HEADER RNA BINDING PROTEIN 08-AUG-13 4M57
TITLE CRYSTAL STRUCTURE OF THE PENTATRICOPEPTIDE REPEAT PROTEIN PPR10 FROM
TITLE 2 MAIZE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHLOROPLAST PENTATRICOPEPTIDE REPEAT PROTEIN 10;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 61-786;
COMPND 5 SYNONYM: PENTATRICOPEPTIDE REPEAT10;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZEA MAYS;
SOURCE 3 ORGANISM_COMMON: MAIZE;
SOURCE 4 ORGANISM_TAXID: 4577;
SOURCE 5 GENE: PPR10, ZEAMMB73_867042;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PENTATRICOPEPTIDE REPEAT, SUPERHELICAL, RNA BINDING PROTEIN, RNA
EXPDTA X-RAY DIFFRACTION
AUTHOR P.YIN,Q.LI,C.YAN,Y.LIU,N.YAN
REVDAT 3 18-DEC-13 4M57 1 JRNL
REVDAT 2 20-NOV-13 4M57 1 JRNL
REVDAT 1 30-OCT-13 4M57 0
JRNL AUTH P.YIN,Q.LI,C.YAN,Y.LIU,J.LIU,F.YU,Z.WANG,J.LONG,J.HE,
JRNL AUTH 2 H.W.WANG,J.WANG,J.K.ZHU,Y.SHI,N.YAN
JRNL TITL STRUCTURAL BASIS FOR THE MODULAR RECOGNITION OF
JRNL TITL 2 SINGLE-STRANDED RNA BY PPR PROTEINS.
JRNL REF NATURE V. 504 168 2013
JRNL REFN ISSN 0028-0836
JRNL PMID 24162847
JRNL DOI 10.1038/NATURE12651
REMARK 2
REMARK 2 RESOLUTION. 2.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 34666
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1765
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 37.0832 - 6.7129 1.00 2560 125 0.1943 0.2572
REMARK 3 2 6.7129 - 5.3333 1.00 2542 135 0.2882 0.3160
REMARK 3 3 5.3333 - 4.6606 1.00 2552 131 0.2174 0.1823
REMARK 3 4 4.6606 - 4.2351 1.00 2535 152 0.1961 0.2046
REMARK 3 5 4.2351 - 3.9320 1.00 2565 126 0.2117 0.2233
REMARK 3 6 3.9320 - 3.7004 1.00 2538 134 0.2259 0.2577
REMARK 3 7 3.7004 - 3.5152 1.00 2520 160 0.2412 0.2200
REMARK 3 8 3.5152 - 3.3623 1.00 2522 142 0.2729 0.3043
REMARK 3 9 3.3623 - 3.2329 1.00 2535 126 0.2934 0.3233
REMARK 3 10 3.2329 - 3.1214 1.00 2575 129 0.2991 0.2908
REMARK 3 11 3.1214 - 3.0239 1.00 2546 133 0.3107 0.3442
REMARK 3 12 3.0239 - 2.9375 1.00 2516 138 0.3216 0.3091
REMARK 3 13 2.9375 - 2.8602 0.94 2395 134 0.3411 0.3130
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.39
REMARK 3 B_SOL : 54.65
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.350
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) : -0.79000
REMARK 3 B22 (A**2) : -16.67780
REMARK 3 B33 (A**2) : 17.46780
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 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 : 0.019 5423
REMARK 3 ANGLE : 1.318 7353
REMARK 3 CHIRALITY : 0.113 841
REMARK 3 PLANARITY : 0.008 945
REMARK 3 DIHEDRAL : 19.605 1945
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: all
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7092 -2.2218 9.2059
REMARK 3 T TENSOR
REMARK 3 T11: 0.4670 T22: 0.5244
REMARK 3 T33: 0.5729 T12: -0.0122
REMARK 3 T13: 0.0242 T23: 0.0238
REMARK 3 L TENSOR
REMARK 3 L11: -0.1205 L22: 0.4762
REMARK 3 L33: 0.1999 L12: 0.1278
REMARK 3 L13: 0.0243 L23: 0.1931
REMARK 3 S TENSOR
REMARK 3 S11: 0.0271 S12: 0.0434 S13: 0.0606
REMARK 3 S21: 0.0759 S22: -0.0483 S23: 0.0161
REMARK 3 S31: -0.0723 S32: 0.0064 S33: 0.0143
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 4M57 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-13.
REMARK 100 THE RCSB ID CODE IS RCSB081480.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-12
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 : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX325HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M SODIUM FORMATE, 0.1M BIS-TRIS
REMARK 280 PROPANE, 0.04M DTT, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 34.18650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 88.26800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.18650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 88.26800
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
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 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 61
REMARK 465 HIS A 62
REMARK 465 GLN A 63
REMARK 465 THR A 64
REMARK 465 PRO A 65
REMARK 465 THR A 66
REMARK 465 PRO A 67
REMARK 465 PRO A 68
REMARK 465 SER A 554
REMARK 465 GLY A 555
REMARK 465 ALA A 556
REMARK 465 VAL A 557
REMARK 465 PHE A 558
REMARK 465 SER A 764
REMARK 465 GLU A 765
REMARK 465 THR A 766
REMARK 465 ASP A 767
REMARK 465 LEU A 768
REMARK 465 ASP A 769
REMARK 465 PHE A 770
REMARK 465 ASP A 771
REMARK 465 LYS A 772
REMARK 465 GLY A 785
REMARK 465 ARG A 786
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 HIS A 69 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 99 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 276 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 298 CG CD OE1 OE2
REMARK 470 GLU A 307 CG CD OE1 OE2
REMARK 470 LYS A 398 CG CD CE NZ
REMARK 470 LYS A 432 CG CD CE NZ
REMARK 470 ARG A 433 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 452 CG CD OE1 OE2
REMARK 470 ASP A 456 CG OD1 OD2
REMARK 470 ARG A 502 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 522 CG CD CE NZ
REMARK 470 LYS A 573 CG CD CE NZ
REMARK 470 LYS A 588 CG CD CE NZ
REMARK 470 ARG A 624 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 679 CG CD CE NZ
REMARK 470 GLU A 685 CG CD OE1 OE2
REMARK 470 ARG A 722 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 723 CG CD OE1 OE2
REMARK 470 GLN A 730 CG CD OE1 NE2
REMARK 470 LYS A 734 CG CD CE NZ
REMARK 470 GLU A 754 CG CD OE1 OE2
REMARK 470 LYS A 773 CG CD CE NZ
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 OE2 GLU A 581 OH TYR A 606 2.09
REMARK 500 O THR A 518 N GLY A 520 2.19
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 OD2 ASP A 244 O LEU A 733 2555 1.99
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 PRO A 165 C - N - CD ANGL. DEV. = -17.9 DEGREES
REMARK 500 PRO A 488 C - N - CD ANGL. DEV. = -18.0 DEGREES
REMARK 500 PRO A 594 C - N - CD ANGL. DEV. = -17.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 71 -10.23 -147.05
REMARK 500 LEU A 103 -8.37 -59.74
REMARK 500 HIS A 119 47.42 -89.36
REMARK 500 GLU A 133 -162.64 -111.13
REMARK 500 PRO A 167 172.54 -56.86
REMARK 500 ASP A 244 -159.33 -113.75
REMARK 500 ASN A 309 52.26 -104.29
REMARK 500 CYS A 311 -71.22 -61.64
REMARK 500 GLN A 312 92.16 84.28
REMARK 500 PRO A 313 147.23 -39.98
REMARK 500 ASN A 349 -152.64 -71.02
REMARK 500 LYS A 365 97.14 -53.12
REMARK 500 THR A 379 32.39 -71.32
REMARK 500 LYS A 398 -83.85 -63.09
REMARK 500 SER A 399 30.91 158.49
REMARK 500 ARG A 400 21.30 -68.80
REMARK 500 PHE A 401 -65.11 21.91
REMARK 500 SER A 414 -75.37 -35.64
REMARK 500 ALA A 428 56.18 -94.08
REMARK 500 LYS A 432 -149.98 -98.70
REMARK 500 SER A 448 10.19 -65.53
REMARK 500 SER A 449 94.01 -175.18
REMARK 500 VAL A 451 78.53 54.13
REMARK 500 SER A 470 61.94 -63.23
REMARK 500 ALA A 484 12.13 -62.45
REMARK 500 PRO A 488 125.22 -31.13
REMARK 500 CYS A 489 -133.92 -92.43
REMARK 500 ASP A 505 68.56 -101.35
REMARK 500 LYS A 519 23.50 -53.91
REMARK 500 PRO A 523 97.47 -37.85
REMARK 500 ASN A 524 149.72 -17.35
REMARK 500 SER A 560 -137.33 -61.22
REMARK 500 TRP A 561 -37.57 -132.25
REMARK 500 ARG A 590 37.46 -79.04
REMARK 500 TYR A 592 -138.41 -114.94
REMARK 500 ARG A 624 -86.69 -54.22
REMARK 500 SER A 625 -84.31 -26.26
REMARK 500 ASP A 630 -157.82 -114.13
REMARK 500 SER A 645 -1.98 72.62
REMARK 500 CYS A 659 40.66 -109.99
REMARK 500 GLN A 661 -23.76 79.51
REMARK 500 LEU A 682 59.55 -64.79
REMARK 500 GLN A 730 36.43 -63.03
REMARK 500 HIS A 731 0.35 -154.75
REMARK 500 LYS A 734 116.53 74.32
REMARK 500 ARG A 752 66.70 -104.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4M59 RELATED DB: PDB
DBREF 4M57 A 61 786 UNP B8Y6I0 B8Y6I0_MAIZE 61 786
SEQADV 4M57 SER A 256 UNP B8Y6I0 CYS 256 ENGINEERED MUTATION
SEQADV 4M57 SER A 279 UNP B8Y6I0 CYS 279 ENGINEERED MUTATION
SEQADV 4M57 SER A 430 UNP B8Y6I0 CYS 430 ENGINEERED MUTATION
SEQADV 4M57 SER A 449 UNP B8Y6I0 CYS 449 ENGINEERED MUTATION
SEQRES 1 A 726 SER HIS GLN THR PRO THR PRO PRO HIS SER PHE LEU SER
SEQRES 2 A 726 PRO ASP ALA GLN VAL LEU VAL LEU ALA ILE SER SER HIS
SEQRES 3 A 726 PRO LEU PRO THR LEU ALA ALA PHE LEU ALA SER ARG ARG
SEQRES 4 A 726 ASP GLU LEU LEU ARG ALA ASP ILE THR SER LEU LEU LYS
SEQRES 5 A 726 ALA LEU GLU LEU SER GLY HIS TRP GLU TRP ALA LEU ALA
SEQRES 6 A 726 LEU LEU ARG TRP ALA GLY LYS GLU GLY ALA ALA ASP ALA
SEQRES 7 A 726 SER ALA LEU GLU MSE VAL VAL ARG ALA LEU GLY ARG GLU
SEQRES 8 A 726 GLY GLN HIS ASP ALA VAL CYS ALA LEU LEU ASP GLU THR
SEQRES 9 A 726 PRO LEU PRO PRO GLY SER ARG LEU ASP VAL ARG ALA TYR
SEQRES 10 A 726 THR THR VAL LEU HIS ALA LEU SER ARG ALA GLY ARG TYR
SEQRES 11 A 726 GLU ARG ALA LEU GLU LEU PHE ALA GLU LEU ARG ARG GLN
SEQRES 12 A 726 GLY VAL ALA PRO THR LEU VAL THR TYR ASN VAL VAL LEU
SEQRES 13 A 726 ASP VAL TYR GLY ARG MSE GLY ARG SER TRP PRO ARG ILE
SEQRES 14 A 726 VAL ALA LEU LEU ASP GLU MSE ARG ALA ALA GLY VAL GLU
SEQRES 15 A 726 PRO ASP GLY PHE THR ALA SER THR VAL ILE ALA ALA CYS
SEQRES 16 A 726 SER ARG ASP GLY LEU VAL ASP GLU ALA VAL ALA PHE PHE
SEQRES 17 A 726 GLU ASP LEU LYS ALA ARG GLY HIS ALA PRO SER VAL VAL
SEQRES 18 A 726 THR TYR ASN ALA LEU LEU GLN VAL PHE GLY LYS ALA GLY
SEQRES 19 A 726 ASN TYR THR GLU ALA LEU ARG VAL LEU GLY GLU MSE GLU
SEQRES 20 A 726 GLN ASN GLY CYS GLN PRO ASP ALA VAL THR TYR ASN GLU
SEQRES 21 A 726 LEU ALA GLY THR TYR ALA ARG ALA GLY PHE PHE GLU GLU
SEQRES 22 A 726 ALA ALA ARG CYS LEU ASP THR MSE ALA SER LYS GLY LEU
SEQRES 23 A 726 LEU PRO ASN ALA PHE THR TYR ASN THR VAL MSE THR ALA
SEQRES 24 A 726 TYR GLY ASN VAL GLY LYS VAL ASP GLU ALA LEU ALA LEU
SEQRES 25 A 726 PHE ASP GLN MSE LYS LYS THR GLY PHE VAL PRO ASN VAL
SEQRES 26 A 726 ASN THR TYR ASN LEU VAL LEU GLY MSE LEU GLY LYS LYS
SEQRES 27 A 726 SER ARG PHE THR VAL MSE LEU GLU MSE LEU GLY GLU MSE
SEQRES 28 A 726 SER ARG SER GLY CYS THR PRO ASN ARG VAL THR TRP ASN
SEQRES 29 A 726 THR MSE LEU ALA VAL SER GLY LYS ARG GLY MSE GLU ASP
SEQRES 30 A 726 TYR VAL THR ARG VAL LEU GLU GLY MSE ARG SER SER GLY
SEQRES 31 A 726 VAL GLU LEU SER ARG ASP THR TYR ASN THR LEU ILE ALA
SEQRES 32 A 726 ALA TYR GLY ARG CYS GLY SER ARG THR ASN ALA PHE LYS
SEQRES 33 A 726 MSE TYR ASN GLU MSE THR SER ALA GLY PHE THR PRO CYS
SEQRES 34 A 726 ILE THR THR TYR ASN ALA LEU LEU ASN VAL LEU SER ARG
SEQRES 35 A 726 GLN GLY ASP TRP SER THR ALA GLN SER ILE VAL SER LYS
SEQRES 36 A 726 MSE ARG THR LYS GLY PHE LYS PRO ASN GLU GLN SER TYR
SEQRES 37 A 726 SER LEU LEU LEU GLN CYS TYR ALA LYS GLY GLY ASN VAL
SEQRES 38 A 726 ALA GLY ILE ALA ALA ILE GLU ASN GLU VAL TYR GLY SER
SEQRES 39 A 726 GLY ALA VAL PHE PRO SER TRP VAL ILE LEU ARG THR LEU
SEQRES 40 A 726 VAL ILE ALA ASN PHE LYS CYS ARG ARG LEU ASP GLY MSE
SEQRES 41 A 726 GLU THR ALA PHE GLN GLU VAL LYS ALA ARG GLY TYR ASN
SEQRES 42 A 726 PRO ASP LEU VAL ILE PHE ASN SER MSE LEU SER ILE TYR
SEQRES 43 A 726 ALA LYS ASN GLY MSE TYR SER LYS ALA THR GLU VAL PHE
SEQRES 44 A 726 ASP SER ILE LYS ARG SER GLY LEU SER PRO ASP LEU ILE
SEQRES 45 A 726 THR TYR ASN SER LEU MSE ASP MSE TYR ALA LYS CYS SER
SEQRES 46 A 726 GLU SER TRP GLU ALA GLU LYS ILE LEU ASN GLN LEU LYS
SEQRES 47 A 726 CYS SER GLN THR MSE LYS PRO ASP VAL VAL SER TYR ASN
SEQRES 48 A 726 THR VAL ILE ASN GLY PHE CYS LYS GLN GLY LEU VAL LYS
SEQRES 49 A 726 GLU ALA GLN ARG VAL LEU SER GLU MSE VAL ALA ASP GLY
SEQRES 50 A 726 MSE ALA PRO CYS ALA VAL THR TYR HIS THR LEU VAL GLY
SEQRES 51 A 726 GLY TYR SER SER LEU GLU MSE PHE SER GLU ALA ARG GLU
SEQRES 52 A 726 VAL ILE GLY TYR MSE VAL GLN HIS GLY LEU LYS PRO MSE
SEQRES 53 A 726 GLU LEU THR TYR ARG ARG VAL VAL GLU SER TYR CYS ARG
SEQRES 54 A 726 ALA LYS ARG PHE GLU GLU ALA ARG GLY PHE LEU SER GLU
SEQRES 55 A 726 VAL SER GLU THR ASP LEU ASP PHE ASP LYS LYS ALA LEU
SEQRES 56 A 726 GLU ALA TYR ILE GLU ASP ALA GLN PHE GLY ARG
MODRES 4M57 MSE A 143 MET SELENOMETHIONINE
MODRES 4M57 MSE A 222 MET SELENOMETHIONINE
MODRES 4M57 MSE A 236 MET SELENOMETHIONINE
MODRES 4M57 MSE A 306 MET SELENOMETHIONINE
MODRES 4M57 MSE A 341 MET SELENOMETHIONINE
MODRES 4M57 MSE A 357 MET SELENOMETHIONINE
MODRES 4M57 MSE A 376 MET SELENOMETHIONINE
MODRES 4M57 MSE A 394 MET SELENOMETHIONINE
MODRES 4M57 MSE A 404 MET SELENOMETHIONINE
MODRES 4M57 MSE A 407 MET SELENOMETHIONINE
MODRES 4M57 MSE A 411 MET SELENOMETHIONINE
MODRES 4M57 MSE A 426 MET SELENOMETHIONINE
MODRES 4M57 MSE A 435 MET SELENOMETHIONINE
MODRES 4M57 MSE A 446 MET SELENOMETHIONINE
MODRES 4M57 MSE A 477 MET SELENOMETHIONINE
MODRES 4M57 MSE A 481 MET SELENOMETHIONINE
MODRES 4M57 MSE A 516 MET SELENOMETHIONINE
MODRES 4M57 MSE A 580 MET SELENOMETHIONINE
MODRES 4M57 MSE A 602 MET SELENOMETHIONINE
MODRES 4M57 MSE A 611 MET SELENOMETHIONINE
MODRES 4M57 MSE A 638 MET SELENOMETHIONINE
MODRES 4M57 MSE A 640 MET SELENOMETHIONINE
MODRES 4M57 MSE A 663 MET SELENOMETHIONINE
MODRES 4M57 MSE A 693 MET SELENOMETHIONINE
MODRES 4M57 MSE A 698 MET SELENOMETHIONINE
MODRES 4M57 MSE A 717 MET SELENOMETHIONINE
MODRES 4M57 MSE A 728 MET SELENOMETHIONINE
MODRES 4M57 MSE A 736 MET SELENOMETHIONINE
HET MSE A 143 8
HET MSE A 222 8
HET MSE A 236 8
HET MSE A 306 8
HET MSE A 341 8
HET MSE A 357 8
HET MSE A 376 8
HET MSE A 394 8
HET MSE A 404 8
HET MSE A 407 8
HET MSE A 411 8
HET MSE A 426 8
HET MSE A 435 8
HET MSE A 446 8
HET MSE A 477 8
HET MSE A 481 8
HET MSE A 516 8
HET MSE A 580 8
HET MSE A 602 8
HET MSE A 611 8
HET MSE A 638 8
HET MSE A 640 8
HET MSE A 663 8
HET MSE A 693 8
HET MSE A 698 8
HET MSE A 717 8
HET MSE A 728 8
HET MSE A 736 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 28(C5 H11 N O2 SE)
HELIX 1 1 SER A 73 SER A 85 1 13
HELIX 2 2 PRO A 87 PRO A 89 5 3
HELIX 3 3 THR A 90 ARG A 98 1 9
HELIX 4 4 ARG A 98 LEU A 103 1 6
HELIX 5 5 ASP A 106 GLY A 118 1 13
HELIX 6 6 HIS A 119 LYS A 132 1 14
HELIX 7 7 ASP A 137 GLU A 151 1 15
HELIX 8 8 GLN A 153 THR A 164 1 12
HELIX 9 9 PRO A 168 LEU A 172 5 5
HELIX 10 10 ASP A 173 ALA A 176 5 4
HELIX 11 11 TYR A 177 ALA A 187 1 11
HELIX 12 12 ARG A 189 ARG A 202 1 14
HELIX 13 13 THR A 208 GLY A 223 1 16
HELIX 14 14 SER A 225 ALA A 239 1 15
HELIX 15 15 ASP A 244 GLY A 259 1 16
HELIX 16 16 LEU A 260 ARG A 274 1 15
HELIX 17 17 SER A 279 GLY A 294 1 16
HELIX 18 18 ASN A 295 ASN A 309 1 15
HELIX 19 19 ASP A 314 GLY A 329 1 16
HELIX 20 20 PHE A 330 LYS A 344 1 15
HELIX 21 21 ALA A 350 GLY A 364 1 15
HELIX 22 22 VAL A 366 THR A 379 1 14
HELIX 23 23 ASN A 384 SER A 399 1 16
HELIX 24 24 ARG A 400 GLY A 415 1 16
HELIX 25 25 ASN A 419 LEU A 427 1 9
HELIX 26 26 GLY A 434 SER A 448 1 15
HELIX 27 27 SER A 454 ARG A 467 1 14
HELIX 28 28 SER A 470 ALA A 484 1 15
HELIX 29 29 CYS A 489 LEU A 500 1 12
HELIX 30 30 ASP A 505 LYS A 519 1 15
HELIX 31 31 ASN A 524 GLY A 538 1 15
HELIX 32 32 ASN A 540 TYR A 552 1 13
HELIX 33 33 TRP A 561 CYS A 574 1 14
HELIX 34 34 ARG A 576 ARG A 590 1 15
HELIX 35 35 ASP A 595 ASN A 609 1 15
HELIX 36 36 MSE A 611 GLY A 626 1 16
HELIX 37 37 ASP A 630 CYS A 644 1 15
HELIX 38 38 TRP A 648 CYS A 659 1 12
HELIX 39 39 ASP A 666 GLN A 680 1 15
HELIX 40 40 LEU A 682 ASP A 696 1 15
HELIX 41 41 CYS A 701 LEU A 715 1 15
HELIX 42 42 MSE A 717 GLN A 730 1 14
HELIX 43 43 MSE A 736 ALA A 750 1 15
HELIX 44 44 ARG A 752 VAL A 763 1 12
HELIX 45 45 ALA A 774 PHE A 784 1 11
LINK C GLU A 142 N MSE A 143 1555 1555 1.33
LINK C MSE A 143 N VAL A 144 1555 1555 1.33
LINK C ARG A 221 N MSE A 222 1555 1555 1.33
LINK C MSE A 222 N GLY A 223 1555 1555 1.33
LINK C GLU A 235 N MSE A 236 1555 1555 1.33
LINK C MSE A 236 N ARG A 237 1555 1555 1.33
LINK C GLU A 305 N MSE A 306 1555 1555 1.33
LINK C MSE A 306 N GLU A 307 1555 1555 1.33
LINK C THR A 340 N MSE A 341 1555 1555 1.33
LINK C MSE A 341 N ALA A 342 1555 1555 1.33
LINK C VAL A 356 N MSE A 357 1555 1555 1.33
LINK C MSE A 357 N THR A 358 1555 1555 1.33
LINK C GLN A 375 N MSE A 376 1555 1555 1.33
LINK C MSE A 376 N LYS A 377 1555 1555 1.33
LINK C GLY A 393 N MSE A 394 1555 1555 1.31
LINK C MSE A 394 N LEU A 395 1555 1555 1.33
LINK C VAL A 403 N MSE A 404 1555 1555 1.33
LINK C MSE A 404 N LEU A 405 1555 1555 1.33
LINK C GLU A 406 N MSE A 407 1555 1555 1.33
LINK C MSE A 407 N LEU A 408 1555 1555 1.33
LINK C GLU A 410 N MSE A 411 1555 1555 1.33
LINK C MSE A 411 N SER A 412 1555 1555 1.33
LINK C THR A 425 N MSE A 426 1555 1555 1.33
LINK C MSE A 426 N LEU A 427 1555 1555 1.33
LINK C GLY A 434 N MSE A 435 1555 1555 1.31
LINK C MSE A 435 N GLU A 436 1555 1555 1.31
LINK C GLY A 445 N MSE A 446 1555 1555 1.33
LINK C MSE A 446 N ARG A 447 1555 1555 1.32
LINK C LYS A 476 N MSE A 477 1555 1555 1.33
LINK C MSE A 477 N TYR A 478 1555 1555 1.33
LINK C GLU A 480 N MSE A 481 1555 1555 1.33
LINK C MSE A 481 N THR A 482 1555 1555 1.33
LINK C LYS A 515 N MSE A 516 1555 1555 1.33
LINK C MSE A 516 N ARG A 517 1555 1555 1.33
LINK C GLY A 579 N MSE A 580 1555 1555 1.33
LINK C MSE A 580 N GLU A 581 1555 1555 1.33
LINK C SER A 601 N MSE A 602 1555 1555 1.33
LINK C MSE A 602 N LEU A 603 1555 1555 1.33
LINK C GLY A 610 N MSE A 611 1555 1555 1.33
LINK C MSE A 611 N TYR A 612 1555 1555 1.33
LINK C LEU A 637 N MSE A 638 1555 1555 1.33
LINK C MSE A 638 N ASP A 639 1555 1555 1.33
LINK C ASP A 639 N MSE A 640 1555 1555 1.33
LINK C MSE A 640 N TYR A 641 1555 1555 1.33
LINK C THR A 662 N MSE A 663 1555 1555 1.33
LINK C MSE A 663 N LYS A 664 1555 1555 1.33
LINK C GLU A 692 N MSE A 693 1555 1555 1.33
LINK C MSE A 693 N VAL A 694 1555 1555 1.33
LINK C GLY A 697 N MSE A 698 1555 1555 1.33
LINK C MSE A 698 N ALA A 699 1555 1555 1.33
LINK C GLU A 716 N MSE A 717 1555 1555 1.33
LINK C MSE A 717 N PHE A 718 1555 1555 1.33
LINK C TYR A 727 N MSE A 728 1555 1555 1.33
LINK C MSE A 728 N VAL A 729 1555 1555 1.33
LINK C PRO A 735 N MSE A 736 1555 1555 1.33
LINK C MSE A 736 N GLU A 737 1555 1555 1.32
CRYST1 68.373 176.536 64.533 90.00 90.00 90.00 P 21 21 2 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 0.014626 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005665 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015496 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
