HEADER RNA BINDING PROTEIN 11-JUL-12 4G24
TITLE CRYSTAL STRUCTURE OF PROTEINACEOUS RNASE P 1 (PRORP1) FROM A. THALIANA
TITLE 2 WITH MN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PENTATRICOPEPTIDE REPEAT-CONTAINING PROTEIN AT2G32230,
COMPND 3 MITOCHONDRIAL;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 77-572;
COMPND 6 EC: 3.1.26.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: AT2G32230, F22D22.2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM-11
KEYWDS METALLONUCLEASE, PRORP, RIBONUCLEASE, PIN, TRNA PROCESSING, RNASE P,
KEYWDS 2 NYN DOMAIN, PPR DOMAIN, CHLOROPLASTS, RNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KOUTMOS,M.J.HOWARD,C.A.FIERKE
REVDAT 3 15-NOV-23 4G24 1 REMARK SEQADV LINK ATOM
REVDAT 2 14-NOV-12 4G24 1 JRNL
REVDAT 1 26-SEP-12 4G24 0
JRNL AUTH M.J.HOWARD,W.H.LIM,C.A.FIERKE,M.KOUTMOS
JRNL TITL MITOCHONDRIAL RIBONUCLEASE P STRUCTURE PROVIDES INSIGHT INTO
JRNL TITL 2 THE EVOLUTION OF CATALYTIC STRATEGIES FOR PRECURSOR-TRNA 5'
JRNL TITL 3 PROCESSING.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 16149 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22991464
JRNL DOI 10.1073/PNAS.1209062109
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 46002
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2451
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2975
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE SET COUNT : 154
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3787
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : 0.73000
REMARK 3 B33 (A**2) : -0.60000
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): 0.146
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.136
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.385
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3939 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5327 ; 1.380 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 489 ; 5.995 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 189 ;33.215 ;24.233
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 709 ;14.986 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;23.753 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 568 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3002 ; 0.006 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4G24 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073641.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.968
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : K-B PAIR OF BIOMORPH MIRRORS FOR
REMARK 200 VERTICAL AND HORIZONTAL FOCUSING
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48526
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.47300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3350, 0.1 M SODIUM CITRATE
REMARK 280 TRIBASIC PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 20.87500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.38100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.23750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.38100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.87500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.23750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 72
REMARK 465 ALA A 73
REMARK 465 GLY A 74
REMARK 465 HIS A 75
REMARK 465 MET A 76
REMARK 465 ALA A 77
REMARK 465 SER A 78
REMARK 465 PRO A 79
REMARK 465 SER A 80
REMARK 465 GLU A 81
REMARK 465 ASN A 82
REMARK 465 LEU A 83
REMARK 465 SER A 84
REMARK 465 ARG A 85
REMARK 465 LYS A 86
REMARK 465 ALA A 87
REMARK 465 LYS A 88
REMARK 465 LYS A 89
REMARK 465 LYS A 90
REMARK 465 ALA A 91
REMARK 465 ILE A 92
REMARK 465 GLN A 93
REMARK 465 GLN A 94
REMARK 465 THR A 571
REMARK 465 PRO A 572
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 VAL A 128 CG1 CG2
REMARK 470 SER A 569 OG
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 TRP A 563 CE2 TRP A 563 CD2 0.073
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 ALA A 148 98.74 -68.65
REMARK 500 GLU A 150 -36.78 -139.65
REMARK 500 SER A 152 152.07 -41.98
REMARK 500 ARG A 277 -56.69 76.37
REMARK 500 ARG A 277 -54.54 74.65
REMARK 500 HIS A 321 -33.25 -131.63
REMARK 500 ALA A 447 16.72 -64.89
REMARK 500 SER A 506 -74.97 -96.14
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 A 108 LYS A 109 144.00
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 ZN A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 344 SG
REMARK 620 2 CYS A 347 SG 114.6
REMARK 620 3 HIS A 548 NE2 108.6 99.2
REMARK 620 4 CYS A 565 SG 107.9 113.2 113.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1002 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 475 OD1
REMARK 620 2 ACA A1004 OXT 169.2
REMARK 620 3 ACA A1004 OXT 166.1 23.1
REMARK 620 4 ACA A1004 O 123.2 54.6 51.5
REMARK 620 5 HOH A1218 O 91.3 98.1 75.1 77.5
REMARK 620 6 HOH A1414 O 93.4 91.8 89.8 141.2 90.5
REMARK 620 7 HOH A1423 O 97.0 73.4 96.4 94.8 170.9 92.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1003 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 475 OD2
REMARK 620 2 ASP A 493 OD2 106.0
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 ZN A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACA A 1004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G23 RELATED DB: PDB
REMARK 900 RELATED ID: 4G26 RELATED DB: PDB
REMARK 900 RELATED ID: 4G25 RELATED DB: PDB
DBREF 4G24 A 77 572 UNP Q66GI4 PP179_ARATH 77 572
SEQADV 4G24 GLY A 72 UNP Q66GI4 EXPRESSION TAG
SEQADV 4G24 ALA A 73 UNP Q66GI4 EXPRESSION TAG
SEQADV 4G24 GLY A 74 UNP Q66GI4 EXPRESSION TAG
SEQADV 4G24 HIS A 75 UNP Q66GI4 EXPRESSION TAG
SEQADV 4G24 MET A 76 UNP Q66GI4 EXPRESSION TAG
SEQRES 1 A 501 GLY ALA GLY HIS MET ALA SER PRO SER GLU ASN LEU SER
SEQRES 2 A 501 ARG LYS ALA LYS LYS LYS ALA ILE GLN GLN SER PRO GLU
SEQRES 3 A 501 ALA LEU LEU LYS GLN LYS LEU ASP MET CYS SER LYS LYS
SEQRES 4 A 501 GLY ASP VAL LEU GLU ALA LEU ARG LEU TYR ASP GLU ALA
SEQRES 5 A 501 ARG ARG ASN GLY VAL GLN LEU SER GLN TYR HIS TYR ASN
SEQRES 6 A 501 VAL LEU LEU TYR VAL CYS SER LEU ALA GLU ALA ALA THR
SEQRES 7 A 501 GLU SER SER PRO ASN PRO GLY LEU SER ARG GLY PHE ASP
SEQRES 8 A 501 ILE PHE LYS GLN MET ILE VAL ASP LYS VAL VAL PRO ASN
SEQRES 9 A 501 GLU ALA THR PHE THR ASN GLY ALA ARG LEU ALA VAL ALA
SEQRES 10 A 501 LYS ASP ASP PRO GLU MET ALA PHE ASP MET VAL LYS GLN
SEQRES 11 A 501 MET LYS ALA PHE GLY ILE GLN PRO ARG LEU ARG SER TYR
SEQRES 12 A 501 GLY PRO ALA LEU PHE GLY PHE CYS ARG LYS GLY ASP ALA
SEQRES 13 A 501 ASP LYS ALA TYR GLU VAL ASP ALA HIS MET VAL GLU SER
SEQRES 14 A 501 GLU VAL VAL PRO GLU GLU PRO GLU LEU ALA ALA LEU LEU
SEQRES 15 A 501 LYS VAL SER MET ASP THR LYS ASN ALA ASP LYS VAL TYR
SEQRES 16 A 501 LYS THR LEU GLN ARG LEU ARG ASP LEU VAL ARG GLN VAL
SEQRES 17 A 501 SER LYS SER THR PHE ASP MET ILE GLU GLU TRP PHE LYS
SEQRES 18 A 501 SER GLU VAL ALA THR LYS THR GLY VAL LYS LYS TRP ASP
SEQRES 19 A 501 VAL LYS LYS ILE ARG ASP ALA VAL VAL SER GLY GLY GLY
SEQRES 20 A 501 GLY TRP HIS GLY GLN GLY TRP LEU GLY THR GLY LYS TRP
SEQRES 21 A 501 ASN VAL LYS ARG THR GLU MET ASP GLU ASN GLY VAL CYS
SEQRES 22 A 501 LYS CYS CYS LYS GLU LYS LEU VAL CYS ILE ASP ILE ASN
SEQRES 23 A 501 PRO VAL GLU THR GLU THR PHE ALA ALA SER LEU THR ARG
SEQRES 24 A 501 LEU ALA CYS GLU ARG GLU VAL LYS ALA ASN PHE ASN GLN
SEQRES 25 A 501 PHE GLN GLU TRP LEU GLU ARG HIS GLY PRO PHE ASP ALA
SEQRES 26 A 501 VAL ILE ASP GLY ALA ASN MET GLY LEU VAL ASN GLN ARG
SEQRES 27 A 501 SER PHE SER PHE PHE GLN LEU ASN ASN THR VAL GLN ARG
SEQRES 28 A 501 CYS GLN GLN ILE SER PRO SER LYS ARG LEU PRO LEU VAL
SEQRES 29 A 501 ILE LEU HIS LYS SER ARG VAL ASN GLY GLY PRO ALA THR
SEQRES 30 A 501 TYR PRO LYS ASN ARG ALA LEU LEU GLU LYS TRP LYS ASN
SEQRES 31 A 501 ALA GLY ALA LEU TYR ALA THR PRO PRO GLY SER ASN ASP
SEQRES 32 A 501 ASP TRP TYR TRP LEU TYR ALA ALA VAL SER CYS LYS CYS
SEQRES 33 A 501 LEU LEU VAL THR ASN ASP GLU MET ARG ASP HIS LEU PHE
SEQRES 34 A 501 GLN LEU LEU GLY ASN SER PHE PHE PRO ARG TRP LYS GLU
SEQRES 35 A 501 LYS HIS GLN VAL ARG ILE SER VAL THR ARG GLU ASP GLY
SEQRES 36 A 501 LEU LYS LEU ASN MET PRO PRO PRO TYR SER ILE VAL ILE
SEQRES 37 A 501 GLN GLU SER GLU ASP GLY THR TRP HIS VAL PRO MET SER
SEQRES 38 A 501 VAL GLU ASP ASP LEU GLN THR SER ARG GLN TRP LEU CYS
SEQRES 39 A 501 ALA LYS ARG SER LYS THR PRO
HET ZN A1001 1
HET MN A1002 1
HET MN A1003 1
HET ACA A1004 18
HETNAM ZN ZINC ION
HETNAM MN MANGANESE (II) ION
HETNAM ACA 6-AMINOHEXANOIC ACID
HETSYN ACA AMINOCAPROIC ACID
FORMUL 2 ZN ZN 2+
FORMUL 3 MN 2(MN 2+)
FORMUL 5 ACA C6 H13 N O2
FORMUL 6 HOH *330(H2 O)
HELIX 1 1 SER A 95 CYS A 107 1 13
HELIX 2 2 ASP A 112 ASN A 126 1 15
HELIX 3 3 SER A 131 SER A 143 1 13
HELIX 4 4 ASN A 154 ASP A 170 1 17
HELIX 5 5 ASN A 175 ASP A 190 1 16
HELIX 6 6 ASP A 191 PHE A 205 1 15
HELIX 7 7 ARG A 210 LYS A 224 1 15
HELIX 8 8 ASP A 226 SER A 240 1 15
HELIX 9 9 GLU A 245 THR A 259 1 15
HELIX 10 10 ASN A 261 VAL A 276 1 16
HELIX 11 11 SER A 280 SER A 293 1 14
HELIX 12 12 SER A 293 THR A 299 1 7
HELIX 13 13 ASP A 305 GLY A 317 1 13
HELIX 14 14 ASN A 357 GLU A 376 1 20
HELIX 15 15 VAL A 377 ARG A 390 1 14
HELIX 16 16 GLY A 400 VAL A 406 1 7
HELIX 17 17 SER A 412 SER A 427 1 16
HELIX 18 18 LYS A 439 ASN A 443 1 5
HELIX 19 19 TYR A 449 ALA A 462 1 14
HELIX 20 20 ASP A 474 LYS A 486 1 13
HELIX 21 21 ASP A 497 LEU A 502 1 6
HELIX 22 22 SER A 506 HIS A 515 1 10
SHEET 1 A 4 TRP A 331 THR A 336 0
SHEET 2 A 4 TRP A 563 ARG A 568 -1 O LYS A 567 N ASN A 332
SHEET 3 A 4 TRP A 547 PRO A 550 -1 N TRP A 547 O ALA A 566
SHEET 4 A 4 GLN A 540 GLU A 541 -1 N GLN A 540 O HIS A 548
SHEET 1 B 6 LEU A 465 THR A 468 0
SHEET 2 B 6 LEU A 434 HIS A 438 1 N VAL A 435 O TYR A 466
SHEET 3 B 6 ALA A 396 ASP A 399 1 N ILE A 398 O LEU A 434
SHEET 4 B 6 LEU A 488 VAL A 490 1 O VAL A 490 N VAL A 397
SHEET 5 B 6 GLN A 516 THR A 522 1 O VAL A 517 N LEU A 489
SHEET 6 B 6 GLY A 526 ASN A 530 -1 O ASN A 530 N ARG A 518
LINK SG CYS A 344 ZN ZN A1001 1555 1555 2.42
LINK SG CYS A 347 ZN ZN A1001 1555 1555 1.94
LINK OD1 ASP A 475 MN MN A1002 1555 1555 2.27
LINK OD2 ASP A 475 MN MN A1003 1555 1555 2.59
LINK OD2 ASP A 493 MN MN A1003 1555 1555 2.30
LINK NE2 HIS A 548 ZN ZN A1001 1555 1555 2.16
LINK SG CYS A 565 ZN ZN A1001 1555 1555 2.30
LINK MN MN A1002 OXTAACA A1004 1555 1555 2.34
LINK MN MN A1002 OXTBACA A1004 1555 1555 2.42
LINK MN MN A1002 O BACA A1004 1555 1555 2.61
LINK MN MN A1002 O HOH A1218 1555 1555 2.14
LINK MN MN A1002 O HOH A1414 1555 1555 2.13
LINK MN MN A1002 O HOH A1423 1555 1555 2.28
CISPEP 1 CYS A 107 SER A 108 0 6.46
CISPEP 2 GLY A 392 PRO A 393 0 6.32
CISPEP 3 GLY A 445 PRO A 446 0 20.07
SITE 1 AC1 4 CYS A 344 CYS A 347 HIS A 548 CYS A 565
SITE 1 AC2 6 ASP A 475 MN A1003 ACA A1004 HOH A1218
SITE 2 AC2 6 HOH A1414 HOH A1423
SITE 1 AC3 5 ASP A 475 ASP A 493 ASP A 497 MN A1002
SITE 2 AC3 5 ACA A1004
SITE 1 AC4 8 ASN A 402 VAL A 406 ASP A 493 MN A1002
SITE 2 AC4 8 MN A1003 HOH A1172 HOH A1218 HOH A1423
CRYST1 41.750 112.475 138.762 90.00 90.00 90.00 P 21 21 21 4
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 0.023952 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008891 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007207 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
