEG-6000, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, NANODROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 46.90500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.45250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 70.35750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.90500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.35750
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 23.45250
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 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 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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 46.90500
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 256 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 -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 VAL A 2
REMARK 465 ARG A 3
REMARK 465 LEU A 4
REMARK 465 SER A 5
REMARK 465 GLU A 6
REMARK 465 ALA A 7
REMARK 465 GLU A 8
REMARK 465 VAL A 9
REMARK 465 GLN A 10
REMARK 465 ASN A 11
REMARK 465 PRO A 12
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 13 CG CD CE NZ
REMARK 470 ASP A 74 OD1 OD2
REMARK 470 LYS A 106 CE NZ
REMARK 470 LYS A 192 CE NZ
REMARK 470 GLU A 206 CD OE1 OE2
REMARK 470 GLN A 232 CD OE1 NE2
REMARK 470 ARG A 233 NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 310 O HOH A 370 2.17
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 362 O HOH A 470 7555 2.17
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 CYS A 19 CB CYS A 19 SG -0.106
REMARK 500 TRP A 116 CB TRP A 116 CG -0.114
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 LEU A 14 126.06 -175.56
REMARK 500 LEU A 14 127.82 -176.85
REMARK 500 ASN A 52 -112.75 51.71
REMARK 500 LEU A 181 -82.82 -112.65
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 236 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 99 OE1
REMARK 620 2 GLU A 99 OE2 48.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 235
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 236
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 237
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 238
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 239
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 241
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 359701 RELATED DB: TARGETDB
DBREF 2EVR A 1 234 UNP B2J9B4 B2J9B4_NOSP7 1 234
SEQADV 2EVR MSE A -11 UNP B2J9B4 EXPRESSION TAG
SEQADV 2EVR GLY A -10 UNP B2J9B4 EXPRESSION TAG
SEQADV 2EVR SER A -9 UNP B2J9B4 EXPRESSION TAG
SEQADV 2EVR ASP A -8 UNP B2J9B4 EXPRESSION TAG
SEQADV 2EVR LYS A -7 UNP B2J9B4 EXPRESSION TAG
SEQADV 2EVR ILE A -6 UNP B2J9B4 EXPRESSION TAG
SEQADV 2EVR HIS A -5 UNP B2J9B4 EXPRESSION TAG
SEQADV 2EVR HIS A -4 UNP B2J9B4 EXPRESSION TAG
SEQADV 2EVR HIS A -3 UNP B2J9B4 EXPRESSION TAG
SEQADV 2EVR HIS A -2 UNP B2J9B4 EXPRESSION TAG
SEQADV 2EVR HIS A -1 UNP B2J9B4 EXPRESSION TAG
SEQADV 2EVR HIS A 0 UNP B2J9B4 EXPRESSION TAG
SEQRES 1 A 246 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 A 246 VAL ARG LEU SER GLU ALA GLU VAL GLN ASN PRO LYS LEU
SEQRES 3 A 246 GLY GLU TYR GLN CYS LEU ALA ASP LEU ASN LEU PHE ASP
SEQRES 4 A 246 SER PRO GLU CYS THR ARG LEU ALA THR GLN SER ALA SER
SEQRES 5 A 246 GLY ARG HIS LEU TRP VAL THR SER ASN HIS GLN ASN LEU
SEQRES 6 A 246 ALA VAL GLU VAL TYR LEU CYS GLU ASP ASP TYR PRO GLY
SEQRES 7 A 246 TRP LEU SER LEU SER ASP PHE ASP SER LEU GLN PRO ALA
SEQRES 8 A 246 THR VAL PRO TYR GLN ALA ALA THR PHE SER GLU SER GLU
SEQRES 9 A 246 ILE LYS LYS LEU LEU ALA GLU VAL ILE ALA PHE THR GLN
SEQRES 10 A 246 LYS ALA MSE GLN GLN SER ASN TYR TYR LEU TRP GLY GLY
SEQRES 11 A 246 THR VAL GLY PRO ASN TYR ASP CYS SER GLY LEU MSE GLN
SEQRES 12 A 246 ALA ALA PHE ALA SER VAL GLY ILE TRP LEU PRO ARG ASP
SEQRES 13 A 246 ALA TYR GLN GLN GLU GLY PHE THR GLN PRO ILE THR ILE
SEQRES 14 A 246 ALA GLU LEU VAL ALA GLY ASP LEU VAL PHE PHE GLY THR
SEQRES 15 A 246 SER GLN LYS ALA THR HIS VAL GLY LEU TYR LEU ALA ASP
SEQRES 16 A 246 GLY TYR TYR ILE HIS SER SER GLY LYS ASP GLN GLY ARG
SEQRES 17 A 246 ASP GLY ILE GLY ILE ASP ILE LEU SER GLU GLN GLY ASP
SEQRES 18 A 246 ALA VAL SER LEU SER TYR TYR GLN GLN LEU ARG GLY ALA
SEQRES 19 A 246 GLY ARG VAL PHE LYS SER TYR GLU PRO GLN ARG ARG
MODRES 2EVR MSE A 108 MET SELENOMETHIONINE
MODRES 2EVR MSE A 130 MET SELENOMETHIONINE
HET MSE A 108 8
HET MSE A 130 8
HET CL A 235 1
HET NA A 236 1
HET EDO A 237 4
HET EDO A 238 4
HET EDO A 239 4
HET EDO A 240 4
HET EDO A 241 4
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 2(C5 H11 N O2 SE)
FORMUL 2 CL CL 1-
FORMUL 3 NA NA 1+
FORMUL 4 EDO 5(C2 H6 O2)
FORMUL 9 HOH *290(H2 O)
HELIX 1 1 SER A 71 ASP A 74 5 4
HELIX 2 2 SER A 89 GLN A 110 1 22
HELIX 3 3 ASP A 125 SER A 136 1 12
HELIX 4 4 ASP A 144 THR A 152 1 9
HELIX 5 5 THR A 156 LEU A 160 5 5
HELIX 6 6 ASP A 209 GLN A 217 1 9
SHEET 1 A 5 PRO A 65 SER A 69 0
SHEET 2 A 5 ALA A 54 LEU A 59 -1 N VAL A 57 O GLY A 66
SHEET 3 A 5 HIS A 43 GLN A 51 -1 N TRP A 45 O TYR A 58
SHEET 4 A 5 GLY A 15 CYS A 19 -1 N TYR A 17 O LEU A 44
SHEET 5 A 5 LEU A 76 PRO A 78 -1 O GLN A 77 N GLN A 18
SHEET 1 B 2 LEU A 23 PHE A 26 0
SHEET 2 B 2 LEU A 34 SER A 38 -1 O ALA A 35 N LEU A 25
SHEET 1 C 6 GLN A 153 ILE A 155 0
SHEET 2 C 6 LEU A 219 ARG A 224 -1 O ARG A 224 N GLN A 153
SHEET 3 C 6 LEU A 165 GLY A 169 -1 N LEU A 165 O GLY A 223
SHEET 4 C 6 ALA A 174 TYR A 180 -1 O THR A 175 N PHE A 168
SHEET 5 C 6 TYR A 185 SER A 190 -1 O ILE A 187 N LEU A 179
SHEET 6 C 6 GLY A 198 ILE A 203 -1 O GLY A 200 N HIS A 188
LINK C ALA A 107 N MSE A 108 1555 1555 1.32
LINK C MSE A 108 N GLN A 109 1555 1555 1.34
LINK C LEU A 129 N MSE A 130 1555 1555 1.34
LINK C MSE A 130 N GLN A 131 1555 1555 1.33
LINK OE1 GLU A 99 NA NA A 236 1555 1555 2.18
LINK OE2 GLU A 99 NA NA A 236 1555 1555 2.94
CISPEP 1 GLY A 121 PRO A 122 0 6.04
CISPEP 2 ARG A 233 ARG A 234 0 -12.98
SITE 1 AC1 5 ASP A 27 SER A 28 CYS A 31 THR A 32
SITE 2 AC1 5 ARG A 33
SITE 1 AC2 3 GLU A 99 ALA A 162 LEU A 181
SITE 1 AC3 6 THR A 119 GLN A 131 ALA A 132 TRP A 140
SITE 2 AC3 6 HOH A 244 HOH A 292
SITE 1 AC4 9 ASN A 112 ARG A 196 ASP A 197 GLY A 198
SITE 2 AC4 9 ILE A 199 HOH A 276 HOH A 371 HOH A 520
SITE 3 AC4 9 HOH A 528
SITE 1 AC5 5 ASP A 22 LEU A 23 ASN A 24 ASP A 72
SITE 2 AC5 5 HOH A 434
SITE 1 AC6 8 THR A 32 GLN A 37 GLY A 121 PRO A 122
SITE 2 AC6 8 ASN A 123 HOH A 246 HOH A 300 HOH A 324
SITE 1 AC7 5 GLN A 84 ALA A 85 THR A 87 GLU A 92
SITE 2 AC7 5 GLU A 230
CRYST1 90.470 90.470 93.810 90.00 90.00 90.00 P 41 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 0.011050 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011050 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010660 0.00000
(ATOM LINES ARE NOT SHOWN.)
END