HEADER HYDROLASE 11-DEC-13 4NYN
TITLE CRYSTAL STRUCTURE OF RNASE H1 FROM HALOPHILIC ARCHAEON HALOBACTERIUM
TITLE 2 SALINARUM NRC-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE HI;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HALO-RNASE HI, RNASE HI;
COMPND 5 EC: 3.1.26.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALOBACTERIUM;
SOURCE 3 ORGANISM_TAXID: 64091;
SOURCE 4 STRAIN: NRC-1;
SOURCE 5 GENE: RNHA, VNG_0255C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET25B
KEYWDS HYDROLASE, RNASE H1
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.YOU,C.ANGKAWIDJAJA,Y.KOGA,S.KANAYA
REVDAT 3 08-NOV-23 4NYN 1 REMARK LINK
REVDAT 2 22-NOV-17 4NYN 1 REMARK
REVDAT 1 12-FEB-14 4NYN 0
JRNL AUTH D.J.YOU,C.ANGKAWIDJAJA,Y.KOGA,S.KANAYA
JRNL TITL CRYSTAL STRUCTURE OF RNASE H1 FROM HALOPHILIC ARCHAEON
JRNL TITL 2 HALOBACTERIUM SALINARUM NRC-1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 48893
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2472
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) : 1.41
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.45
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3360
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 158
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1994
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 301
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.57000
REMARK 3 B22 (A**2) : -0.57000
REMARK 3 B33 (A**2) : 1.15000
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): 0.063
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.037
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.905
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2028 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2757 ; 1.026 ; 1.938
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 263 ; 6.736 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 110 ;33.920 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 294 ;13.282 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;16.037 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 296 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1638 ; 0.020 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1302 ; 1.832 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2047 ; 2.979 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 726 ; 4.226 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 710 ; 6.443 ; 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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4NYN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083820.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-11
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 : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : HORIZONTAL FOCUSING MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6500
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48997
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.410
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.38100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, DM 6.1
REMARK 200 STARTING MODEL: 2EHG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 19.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V) PEG 8000, IMIDAZOLE(PH6.5),
REMARK 280 3%(V/V) MPD, 10MM MANGANESE(II) CHLORIDE, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,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 57.90100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 57.90100
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 19.14100
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 57.90100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 9.57050
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 57.90100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.71150
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 57.90100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.90100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 19.14100
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 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 57.90100
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 28.71150
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 57.90100
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 9.57050
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 VAL A 3
REMARK 465 VAL A 4
REMARK 465 GLU A 5
REMARK 465 CYS A 6
REMARK 465 ASP A 7
REMARK 465 ILE A 8
REMARK 465 GLN A 9
REMARK 465 THR A 10
REMARK 465 ALA A 11
REMARK 465 ARG A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 LEU A 15
REMARK 465 ALA A 16
REMARK 465 ASP A 17
REMARK 465 ALA A 18
REMARK 465 GLY A 19
REMARK 465 ALA A 20
REMARK 465 SER A 21
REMARK 465 PHE A 22
REMARK 465 SER A 23
REMARK 465 ASP A 24
REMARK 465 GLY A 25
REMARK 465 ASN A 26
REMARK 465 SER A 27
REMARK 465 GLU A 28
REMARK 465 HIS A 29
REMARK 465 GLU A 30
REMARK 465 LEU A 31
REMARK 465 TRP A 32
REMARK 465 HIS A 33
REMARK 465 ALA A 34
REMARK 465 ASP A 35
REMARK 465 LEU A 36
REMARK 465 GLY A 37
REMARK 465 ASP A 38
REMARK 465 ALA A 39
REMARK 465 HIS A 40
REMARK 465 ALA A 41
REMARK 465 VAL A 42
REMARK 465 ALA A 43
REMARK 465 TYR A 44
REMARK 465 ALA A 45
REMARK 465 ASP A 46
REMARK 465 LYS A 47
REMARK 465 LEU A 48
REMARK 465 VAL A 49
REMARK 465 VAL A 50
REMARK 465 GLN A 51
REMARK 465 GLY A 52
REMARK 465 GLY A 53
REMARK 465 SER A 54
REMARK 465 PRO A 55
REMARK 465 THR A 56
REMARK 465 ASP A 57
REMARK 465 ILE A 58
REMARK 465 THR A 59
REMARK 465 ALA A 60
REMARK 465 VAL A 61
REMARK 465 VAL A 62
REMARK 465 GLN A 63
REMARK 465 PRO A 64
REMARK 465 ASP A 65
REMARK 465 ARG A 66
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 VAL B 3
REMARK 465 VAL B 4
REMARK 465 GLU B 5
REMARK 465 CYS B 6
REMARK 465 ASP B 7
REMARK 465 ILE B 8
REMARK 465 GLN B 9
REMARK 465 THR B 10
REMARK 465 ALA B 11
REMARK 465 ARG B 12
REMARK 465 ALA B 13
REMARK 465 ALA B 14
REMARK 465 LEU B 15
REMARK 465 ALA B 16
REMARK 465 ASP B 17
REMARK 465 ALA B 18
REMARK 465 GLY B 19
REMARK 465 ALA B 20
REMARK 465 SER B 21
REMARK 465 PHE B 22
REMARK 465 SER B 23
REMARK 465 ASP B 24
REMARK 465 GLY B 25
REMARK 465 ASN B 26
REMARK 465 SER B 27
REMARK 465 GLU B 28
REMARK 465 HIS B 29
REMARK 465 GLU B 30
REMARK 465 LEU B 31
REMARK 465 TRP B 32
REMARK 465 HIS B 33
REMARK 465 ALA B 34
REMARK 465 ASP B 35
REMARK 465 LEU B 36
REMARK 465 GLY B 37
REMARK 465 ASP B 38
REMARK 465 ALA B 39
REMARK 465 HIS B 40
REMARK 465 ALA B 41
REMARK 465 VAL B 42
REMARK 465 ALA B 43
REMARK 465 TYR B 44
REMARK 465 ALA B 45
REMARK 465 ASP B 46
REMARK 465 LYS B 47
REMARK 465 LEU B 48
REMARK 465 VAL B 49
REMARK 465 VAL B 50
REMARK 465 GLN B 51
REMARK 465 GLY B 52
REMARK 465 GLY B 53
REMARK 465 SER B 54
REMARK 465 PRO B 55
REMARK 465 THR B 56
REMARK 465 ASP B 57
REMARK 465 ILE B 58
REMARK 465 THR B 59
REMARK 465 ALA B 60
REMARK 465 VAL B 61
REMARK 465 VAL B 62
REMARK 465 GLN B 63
REMARK 465 PRO B 64
REMARK 465 ASP B 65
REMARK 465 ARG B 66
REMARK 465 GLY B 67
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 ARG B 79 77.50 -102.16
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 ASP B 95 GLY B 96 141.50
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 MN A 301 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 75 OD1
REMARK 620 2 GLU A 115 OE2 102.7
REMARK 620 3 ASP A 139 OD1 96.7 108.9
REMARK 620 4 HOH A 530 O 84.4 90.9 159.3
REMARK 620 5 HOH A 540 O 80.7 162.9 87.0 72.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 302 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 75 OD2
REMARK 620 2 ASP A 189 OD1 95.0
REMARK 620 3 HOH A 528 O 91.2 90.0
REMARK 620 4 HOH A 530 O 92.5 167.1 79.4
REMARK 620 5 HOH A 540 O 91.3 111.9 157.7 78.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 202 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 198 OD1
REMARK 620 2 HOH A 421 O 86.1
REMARK 620 3 ASP B 75 OD2 173.8 87.7
REMARK 620 4 ASP B 189 OD1 92.7 174.4 93.5
REMARK 620 5 HOH B 426 O 83.4 77.0 95.5 108.3
REMARK 620 6 HOH B 428 O 90.4 83.4 88.6 91.2 159.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 201 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 421 O
REMARK 620 2 ASP B 75 OD1 85.4
REMARK 620 3 GLU B 115 OE1 109.2 90.2
REMARK 620 4 ASP B 139 OD1 155.3 95.7 95.5
REMARK 620 5 HOH B 426 O 73.9 87.7 176.1 81.4
REMARK 620 6 HOH B 429 O 87.5 172.2 89.0 92.1 93.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 203 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 103 O
REMARK 620 2 HOH B 443 O 95.9
REMARK 620 3 HOH B 444 O 88.5 90.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 203
DBREF 4NYN A 1 199 UNP Q9HSF6 RNH_HALSA 1 199
DBREF 4NYN B 1 199 UNP Q9HSF6 RNH_HALSA 1 199
SEQRES 1 A 199 MET PRO VAL VAL GLU CYS ASP ILE GLN THR ALA ARG ALA
SEQRES 2 A 199 ALA LEU ALA ASP ALA GLY ALA SER PHE SER ASP GLY ASN
SEQRES 3 A 199 SER GLU HIS GLU LEU TRP HIS ALA ASP LEU GLY ASP ALA
SEQRES 4 A 199 HIS ALA VAL ALA TYR ALA ASP LYS LEU VAL VAL GLN GLY
SEQRES 5 A 199 GLY SER PRO THR ASP ILE THR ALA VAL VAL GLN PRO ASP
SEQRES 6 A 199 ARG GLY GLY ARG VAL HIS ALA TYR PHE ASP GLY ALA SER
SEQRES 7 A 199 ARG GLY ASN PRO GLY PRO ALA ALA VAL GLY TRP VAL LEU
SEQRES 8 A 199 VAL SER GLY ASP GLY GLY ILE VAL ALA GLU GLY GLY ASP
SEQRES 9 A 199 THR ILE GLY ARG ALA THR ASN ASN GLN ALA GLU TYR ASP
SEQRES 10 A 199 ALA LEU ILE ALA ALA LEU GLU ALA ALA ALA ASP PHE GLY
SEQRES 11 A 199 PHE ASP ASP ILE GLU LEU ARG GLY ASP SER GLN LEU VAL
SEQRES 12 A 199 GLU LYS GLN LEU THR GLY ALA TRP ASP THR ASN ASP PRO
SEQRES 13 A 199 ASP LEU ARG ARG LYS ARG VAL ARG ALA ARG GLU LEU LEU
SEQRES 14 A 199 THR GLY PHE ASP ASP TRP SER ILE THR HIS VAL PRO ARG
SEQRES 15 A 199 ALA THR ASN GLU ARG ALA ASP ALA LEU ALA ASN GLU ALA
SEQRES 16 A 199 LEU ASP ASP ALA
SEQRES 1 B 199 MET PRO VAL VAL GLU CYS ASP ILE GLN THR ALA ARG ALA
SEQRES 2 B 199 ALA LEU ALA ASP ALA GLY ALA SER PHE SER ASP GLY ASN
SEQRES 3 B 199 SER GLU HIS GLU LEU TRP HIS ALA ASP LEU GLY ASP ALA
SEQRES 4 B 199 HIS ALA VAL ALA TYR ALA ASP LYS LEU VAL VAL GLN GLY
SEQRES 5 B 199 GLY SER PRO THR ASP ILE THR ALA VAL VAL GLN PRO ASP
SEQRES 6 B 199 ARG GLY GLY ARG VAL HIS ALA TYR PHE ASP GLY ALA SER
SEQRES 7 B 199 ARG GLY ASN PRO GLY PRO ALA ALA VAL GLY TRP VAL LEU
SEQRES 8 B 199 VAL SER GLY ASP GLY GLY ILE VAL ALA GLU GLY GLY ASP
SEQRES 9 B 199 THR ILE GLY ARG ALA THR ASN ASN GLN ALA GLU TYR ASP
SEQRES 10 B 199 ALA LEU ILE ALA ALA LEU GLU ALA ALA ALA ASP PHE GLY
SEQRES 11 B 199 PHE ASP ASP ILE GLU LEU ARG GLY ASP SER GLN LEU VAL
SEQRES 12 B 199 GLU LYS GLN LEU THR GLY ALA TRP ASP THR ASN ASP PRO
SEQRES 13 B 199 ASP LEU ARG ARG LYS ARG VAL ARG ALA ARG GLU LEU LEU
SEQRES 14 B 199 THR GLY PHE ASP ASP TRP SER ILE THR HIS VAL PRO ARG
SEQRES 15 B 199 ALA THR ASN GLU ARG ALA ASP ALA LEU ALA ASN GLU ALA
SEQRES 16 B 199 LEU ASP ASP ALA
HET MN A 301 1
HET MN A 302 1
HET MN B 201 1
HET MN B 202 1
HET MN B 203 1
HETNAM MN MANGANESE (II) ION
FORMUL 3 MN 5(MN 2+)
FORMUL 8 HOH *301(H2 O)
HELIX 1 1 THR A 110 PHE A 129 1 20
HELIX 2 2 SER A 140 THR A 148 1 9
HELIX 3 3 ASP A 155 GLY A 171 1 17
HELIX 4 4 ASN A 185 ASP A 198 1 14
HELIX 5 5 THR B 110 PHE B 129 1 20
HELIX 6 6 SER B 140 THR B 148 1 9
HELIX 7 7 ASP B 155 THR B 170 1 16
HELIX 8 8 PRO B 181 THR B 184 5 4
HELIX 9 9 ASN B 185 ALA B 199 1 15
SHEET 1 A 5 ILE A 98 ALA A 109 0
SHEET 2 A 5 GLY A 83 VAL A 92 -1 N LEU A 91 O ALA A 100
SHEET 3 A 5 ARG A 69 SER A 78 -1 N HIS A 71 O VAL A 92
SHEET 4 A 5 ASP A 133 GLY A 138 1 O GLU A 135 N VAL A 70
SHEET 5 A 5 ASP A 174 HIS A 179 1 O SER A 176 N LEU A 136
SHEET 1 B 5 ILE B 98 ALA B 109 0
SHEET 2 B 5 GLY B 83 SER B 93 -1 N LEU B 91 O ALA B 100
SHEET 3 B 5 ARG B 69 SER B 78 -1 N HIS B 71 O VAL B 92
SHEET 4 B 5 ASP B 133 GLY B 138 1 O GLU B 135 N VAL B 70
SHEET 5 B 5 ASP B 174 HIS B 179 1 O SER B 176 N LEU B 136
LINK OD1 ASP A 75 MN MN A 301 1555 1555 2.09
LINK OD2 ASP A 75 MN MN A 302 1555 1555 2.15
LINK OE2 GLU A 115 MN MN A 301 1555 1555 2.12
LINK OD1 ASP A 139 MN MN A 301 1555 1555 2.10
LINK OD1 ASP A 189 MN MN A 302 1555 1555 2.11
LINK OD1 ASP A 198 MN MN B 202 1555 1555 2.14
LINK MN MN A 301 O HOH A 530 1555 1555 2.28
LINK MN MN A 301 O HOH A 540 1555 1555 2.60
LINK MN MN A 302 O HOH A 528 1555 1555 2.28
LINK MN MN A 302 O HOH A 530 1555 1555 2.45
LINK MN MN A 302 O HOH A 540 1555 1555 2.14
LINK O HOH A 421 MN MN B 201 1555 1555 2.37
LINK O HOH A 421 MN MN B 202 1555 1555 2.36
LINK OD1 ASP B 75 MN MN B 201 1555 1555 2.09
LINK OD2 ASP B 75 MN MN B 202 1555 1555 2.18
LINK O GLY B 103 MN MN B 203 1555 1555 2.19
LINK OE1 GLU B 115 MN MN B 201 1555 1555 2.13
LINK OD1 ASP B 139 MN MN B 201 1555 1555 2.21
LINK OD1 ASP B 189 MN MN B 202 1555 1555 2.08
LINK MN MN B 201 O HOH B 426 1555 1555 2.41
LINK MN MN B 201 O HOH B 429 1555 1555 2.07
LINK MN MN B 202 O HOH B 426 1555 1555 2.26
LINK MN MN B 202 O HOH B 428 1555 1555 2.22
LINK MN MN B 203 O HOH B 443 1555 1555 2.24
LINK MN MN B 203 O HOH B 444 1555 1555 2.16
CISPEP 1 ASN A 81 PRO A 82 0 4.28
CISPEP 2 ASN B 81 PRO B 82 0 12.97
SITE 1 AC1 7 ASP A 75 GLU A 115 ASP A 139 ASP A 174
SITE 2 AC1 7 MN A 302 HOH A 530 HOH A 540
SITE 1 AC2 7 ASP A 75 ASP A 173 ASP A 189 MN A 301
SITE 2 AC2 7 HOH A 528 HOH A 530 HOH A 540
SITE 1 AC3 7 HOH A 421 ASP B 75 GLU B 115 ASP B 139
SITE 2 AC3 7 MN B 202 HOH B 426 HOH B 429
SITE 1 AC4 7 ASP A 198 HOH A 421 ASP B 75 ASP B 189
SITE 2 AC4 7 MN B 201 HOH B 426 HOH B 428
SITE 1 AC5 6 GLY B 103 HOH B 325 HOH B 413 HOH B 423
SITE 2 AC5 6 HOH B 443 HOH B 444
CRYST1 115.802 115.802 38.282 90.00 90.00 90.00 I 41 16
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 0.008635 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008635 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026122 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
