HEADER TRANSCRIPTION REGULATOR 30-JUN-10 3NRV
TITLE CRYSTAL STRUCTURE OF MARR/EMRR FAMILY TRANSCRIPTIONAL REGULATOR FROM
TITLE 2 ACINETOBACTER SP. ADP1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE TRANSCRIPTIONAL REGULATOR (MARR/EMRR FAMILY);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACINETOBACTER SP. ADP1;
SOURCE 3 ORGANISM_TAXID: 62977;
SOURCE 4 GENE: 2878967, ACIAD1811;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PDM68
KEYWDS TRANSCRIPTIONAL REGULATOR, PSI-2, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 STRUCTURAL GENOMICS, MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG),
KEYWDS 3 TRANSCRIPTION REGULATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ZHANG,R.WU,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS
AUTHOR 2 (MCSG)
REVDAT 3 27-DEC-23 3NRV 1 REMARK
REVDAT 2 09-SEP-20 3NRV 1 JRNL REMARK SEQADV LINK
REVDAT 1 15-SEP-10 3NRV 0
JRNL AUTH Z.RONGGUANG,W.RUIYING,J.ANDRZEJ,
JRNL AUTH 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
JRNL TITL CRYSTAL STRUCTURE OF MARR/EMRR FAMILY TRANSCRIPTIONAL
JRNL TITL 2 REGULATOR FROM ACINETOBACTER SP. ADP1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 53697
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2856
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 32.5886 - 4.3086 0.98 5472 282 0.1922 0.2271
REMARK 3 2 4.3086 - 3.4211 1.00 5405 309 0.1653 0.1722
REMARK 3 3 3.4211 - 2.9890 1.00 5372 301 0.1979 0.2445
REMARK 3 4 2.9890 - 2.7158 1.00 5375 262 0.2025 0.2301
REMARK 3 5 2.7158 - 2.5213 1.00 5392 275 0.2003 0.2321
REMARK 3 6 2.5213 - 2.3727 1.00 5322 282 0.2048 0.2503
REMARK 3 7 2.3727 - 2.2539 0.99 5358 292 0.2088 0.2634
REMARK 3 8 2.2539 - 2.1558 1.00 5282 308 0.2107 0.2534
REMARK 3 9 2.1558 - 2.0728 0.99 5302 284 0.2124 0.2585
REMARK 3 10 2.0728 - 2.0013 0.98 5234 261 0.2326 0.2853
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 60.18
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.25540
REMARK 3 B22 (A**2) : -4.25580
REMARK 3 B33 (A**2) : -2.99960
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.22740
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 4590
REMARK 3 ANGLE : 1.040 6148
REMARK 3 CHIRALITY : 0.079 700
REMARK 3 PLANARITY : 0.003 771
REMARK 3 DIHEDRAL : 17.065 1778
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A RESID 3:145
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8372 29.4190 78.7363
REMARK 3 T TENSOR
REMARK 3 T11: 0.2035 T22: 0.1820
REMARK 3 T33: 0.1892 T12: -0.0310
REMARK 3 T13: -0.0764 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 0.8559 L22: 0.9545
REMARK 3 L33: 0.7639 L12: 0.0882
REMARK 3 L13: 0.5990 L23: -0.1739
REMARK 3 S TENSOR
REMARK 3 S11: -0.1579 S12: 0.1587 S13: 0.0427
REMARK 3 S21: -0.2202 S22: 0.0821 S23: 0.1135
REMARK 3 S31: -0.0458 S32: 0.0634 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B RESID 2:145
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6896 26.3160 67.8488
REMARK 3 T TENSOR
REMARK 3 T11: 0.1990 T22: 0.1847
REMARK 3 T33: 0.2000 T12: 0.0217
REMARK 3 T13: 0.0760 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 1.2391 L22: 1.0511
REMARK 3 L33: 0.9522 L12: -0.3502
REMARK 3 L13: -0.4209 L23: -0.0353
REMARK 3 S TENSOR
REMARK 3 S11: -0.1570 S12: -0.1693 S13: -0.0574
REMARK 3 S21: 0.2062 S22: 0.1120 S23: 0.1613
REMARK 3 S31: 0.0272 S32: -0.0032 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C RESID 4:145
REMARK 3 ORIGIN FOR THE GROUP (A): 38.4050 28.7512 90.2053
REMARK 3 T TENSOR
REMARK 3 T11: 0.1927 T22: 0.1750
REMARK 3 T33: 0.1618 T12: 0.0322
REMARK 3 T13: 0.0057 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.8358 L22: 1.3402
REMARK 3 L33: 1.1498 L12: 0.3980
REMARK 3 L13: -0.1437 L23: -0.1966
REMARK 3 S TENSOR
REMARK 3 S11: -0.1022 S12: -0.0206 S13: 0.0360
REMARK 3 S21: -0.0853 S22: 0.1046 S23: 0.0344
REMARK 3 S31: 0.0678 S32: 0.0628 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D RESID 4:145
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9131 27.1178 56.4163
REMARK 3 T TENSOR
REMARK 3 T11: 0.1751 T22: 0.1639
REMARK 3 T33: 0.1470 T12: -0.0346
REMARK 3 T13: 0.0002 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.8062 L22: 1.4005
REMARK 3 L33: 1.2723 L12: -0.3841
REMARK 3 L13: 0.1718 L23: -0.0638
REMARK 3 S TENSOR
REMARK 3 S11: -0.0963 S12: 0.0449 S13: -0.0663
REMARK 3 S21: 0.0738 S22: 0.0959 S23: 0.0336
REMARK 3 S31: -0.0537 S32: 0.0664 S33: -0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NRV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060202.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-10
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-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97926
REMARK 200 MONOCHROMATOR : SI 111, CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-2
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53697
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.51400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.5; 2M NH4SO4, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 29.78650
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 SER A 25
REMARK 465 SER A 26
REMARK 465 THR A 27
REMARK 465 ALA A 28
REMARK 465 ASN A 84
REMARK 465 GLY A 85
REMARK 465 HIS A 86
REMARK 465 SER A 87
REMARK 465 GLU A 88
REMARK 465 ASP A 89
REMARK 465 LYS A 90
REMARK 465 ARG A 91
REMARK 465 THR A 92
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 LYS B 24
REMARK 465 SER B 25
REMARK 465 SER B 26
REMARK 465 THR B 27
REMARK 465 ALA B 28
REMARK 465 ASN B 84
REMARK 465 GLY B 85
REMARK 465 HIS B 86
REMARK 465 SER B 87
REMARK 465 GLU B 88
REMARK 465 ASP B 89
REMARK 465 LYS B 90
REMARK 465 ARG B 91
REMARK 465 THR B 92
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 ALA C 0
REMARK 465 MSE C 1
REMARK 465 GLN C 2
REMARK 465 LYS C 3
REMARK 465 SER D -2
REMARK 465 ASN D -1
REMARK 465 ALA D 0
REMARK 465 MSE D 1
REMARK 465 GLN D 2
REMARK 465 LYS D 3
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 GLN B 2 CG CD OE1 NE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 99 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 399 O HOH B 400 2.13
REMARK 500 O HOH A 358 O HOH A 359 2.18
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 ASP D 51 N ASP D 51 CA -0.133
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 ASP D 51 CB - CA - C ANGL. DEV. = 16.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR B 30 -35.52 -130.34
REMARK 500 GLU C 88 31.70 -98.39
REMARK 500 ASP D 51 105.01 -41.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER D 50 ASP D 51 -128.18
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 B 146 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 33 O
REMARK 620 2 TYR B 80 OH 110.8
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 SO4 A 146
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 146
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 146
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 148
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 146
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 147
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC88533 RELATED DB: TARGETDB
DBREF 3NRV A 1 145 UNP Q6FBB7 Q6FBB7_ACIAD 1 145
DBREF 3NRV B 1 145 UNP Q6FBB7 Q6FBB7_ACIAD 1 145
DBREF 3NRV C 1 145 UNP Q6FBB7 Q6FBB7_ACIAD 1 145
DBREF 3NRV D 1 145 UNP Q6FBB7 Q6FBB7_ACIAD 1 145
SEQADV 3NRV SER A -2 UNP Q6FBB7 EXPRESSION TAG
SEQADV 3NRV ASN A -1 UNP Q6FBB7 EXPRESSION TAG
SEQADV 3NRV ALA A 0 UNP Q6FBB7 EXPRESSION TAG
SEQADV 3NRV SER B -2 UNP Q6FBB7 EXPRESSION TAG
SEQADV 3NRV ASN B -1 UNP Q6FBB7 EXPRESSION TAG
SEQADV 3NRV ALA B 0 UNP Q6FBB7 EXPRESSION TAG
SEQADV 3NRV SER C -2 UNP Q6FBB7 EXPRESSION TAG
SEQADV 3NRV ASN C -1 UNP Q6FBB7 EXPRESSION TAG
SEQADV 3NRV ALA C 0 UNP Q6FBB7 EXPRESSION TAG
SEQADV 3NRV SER D -2 UNP Q6FBB7 EXPRESSION TAG
SEQADV 3NRV ASN D -1 UNP Q6FBB7 EXPRESSION TAG
SEQADV 3NRV ALA D 0 UNP Q6FBB7 EXPRESSION TAG
SEQRES 1 A 148 SER ASN ALA MSE GLN LYS ILE ASN ILE ASP ARG HIS ALA
SEQRES 2 A 148 THR ALA GLN ILE ASN MSE LEU ALA ASN LYS LEU MSE LEU
SEQRES 3 A 148 LYS SER SER THR ALA TYR THR GLN LYS PHE GLY ILE GLY
SEQRES 4 A 148 MSE THR GLU TRP ARG ILE ILE SER VAL LEU SER SER ALA
SEQRES 5 A 148 SER ASP CYS SER VAL GLN LYS ILE SER ASP ILE LEU GLY
SEQRES 6 A 148 LEU ASP LYS ALA ALA VAL SER ARG THR VAL LYS LYS LEU
SEQRES 7 A 148 GLU GLU LYS LYS TYR ILE GLU VAL ASN GLY HIS SER GLU
SEQRES 8 A 148 ASP LYS ARG THR TYR ALA ILE ASN LEU THR GLU MSE GLY
SEQRES 9 A 148 GLN GLU LEU TYR GLU VAL ALA SER ASP PHE ALA ILE GLU
SEQRES 10 A 148 ARG GLU LYS GLN LEU LEU GLU GLU PHE GLU GLU ALA GLU
SEQRES 11 A 148 LYS ASP GLN LEU PHE ILE LEU LEU LYS LYS LEU ARG ASN
SEQRES 12 A 148 LYS VAL ASP GLN MSE
SEQRES 1 B 148 SER ASN ALA MSE GLN LYS ILE ASN ILE ASP ARG HIS ALA
SEQRES 2 B 148 THR ALA GLN ILE ASN MSE LEU ALA ASN LYS LEU MSE LEU
SEQRES 3 B 148 LYS SER SER THR ALA TYR THR GLN LYS PHE GLY ILE GLY
SEQRES 4 B 148 MSE THR GLU TRP ARG ILE ILE SER VAL LEU SER SER ALA
SEQRES 5 B 148 SER ASP CYS SER VAL GLN LYS ILE SER ASP ILE LEU GLY
SEQRES 6 B 148 LEU ASP LYS ALA ALA VAL SER ARG THR VAL LYS LYS LEU
SEQRES 7 B 148 GLU GLU LYS LYS TYR ILE GLU VAL ASN GLY HIS SER GLU
SEQRES 8 B 148 ASP LYS ARG THR TYR ALA ILE ASN LEU THR GLU MSE GLY
SEQRES 9 B 148 GLN GLU LEU TYR GLU VAL ALA SER ASP PHE ALA ILE GLU
SEQRES 10 B 148 ARG GLU LYS GLN LEU LEU GLU GLU PHE GLU GLU ALA GLU
SEQRES 11 B 148 LYS ASP GLN LEU PHE ILE LEU LEU LYS LYS LEU ARG ASN
SEQRES 12 B 148 LYS VAL ASP GLN MSE
SEQRES 1 C 148 SER ASN ALA MSE GLN LYS ILE ASN ILE ASP ARG HIS ALA
SEQRES 2 C 148 THR ALA GLN ILE ASN MSE LEU ALA ASN LYS LEU MSE LEU
SEQRES 3 C 148 LYS SER SER THR ALA TYR THR GLN LYS PHE GLY ILE GLY
SEQRES 4 C 148 MSE THR GLU TRP ARG ILE ILE SER VAL LEU SER SER ALA
SEQRES 5 C 148 SER ASP CYS SER VAL GLN LYS ILE SER ASP ILE LEU GLY
SEQRES 6 C 148 LEU ASP LYS ALA ALA VAL SER ARG THR VAL LYS LYS LEU
SEQRES 7 C 148 GLU GLU LYS LYS TYR ILE GLU VAL ASN GLY HIS SER GLU
SEQRES 8 C 148 ASP LYS ARG THR TYR ALA ILE ASN LEU THR GLU MSE GLY
SEQRES 9 C 148 GLN GLU LEU TYR GLU VAL ALA SER ASP PHE ALA ILE GLU
SEQRES 10 C 148 ARG GLU LYS GLN LEU LEU GLU GLU PHE GLU GLU ALA GLU
SEQRES 11 C 148 LYS ASP GLN LEU PHE ILE LEU LEU LYS LYS LEU ARG ASN
SEQRES 12 C 148 LYS VAL ASP GLN MSE
SEQRES 1 D 148 SER ASN ALA MSE GLN LYS ILE ASN ILE ASP ARG HIS ALA
SEQRES 2 D 148 THR ALA GLN ILE ASN MSE LEU ALA ASN LYS LEU MSE LEU
SEQRES 3 D 148 LYS SER SER THR ALA TYR THR GLN LYS PHE GLY ILE GLY
SEQRES 4 D 148 MSE THR GLU TRP ARG ILE ILE SER VAL LEU SER SER ALA
SEQRES 5 D 148 SER ASP CYS SER VAL GLN LYS ILE SER ASP ILE LEU GLY
SEQRES 6 D 148 LEU ASP LYS ALA ALA VAL SER ARG THR VAL LYS LYS LEU
SEQRES 7 D 148 GLU GLU LYS LYS TYR ILE GLU VAL ASN GLY HIS SER GLU
SEQRES 8 D 148 ASP LYS ARG THR TYR ALA ILE ASN LEU THR GLU MSE GLY
SEQRES 9 D 148 GLN GLU LEU TYR GLU VAL ALA SER ASP PHE ALA ILE GLU
SEQRES 10 D 148 ARG GLU LYS GLN LEU LEU GLU GLU PHE GLU GLU ALA GLU
SEQRES 11 D 148 LYS ASP GLN LEU PHE ILE LEU LEU LYS LYS LEU ARG ASN
SEQRES 12 D 148 LYS VAL ASP GLN MSE
MODRES 3NRV MSE A 16 MET SELENOMETHIONINE
MODRES 3NRV MSE A 22 MET SELENOMETHIONINE
MODRES 3NRV MSE A 37 MET SELENOMETHIONINE
MODRES 3NRV MSE A 100 MET SELENOMETHIONINE
MODRES 3NRV MSE A 145 MET SELENOMETHIONINE
MODRES 3NRV MSE B 16 MET SELENOMETHIONINE
MODRES 3NRV MSE B 22 MET SELENOMETHIONINE
MODRES 3NRV MSE B 37 MET SELENOMETHIONINE
MODRES 3NRV MSE B 100 MET SELENOMETHIONINE
MODRES 3NRV MSE B 145 MET SELENOMETHIONINE
MODRES 3NRV MSE C 16 MET SELENOMETHIONINE
MODRES 3NRV MSE C 22 MET SELENOMETHIONINE
MODRES 3NRV MSE C 37 MET SELENOMETHIONINE
MODRES 3NRV MSE C 100 MET SELENOMETHIONINE
MODRES 3NRV MSE C 145 MET SELENOMETHIONINE
MODRES 3NRV MSE D 16 MET SELENOMETHIONINE
MODRES 3NRV MSE D 22 MET SELENOMETHIONINE
MODRES 3NRV MSE D 37 MET SELENOMETHIONINE
MODRES 3NRV MSE D 100 MET SELENOMETHIONINE
MODRES 3NRV MSE D 145 MET SELENOMETHIONINE
HET MSE A 16 16
HET MSE A 22 8
HET MSE A 37 8
HET MSE A 100 8
HET MSE A 145 8
HET MSE B 16 16
HET MSE B 22 8
HET MSE B 37 8
HET MSE B 100 8
HET MSE B 145 8
HET MSE C 16 8
HET MSE C 22 8
HET MSE C 37 8
HET MSE C 100 8
HET MSE C 145 8
HET MSE D 16 8
HET MSE D 22 8
HET MSE D 37 8
HET MSE D 100 8
HET MSE D 145 8
HET SO4 A 146 5
HET SO4 A 147 5
HET GOL A 148 6
HET GOL A 149 6
HET NA B 146 1
HET GOL B 147 6
HET GOL B 148 6
HET SO4 C 146 5
HET SO4 C 147 5
HET SO4 C 148 5
HET SO4 D 146 5
HET SO4 D 147 5
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 5 SO4 7(O4 S 2-)
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 9 NA NA 1+
FORMUL 17 HOH *302(H2 O)
HELIX 1 1 ASN A 5 ARG A 8 5 4
HELIX 2 2 HIS A 9 LYS A 24 1 16
HELIX 3 3 THR A 30 GLY A 34 5 5
HELIX 4 4 GLY A 36 ALA A 49 1 14
HELIX 5 5 SER A 53 GLY A 62 1 10
HELIX 6 6 ASP A 64 LYS A 78 1 15
HELIX 7 7 THR A 98 ALA A 112 1 15
HELIX 8 8 ALA A 112 LEU A 120 1 9
HELIX 9 9 GLU A 124 MSE A 145 1 22
HELIX 10 10 ASN B 5 ARG B 8 5 4
HELIX 11 11 HIS B 9 LEU B 23 1 15
HELIX 12 12 THR B 30 GLY B 34 5 5
HELIX 13 13 GLY B 36 ALA B 49 1 14
HELIX 14 14 SER B 53 GLY B 62 1 10
HELIX 15 15 ASP B 64 LYS B 78 1 15
HELIX 16 16 THR B 98 ALA B 112 1 15
HELIX 17 17 ALA B 112 LEU B 120 1 9
HELIX 18 18 GLU B 124 MSE B 145 1 22
HELIX 19 19 HIS C 9 GLY C 34 1 26
HELIX 20 20 GLY C 36 ALA C 49 1 14
HELIX 21 21 SER C 53 GLY C 62 1 10
HELIX 22 22 ASP C 64 LYS C 78 1 15
HELIX 23 23 THR C 98 LEU C 120 1 23
HELIX 24 24 GLU C 124 GLN C 144 1 21
HELIX 25 25 HIS D 9 GLY D 34 1 26
HELIX 26 26 GLY D 36 ALA D 49 1 14
HELIX 27 27 SER D 53 GLY D 62 1 10
HELIX 28 28 ASP D 64 LYS D 78 1 15
HELIX 29 29 THR D 98 LEU D 120 1 23
HELIX 30 30 GLU D 124 MSE D 145 1 22
SHEET 1 A 2 ILE A 81 GLU A 82 0
SHEET 2 A 2 ASN A 96 LEU A 97 -1 O ASN A 96 N GLU A 82
SHEET 1 B 2 ILE B 81 GLU B 82 0
SHEET 2 B 2 ASN B 96 LEU B 97 -1 O ASN B 96 N GLU B 82
SHEET 1 C 2 ILE C 81 ASN C 84 0
SHEET 2 C 2 ALA C 94 LEU C 97 -1 O ALA C 94 N ASN C 84
SHEET 1 D 2 ILE D 81 ASN D 84 0
SHEET 2 D 2 ALA D 94 LEU D 97 -1 O ALA D 94 N ASN D 84
LINK C ASN A 15 N AMSE A 16 1555 1555 1.32
LINK C ASN A 15 N BMSE A 16 1555 1555 1.34
LINK C AMSE A 16 N LEU A 17 1555 1555 1.33
LINK C BMSE A 16 N LEU A 17 1555 1555 1.33
LINK C LEU A 21 N MSE A 22 1555 1555 1.33
LINK C MSE A 22 N LEU A 23 1555 1555 1.33
LINK C GLY A 36 N MSE A 37 1555 1555 1.33
LINK C MSE A 37 N THR A 38 1555 1555 1.33
LINK C GLU A 99 N MSE A 100 1555 1555 1.33
LINK C MSE A 100 N GLY A 101 1555 1555 1.33
LINK C GLN A 144 N MSE A 145 1555 1555 1.33
LINK C ASN B 15 N AMSE B 16 1555 1555 1.34
LINK C ASN B 15 N BMSE B 16 1555 1555 1.32
LINK C AMSE B 16 N LEU B 17 1555 1555 1.33
LINK C BMSE B 16 N LEU B 17 1555 1555 1.33
LINK C LEU B 21 N MSE B 22 1555 1555 1.33
LINK C MSE B 22 N LEU B 23 1555 1555 1.33
LINK C GLY B 36 N MSE B 37 1555 1555 1.33
LINK C MSE B 37 N THR B 38 1555 1555 1.33
LINK C GLU B 99 N MSE B 100 1555 1555 1.32
LINK C MSE B 100 N GLY B 101 1555 1555 1.32
LINK C GLN B 144 N MSE B 145 1555 1555 1.34
LINK C ASN C 15 N MSE C 16 1555 1555 1.33
LINK C MSE C 16 N LEU C 17 1555 1555 1.33
LINK C LEU C 21 N MSE C 22 1555 1555 1.33
LINK C MSE C 22 N LEU C 23 1555 1555 1.34
LINK C GLY C 36 N MSE C 37 1555 1555 1.33
LINK C MSE C 37 N THR C 38 1555 1555 1.32
LINK C GLU C 99 N MSE C 100 1555 1555 1.33
LINK C MSE C 100 N GLY C 101 1555 1555 1.33
LINK C GLN C 144 N MSE C 145 1555 1555 1.33
LINK C ASN D 15 N MSE D 16 1555 1555 1.33
LINK C MSE D 16 N LEU D 17 1555 1555 1.33
LINK C LEU D 21 N MSE D 22 1555 1555 1.33
LINK C MSE D 22 N LEU D 23 1555 1555 1.34
LINK C GLY D 36 N MSE D 37 1555 1555 1.33
LINK C MSE D 37 N THR D 38 1555 1555 1.32
LINK C GLU D 99 N MSE D 100 1555 1555 1.33
LINK C MSE D 100 N GLY D 101 1555 1555 1.33
LINK C GLN D 144 N MSE D 145 1555 1555 1.33
LINK O PHE B 33 NA NA B 146 1555 1555 2.73
LINK OH TYR B 80 NA NA B 146 1555 1555 2.77
SITE 1 AC1 5 ALA A 49 SER A 50 HOH A 396 LYS C 20
SITE 2 AC1 5 HOH C 165
SITE 1 AC2 4 LYS A 24 TYR A 29 MSE A 37 GOL A 149
SITE 1 AC3 10 MSE A 22 ARG A 41 SER A 44 LEU A 61
SITE 2 AC3 10 HOH A 161 HOH A 483 HOH A 494 ASN C 15
SITE 3 AC3 10 ASN C 19 MSE C 22
SITE 1 AC4 7 THR A 30 TRP A 40 ALA A 112 SO4 A 147
SITE 2 AC4 7 HOH A 156 HOH A 171 HIS C 9
SITE 1 AC5 5 PHE B 33 TYR B 80 GLY C 85 TYR C 93
SITE 2 AC5 5 HOH C 393
SITE 1 AC6 9 MSE B 22 ARG B 41 SER B 44 LEU B 61
SITE 2 AC6 9 HOH B 157 HOH B 445 ASN D 15 ASN D 19
SITE 3 AC6 9 MSE D 22
SITE 1 AC7 5 THR B 38 ARG B 41 HOH B 482 ASP D 64
SITE 2 AC7 5 HOH D 176
SITE 1 AC8 4 ASP A 64 LYS A 65 ARG C 70 LYS C 74
SITE 1 AC9 3 GLU A 125 LYS A 128 ARG C 8
SITE 1 BC1 7 SER C 50 ASP C 51 HIS C 86 ARG C 91
SITE 2 BC1 7 ALA C 94 ASN C 96 HOH C 170
SITE 1 BC2 3 ALA B 49 SER B 50 LYS D 20
SITE 1 BC3 4 ASP B 64 LYS B 65 ARG D 70 LYS D 74
CRYST1 72.809 59.573 97.753 90.00 89.99 90.00 P 1 21 1 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 0.013735 0.000000 -0.000002 0.00000
SCALE2 0.000000 0.016786 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010230 0.00000
(ATOM LINES ARE NOT SHOWN.)
END