HEADER TRANSCRIPTION 13-JAN-17 5WYI
TITLE THE YAF9 YEATS DOMAIN RECOGNIZING H3K122SUC PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: YAF9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 8-169;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: YAF9;
COMPND 9 CHAIN: B, C;
COMPND 10 FRAGMENT: UNP RESIDUES 8-169;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: ILE-MET-PRO-LYS-ASP-ILE-GLN-LEU;
COMPND 15 CHAIN: E;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN RM11-1A);
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 285006;
SOURCE 5 STRAIN: RM11-1A;
SOURCE 6 GENE: SCRG_03242;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI-PICHIA PASTORIS SHUTTLE VECTOR
SOURCE 8 PPPARG4;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 1182032;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN RM11-1A);
SOURCE 12 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 13 ORGANISM_TAXID: 285006;
SOURCE 14 STRAIN: RM11-1A;
SOURCE 15 GENE: SCRG_03242;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI-PICHIA PASTORIS SHUTTLE VECTOR
SOURCE 17 PPPARG4;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 1182032;
SOURCE 19 MOL_ID: 3;
SOURCE 20 SYNTHETIC: YES;
SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 22 ORGANISM_TAXID: 9606
KEYWDS YEATS DOMAIN, SUCCINYLATION, TRANSCRIPTIONAL FACTOR, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.WANG,Q.HAO
REVDAT 1 17-JAN-18 5WYI 0
JRNL AUTH Y.WANG,Q.HAO
JRNL TITL THE YAF9 YEATS DOMAIN RECOGNIZING H3K122SUC PEPTIDE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 36911
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1864
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 39.5366 - 4.7003 1.00 2711 154 0.1872 0.1946
REMARK 3 2 4.7003 - 3.7317 1.00 2669 151 0.1657 0.1604
REMARK 3 3 3.7317 - 3.2602 1.00 2714 129 0.1810 0.2627
REMARK 3 4 3.2602 - 2.9623 1.00 2722 154 0.1983 0.2331
REMARK 3 5 2.9623 - 2.7500 1.00 2763 124 0.2159 0.2183
REMARK 3 6 2.7500 - 2.5879 1.00 2657 156 0.2159 0.2563
REMARK 3 7 2.5879 - 2.4583 1.00 2737 145 0.2207 0.2314
REMARK 3 8 2.4583 - 2.3513 1.00 2692 140 0.2206 0.2481
REMARK 3 9 2.3513 - 2.2608 1.00 2728 141 0.2188 0.2572
REMARK 3 10 2.2608 - 2.1828 1.00 2641 141 0.2226 0.2421
REMARK 3 11 2.1828 - 2.1145 1.00 2773 150 0.2323 0.2668
REMARK 3 12 2.1145 - 2.0541 0.99 2693 132 0.2275 0.2627
REMARK 3 13 2.0541 - 2.0000 0.95 2547 147 0.2501 0.2922
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.930
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5WYI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1300002603.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39259
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: 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 (%): 49.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M BIS-TRIS
REMARK 280 PH 5.5, 25% PEG 3,350, VAPOR DIFFUSION, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 441 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 TYR A 120
REMARK 465 ALA A 121
REMARK 465 ASN A 122
REMARK 465 PRO A 123
REMARK 465 VAL A 124
REMARK 465 PRO A 125
REMARK 465 ASN A 126
REMARK 465 SER A 127
REMARK 465 ASP A 128
REMARK 465 ASN A 129
REMARK 465 GLY A 130
REMARK 465 ASN A 131
REMARK 465 GLU A 132
REMARK 465 GLN A 133
REMARK 465 ASN A 134
REMARK 465 THR A 135
REMARK 465 THR A 136
REMARK 465 ASP A 137
REMARK 465 HIS A 138
REMARK 465 ASN A 139
REMARK 465 SER A 140
REMARK 465 LYS A 141
REMARK 465 ASP A 142
REMARK 465 ALA A 143
REMARK 465 PRO B 33
REMARK 465 ASN B 34
REMARK 465 TYR B 120
REMARK 465 ALA B 121
REMARK 465 ASN B 122
REMARK 465 PRO B 123
REMARK 465 VAL B 124
REMARK 465 PRO B 125
REMARK 465 ASN B 126
REMARK 465 SER B 127
REMARK 465 ASP B 128
REMARK 465 ASN B 129
REMARK 465 GLY B 130
REMARK 465 ASN B 131
REMARK 465 GLU B 132
REMARK 465 GLN B 133
REMARK 465 ASN B 134
REMARK 465 THR B 135
REMARK 465 THR B 136
REMARK 465 ASP B 137
REMARK 465 HIS B 138
REMARK 465 ASN B 139
REMARK 465 SER B 140
REMARK 465 LYS B 141
REMARK 465 ASP B 142
REMARK 465 ALA B 143
REMARK 465 GLY C 28
REMARK 465 SER C 29
REMARK 465 VAL C 30
REMARK 465 LYS C 31
REMARK 465 PRO C 32
REMARK 465 PRO C 33
REMARK 465 ASN C 34
REMARK 465 TYR C 120
REMARK 465 ALA C 121
REMARK 465 ASN C 122
REMARK 465 PRO C 123
REMARK 465 VAL C 124
REMARK 465 PRO C 125
REMARK 465 ASN C 126
REMARK 465 SER C 127
REMARK 465 ASP C 128
REMARK 465 ASN C 129
REMARK 465 GLY C 130
REMARK 465 ASN C 131
REMARK 465 GLU C 132
REMARK 465 GLN C 133
REMARK 465 ASN C 134
REMARK 465 THR C 135
REMARK 465 THR C 136
REMARK 465 ASP C 137
REMARK 465 HIS C 138
REMARK 465 ASN C 139
REMARK 465 SER C 140
REMARK 465 LYS C 141
REMARK 465 ASP C 142
REMARK 465 ALA C 143
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 205 O HOH B 324 1.72
REMARK 500 O HOH B 304 O HOH B 324 1.83
REMARK 500 O HOH B 310 O HOH B 318 1.84
REMARK 500 OE1 GLU A 161 O HOH A 201 1.89
REMARK 500 O HOH C 308 O HOH C 353 1.91
REMARK 500 OE1 GLU C 38 O HOH C 301 1.95
REMARK 500 O HOH C 349 O HOH C 384 1.97
REMARK 500 O HOH C 413 O HOH C 428 1.99
REMARK 500 O HOH A 204 O HOH A 285 1.99
REMARK 500 O HOH A 204 O HOH A 335 2.04
REMARK 500 O HOH A 253 O HOH A 290 2.04
REMARK 500 O HOH B 264 O HOH B 266 2.06
REMARK 500 O HOH B 309 O HOH B 321 2.06
REMARK 500 NH1 ARG C 8 O HOH C 302 2.07
REMARK 500 O HOH C 301 O HOH C 328 2.07
REMARK 500 NE ARG C 8 O HOH C 303 2.07
REMARK 500 O HOH A 239 O HOH A 321 2.07
REMARK 500 NZ LYS E 1 C2 SIN E 101 2.08
REMARK 500 O HOH B 296 O HOH B 350 2.09
REMARK 500 OD2 ASP C 68 O HOH C 304 2.10
REMARK 500 O ARG C 169 O HOH C 305 2.10
REMARK 500 O HOH C 414 O HOH C 420 2.10
REMARK 500 O PRO B 32 O HOH B 201 2.10
REMARK 500 O HOH A 242 O HOH A 266 2.12
REMARK 500 OE2 GLU B 83 O HOH B 202 2.13
REMARK 500 OE1 GLU C 157 O HOH C 306 2.13
REMARK 500 N ALA B 35 O HOH B 203 2.14
REMARK 500 O HOH C 376 O HOH C 425 2.15
REMARK 500 O HOH C 305 O HOH C 351 2.15
REMARK 500 NE2 GLN E 4 O HOH E 201 2.16
REMARK 500 O GLU B 78 O HOH B 204 2.18
REMARK 500 O HOH A 210 O HOH A 330 2.18
REMARK 500 O HOH A 330 O HOH A 336 2.19
REMARK 500 CE LYS E 1 C1 SIN E 101 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 O HOH A 334 O HOH A 337 1554 1.89
REMARK 500 O HOH C 303 O HOH C 416 3555 1.92
REMARK 500 O HOH C 355 O HOH C 422 1554 1.96
REMARK 500 O HOH B 313 O HOH B 332 1554 1.99
REMARK 500 O HOH B 322 O HOH B 340 3665 2.09
REMARK 500 O HOH B 339 O HOH B 350 1556 2.09
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 LYS E 1 O - C - N ANGL. DEV. = -11.2 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 ASP A 151 -160.42 -114.56
REMARK 500 ASP B 151 -160.20 -115.01
REMARK 500 ASP C 151 -160.44 -114.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LYS E 1 20.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 353 DISTANCE = 5.85 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 SLL C 201
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SLL C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide SIN E 101 and LYS E
REMARK 800 1
DBREF 5WYI A 8 169 UNP B3LNW5 B3LNW5_YEAS1 8 169
DBREF 5WYI B 8 169 UNP B3LNW5 B3LNW5_YEAS1 8 169
DBREF 5WYI C 8 169 UNP B3LNW5 B3LNW5_YEAS1 8 169
DBREF 5WYI E -2 5 PDB 5WYI 5WYI -2 5
SEQADV 5WYI GLY A 6 UNP B3LNW5 EXPRESSION TAG
SEQADV 5WYI ALA A 7 UNP B3LNW5 EXPRESSION TAG
SEQADV 5WYI TYR A 57 UNP B3LNW5 HIS 57 ENGINEERED MUTATION
SEQADV 5WYI LYS A 60 UNP B3LNW5 THR 60 ENGINEERED MUTATION
SEQADV 5WYI SER A 76 UNP B3LNW5 TYR 76 ENGINEERED MUTATION
SEQADV 5WYI GLY A 170 UNP B3LNW5 EXPRESSION TAG
SEQADV 5WYI GLY B 6 UNP B3LNW5 EXPRESSION TAG
SEQADV 5WYI ALA B 7 UNP B3LNW5 EXPRESSION TAG
SEQADV 5WYI TYR B 57 UNP B3LNW5 HIS 57 ENGINEERED MUTATION
SEQADV 5WYI LYS B 60 UNP B3LNW5 THR 60 ENGINEERED MUTATION
SEQADV 5WYI SER B 76 UNP B3LNW5 TYR 76 ENGINEERED MUTATION
SEQADV 5WYI GLY C 6 UNP B3LNW5 EXPRESSION TAG
SEQADV 5WYI ALA C 7 UNP B3LNW5 EXPRESSION TAG
SEQADV 5WYI TYR C 57 UNP B3LNW5 HIS 57 ENGINEERED MUTATION
SEQADV 5WYI LYS C 60 UNP B3LNW5 THR 60 ENGINEERED MUTATION
SEQADV 5WYI SER C 76 UNP B3LNW5 TYR 76 ENGINEERED MUTATION
SEQRES 1 A 165 GLY ALA ARG ILE LYS THR LEU SER VAL SER ARG PRO ILE
SEQRES 2 A 165 ILE TYR GLY ASN THR ALA LYS LYS MET GLY SER VAL LYS
SEQRES 3 A 165 PRO PRO ASN ALA PRO ALA GLU HIS THR HIS LEU TRP THR
SEQRES 4 A 165 ILE PHE VAL ARG GLY PRO GLN ASN GLU ASP ILE SER TYR
SEQRES 5 A 165 PHE ILE LYS LYS VAL VAL PHE LYS LEU HIS ASP THR TYR
SEQRES 6 A 165 PRO ASN PRO VAL ARG SER ILE GLU ALA PRO PRO PHE GLU
SEQRES 7 A 165 LEU THR GLU THR GLY TRP GLY GLU PHE ASP ILE ASN ILE
SEQRES 8 A 165 LYS VAL TYR PHE VAL GLU GLU ALA ASN GLU LYS VAL LEU
SEQRES 9 A 165 ASN PHE TYR HIS ARG LEU ARG LEU HIS PRO TYR ALA ASN
SEQRES 10 A 165 PRO VAL PRO ASN SER ASP ASN GLY ASN GLU GLN ASN THR
SEQRES 11 A 165 THR ASP HIS ASN SER LYS ASP ALA GLU VAL SER SER VAL
SEQRES 12 A 165 TYR PHE ASP GLU ILE VAL PHE ASN GLU PRO ASN GLU GLU
SEQRES 13 A 165 PHE PHE LYS ILE LEU MET SER ARG GLY
SEQRES 1 B 164 GLY ALA ARG ILE LYS THR LEU SER VAL SER ARG PRO ILE
SEQRES 2 B 164 ILE TYR GLY ASN THR ALA LYS LYS MET GLY SER VAL LYS
SEQRES 3 B 164 PRO PRO ASN ALA PRO ALA GLU HIS THR HIS LEU TRP THR
SEQRES 4 B 164 ILE PHE VAL ARG GLY PRO GLN ASN GLU ASP ILE SER TYR
SEQRES 5 B 164 PHE ILE LYS LYS VAL VAL PHE LYS LEU HIS ASP THR TYR
SEQRES 6 B 164 PRO ASN PRO VAL ARG SER ILE GLU ALA PRO PRO PHE GLU
SEQRES 7 B 164 LEU THR GLU THR GLY TRP GLY GLU PHE ASP ILE ASN ILE
SEQRES 8 B 164 LYS VAL TYR PHE VAL GLU GLU ALA ASN GLU LYS VAL LEU
SEQRES 9 B 164 ASN PHE TYR HIS ARG LEU ARG LEU HIS PRO TYR ALA ASN
SEQRES 10 B 164 PRO VAL PRO ASN SER ASP ASN GLY ASN GLU GLN ASN THR
SEQRES 11 B 164 THR ASP HIS ASN SER LYS ASP ALA GLU VAL SER SER VAL
SEQRES 12 B 164 TYR PHE ASP GLU ILE VAL PHE ASN GLU PRO ASN GLU GLU
SEQRES 13 B 164 PHE PHE LYS ILE LEU MET SER ARG
SEQRES 1 C 164 GLY ALA ARG ILE LYS THR LEU SER VAL SER ARG PRO ILE
SEQRES 2 C 164 ILE TYR GLY ASN THR ALA LYS LYS MET GLY SER VAL LYS
SEQRES 3 C 164 PRO PRO ASN ALA PRO ALA GLU HIS THR HIS LEU TRP THR
SEQRES 4 C 164 ILE PHE VAL ARG GLY PRO GLN ASN GLU ASP ILE SER TYR
SEQRES 5 C 164 PHE ILE LYS LYS VAL VAL PHE LYS LEU HIS ASP THR TYR
SEQRES 6 C 164 PRO ASN PRO VAL ARG SER ILE GLU ALA PRO PRO PHE GLU
SEQRES 7 C 164 LEU THR GLU THR GLY TRP GLY GLU PHE ASP ILE ASN ILE
SEQRES 8 C 164 LYS VAL TYR PHE VAL GLU GLU ALA ASN GLU LYS VAL LEU
SEQRES 9 C 164 ASN PHE TYR HIS ARG LEU ARG LEU HIS PRO TYR ALA ASN
SEQRES 10 C 164 PRO VAL PRO ASN SER ASP ASN GLY ASN GLU GLN ASN THR
SEQRES 11 C 164 THR ASP HIS ASN SER LYS ASP ALA GLU VAL SER SER VAL
SEQRES 12 C 164 TYR PHE ASP GLU ILE VAL PHE ASN GLU PRO ASN GLU GLU
SEQRES 13 C 164 PHE PHE LYS ILE LEU MET SER ARG
SEQRES 1 E 8 ILE MET PRO LYS ASP ILE GLN LEU
HET SLL C 201 16
HET SIN E 101 7
HETNAM SLL (2S)-2-AZANYL-6-[(4-HYDROXY-4-OXO-BUTANOYL)
HETNAM 2 SLL AMINO]HEXANOIC ACID
HETNAM SIN SUCCINIC ACID
HETSYN SLL 6-N-SUCCINYL-L-LYSINE
FORMUL 5 SLL C10 H18 N2 O5
FORMUL 6 SIN C4 H6 O4
FORMUL 7 HOH *478(H2 O)
HELIX 1 AA1 GLY A 49 GLU A 53 5 5
HELIX 2 AA2 GLU A 102 ASN A 105 5 4
HELIX 3 AA3 ASN A 159 MET A 167 1 9
HELIX 4 AA4 GLY B 49 GLU B 53 5 5
HELIX 5 AA5 GLU B 102 ASN B 105 5 4
HELIX 6 AA6 ASN B 159 MET B 167 1 9
HELIX 7 AA7 GLY C 49 GLU C 53 5 5
HELIX 8 AA8 GLU C 102 ASN C 105 5 4
HELIX 9 AA9 ASN C 159 SER C 168 1 10
SHEET 1 AA1 4 PHE A 82 GLY A 88 0
SHEET 2 AA1 4 HIS A 41 ARG A 48 -1 N TRP A 43 O GLU A 86
SHEET 3 AA1 4 SER A 13 LYS A 26 -1 N ILE A 19 O ARG A 48
SHEET 4 AA1 4 VAL A 145 ASN A 156 -1 O TYR A 149 N TYR A 20
SHEET 1 AA2 4 VAL A 74 ILE A 77 0
SHEET 2 AA2 4 ILE A 59 LYS A 65 -1 N PHE A 64 O ARG A 75
SHEET 3 AA2 4 ASP A 93 PHE A 100 -1 O ASN A 95 N LYS A 65
SHEET 4 AA2 4 LEU A 109 ARG A 114 -1 O HIS A 113 N ILE A 94
SHEET 1 AA3 4 PHE B 82 GLY B 88 0
SHEET 2 AA3 4 HIS B 41 ARG B 48 -1 N TRP B 43 O GLU B 86
SHEET 3 AA3 4 SER B 13 LYS B 26 -1 N ILE B 19 O ARG B 48
SHEET 4 AA3 4 VAL B 145 ASN B 156 -1 O TYR B 149 N TYR B 20
SHEET 1 AA4 4 VAL B 74 ILE B 77 0
SHEET 2 AA4 4 ILE B 59 LYS B 65 -1 N PHE B 64 O ARG B 75
SHEET 3 AA4 4 ASP B 93 PHE B 100 -1 O TYR B 99 N LYS B 61
SHEET 4 AA4 4 LEU B 109 ARG B 114 -1 O HIS B 113 N ILE B 94
SHEET 1 AA5 4 PHE C 82 GLY C 88 0
SHEET 2 AA5 4 HIS C 41 ARG C 48 -1 N HIS C 41 O GLY C 88
SHEET 3 AA5 4 SER C 13 LYS C 26 -1 N ILE C 19 O ARG C 48
SHEET 4 AA5 4 VAL C 145 ASN C 156 -1 O TYR C 149 N TYR C 20
SHEET 1 AA6 4 VAL C 74 ILE C 77 0
SHEET 2 AA6 4 ILE C 59 LYS C 65 -1 N PHE C 64 O ARG C 75
SHEET 3 AA6 4 ASP C 93 PHE C 100 -1 O ASN C 95 N LYS C 65
SHEET 4 AA6 4 LEU C 109 ARG C 114 -1 O HIS C 113 N ILE C 94
LINK NZ LYS E 1 C1 SIN E 101 1555 1555 1.43
CISPEP 1 PRO A 80 PRO A 81 0 -0.81
CISPEP 2 PRO B 80 PRO B 81 0 -0.52
CISPEP 3 PRO C 80 PRO C 81 0 -0.88
SITE 1 AC1 7 HIS C 39 HIS C 67 THR C 69 TYR C 70
SITE 2 AC1 7 GLY C 88 TRP C 89 GLU C 91
SITE 1 AC2 11 HIS B 39 HIS B 67 THR B 69 TYR B 70
SITE 2 AC2 11 GLY B 88 TRP B 89 GLU B 91 PRO E 0
SITE 3 AC2 11 ASP E 2 HOH E 203 HOH E 207
CRYST1 136.932 136.932 26.168 90.00 90.00 120.00 P 3 6
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 0.007303 0.004216 0.000000 0.00000
SCALE2 0.000000 0.008433 0.000000 0.00000
SCALE3 0.000000 0.000000 0.038215 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
