HEADER RNA BINDING PROTEIN 05-FEB-13 4J37
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN PUS1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRNA PSEUDOURIDINE SYNTHASE A, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 79-408);
COMPND 5 SYNONYM: TRNA PSEUDOURIDINE(38-40) SYNTHASE, TRNA PSEUDOURIDYLATE
COMPND 6 SYNTHASE I, TRNA-URIDINE ISOMERASE I;
COMPND 7 EC: 5.4.99.12;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PUS1, PP8985;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE)3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET47MODIFIED
KEYWDS BETA SHEET, PSEUDOURIDINE SYNTHASE, RNA BINDING PROTEIN, TRNA, PRE-
KEYWDS 2 TRNA, STEROID RECEPTOR RNA ACTIVATOR, U2 SNRNA, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.CZUDNOCHOWSKI,J.S.FINER-MOORE,R.M.STROUD
REVDAT 5 20-SEP-23 4J37 1 REMARK SEQADV
REVDAT 4 17-JUL-19 4J37 1 REMARK
REVDAT 3 15-NOV-17 4J37 1 REMARK
REVDAT 2 23-OCT-13 4J37 1 JRNL
REVDAT 1 05-JUN-13 4J37 0
JRNL AUTH N.CZUDNOCHOWSKI,A.L.WANG,J.FINER-MOORE,R.M.STROUD
JRNL TITL IN HUMAN PSEUDOURIDINE SYNTHASE 1 (HPUS1), A C-TERMINAL
JRNL TITL 2 HELICAL INSERT BLOCKS TRNA FROM BINDING IN THE SAME
JRNL TITL 3 ORIENTATION AS IN THE PUS1 BACTERIAL HOMOLOGUE TRUA,
JRNL TITL 4 CONSISTENT WITH THEIR DIFFERENT TARGET SELECTIVITIES.
JRNL REF J.MOL.BIOL. V. 425 3875 2013
JRNL REFN ISSN 0022-2836
JRNL PMID 23707380
JRNL DOI 10.1016/J.JMB.2013.05.014
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 37344
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.180
REMARK 3 FREE R VALUE TEST SET COUNT : 2309
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 44.7770 - 4.4084 1.00 2564 169 0.2030 0.2258
REMARK 3 2 4.4084 - 3.4995 1.00 2337 157 0.1708 0.2210
REMARK 3 3 3.4995 - 3.0573 1.00 2271 148 0.1898 0.2017
REMARK 3 4 3.0573 - 2.7778 1.00 2279 152 0.1929 0.2435
REMARK 3 5 2.7778 - 2.5787 1.00 2208 149 0.1837 0.2291
REMARK 3 6 2.5787 - 2.4267 1.00 2232 145 0.1895 0.2487
REMARK 3 7 2.4267 - 2.3052 1.00 2202 149 0.1880 0.2281
REMARK 3 8 2.3052 - 2.2048 1.00 2184 145 0.1878 0.2444
REMARK 3 9 2.2048 - 2.1200 1.00 2207 146 0.1923 0.2558
REMARK 3 10 2.1200 - 2.0468 1.00 2159 142 0.2032 0.2475
REMARK 3 11 2.0468 - 1.9828 1.00 2163 145 0.2225 0.2577
REMARK 3 12 1.9828 - 1.9261 0.99 2134 138 0.2485 0.3139
REMARK 3 13 1.9261 - 1.8754 0.97 2090 140 0.2589 0.2946
REMARK 3 14 1.8754 - 1.8297 0.95 2078 129 0.2744 0.3138
REMARK 3 15 1.8297 - 1.7881 0.93 1999 129 0.2820 0.3341
REMARK 3 16 1.7881 - 1.7500 0.89 1928 126 0.2914 0.2917
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 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) : 21.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.81
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 : 0.012 2471
REMARK 3 ANGLE : 1.231 3332
REMARK 3 CHIRALITY : 0.076 359
REMARK 3 PLANARITY : 0.007 428
REMARK 3 DIHEDRAL : 14.029 929
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 4J37 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077538.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-AUG-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 : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.115869
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI(111)
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37347
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
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 (%) : 98.4
REMARK 200 DATA REDUNDANCY : 11.45
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.78
REMARK 200 R MERGE FOR SHELL (I) : 1.35300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.330
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: PDB ID: 4ITS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG8000, 0.1 M MES, 0.3 M AMSO4,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 296.99333
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 148.49667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 222.74500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 74.24833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 371.24167
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 296.99333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 148.49667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 74.24833
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 222.74500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 371.24167
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 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 A 664 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 GLY A 73
REMARK 465 PRO A 74
REMARK 465 GLY A 75
REMARK 465 SER A 76
REMARK 465 GLU A 77
REMARK 465 PHE A 78
REMARK 465 GLU A 79
REMARK 465 LYS A 80
REMARK 465 VAL A 104
REMARK 465 GLY A 105
REMARK 465 SER A 106
REMARK 465 SER A 107
REMARK 465 SER A 192
REMARK 465 LYS A 193
REMARK 465 ASN A 194
REMARK 465 GLU A 341
REMARK 465 LYS A 342
REMARK 465 TYR A 343
REMARK 465 ASN A 344
REMARK 465 GLN A 345
REMARK 465 ARG A 346
REMARK 465 PHE A 347
REMARK 465 GLY A 348
REMARK 465 ASN A 349
REMARK 465 ASP A 350
REMARK 465 GLY A 351
REMARK 465 LEU A 352
REMARK 465 HIS A 353
REMARK 465 SER A 400
REMARK 465 ALA A 401
REMARK 465 THR A 402
REMARK 465 ALA A 403
REMARK 465 LEU A 404
REMARK 465 THR A 405
REMARK 465 ALA A 406
REMARK 465 GLY A 407
REMARK 465 GLY A 408
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 ARG A 195 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 252 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 O HOH A 632 O HOH A 718 2.02
REMARK 500 O HOH A 633 O HOH A 725 2.02
REMARK 500 O HOH A 736 O HOH A 782 2.07
REMARK 500 O HOH A 764 O HOH A 765 2.09
REMARK 500 OD1 ASP A 165 O HOH A 775 2.10
REMARK 500 OE2 GLU A 269 O HOH A 684 2.12
REMARK 500 O HOH A 663 O HOH A 757 2.14
REMARK 500 NZ LYS A 285 O HOH A 777 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 125 CB CYS A 125 SG -0.103
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 HIS A 98 37.61 -96.47
REMARK 500 GLN A 251 156.74 167.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IQM RELATED DB: PDB
REMARK 900 RELATED ID: 4ITS RELATED DB: PDB
DBREF 4J37 A 79 408 UNP Q9Y606 TRUA_HUMAN 79 408
SEQADV 4J37 GLY A 73 UNP Q9Y606 EXPRESSION TAG
SEQADV 4J37 PRO A 74 UNP Q9Y606 EXPRESSION TAG
SEQADV 4J37 GLY A 75 UNP Q9Y606 EXPRESSION TAG
SEQADV 4J37 SER A 76 UNP Q9Y606 EXPRESSION TAG
SEQADV 4J37 GLU A 77 UNP Q9Y606 EXPRESSION TAG
SEQADV 4J37 PHE A 78 UNP Q9Y606 EXPRESSION TAG
SEQRES 1 A 336 GLY PRO GLY SER GLU PHE GLU LYS PRO PRO LYS ARG LYS
SEQRES 2 A 336 ILE VAL LEU LEU MET ALA TYR SER GLY LYS GLY TYR HIS
SEQRES 3 A 336 GLY MET GLN ARG ASN VAL GLY SER SER GLN PHE LYS THR
SEQRES 4 A 336 ILE GLU ASP ASP LEU VAL SER ALA LEU VAL ARG SER GLY
SEQRES 5 A 336 CYS ILE PRO GLU ASN HIS GLY GLU ASP MET ARG LYS MET
SEQRES 6 A 336 SER PHE GLN ARG CYS ALA ARG THR ASP LYS GLY VAL SER
SEQRES 7 A 336 ALA ALA GLY GLN VAL VAL SER LEU LYS VAL TRP LEU ILE
SEQRES 8 A 336 ASP ASP ILE LEU GLU LYS ILE ASN SER HIS LEU PRO SER
SEQRES 9 A 336 HIS ILE ARG ILE LEU GLY LEU LYS ARG VAL THR GLY GLY
SEQRES 10 A 336 PHE ASN SER LYS ASN ARG CYS ASP ALA ARG THR TYR CYS
SEQRES 11 A 336 TYR LEU LEU PRO THR PHE ALA PHE ALA HIS LYS ASP ARG
SEQRES 12 A 336 ASP VAL GLN ASP GLU THR TYR ARG LEU SER ALA GLU THR
SEQRES 13 A 336 LEU GLN GLN VAL ASN ARG LEU LEU ALA CYS TYR LYS GLY
SEQRES 14 A 336 THR HIS ASN PHE HIS ASN PHE THR SER GLN LYS GLY PRO
SEQRES 15 A 336 GLN ASP PRO SER ALA CYS ARG TYR ILE LEU GLU MET TYR
SEQRES 16 A 336 CYS GLU GLU PRO PHE VAL ARG GLU GLY LEU GLU PHE ALA
SEQRES 17 A 336 VAL ILE ARG VAL LYS GLY GLN SER PHE MET MET HIS GLN
SEQRES 18 A 336 ILE ARG LYS MET VAL GLY LEU VAL VAL ALA ILE VAL LYS
SEQRES 19 A 336 GLY TYR ALA PRO GLU SER VAL LEU GLU ARG SER TRP GLY
SEQRES 20 A 336 THR GLU LYS VAL ASP VAL PRO LYS ALA PRO GLY LEU GLY
SEQRES 21 A 336 LEU VAL LEU GLU ARG VAL HIS PHE GLU LYS TYR ASN GLN
SEQRES 22 A 336 ARG PHE GLY ASN ASP GLY LEU HIS GLU PRO LEU ASP TRP
SEQRES 23 A 336 ALA GLN GLU GLU GLY LYS VAL ALA ALA PHE LYS GLU GLU
SEQRES 24 A 336 HIS ILE TYR PRO THR ILE ILE GLY THR GLU ARG ASP GLU
SEQRES 25 A 336 ARG SER MET ALA GLN TRP LEU SER THR LEU PRO ILE HIS
SEQRES 26 A 336 ASN PHE SER ALA THR ALA LEU THR ALA GLY GLY
HET SO4 A 501 5
HET SO4 A 502 5
HET CL A 503 1
HET EDO A 504 10
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 CL CL 1-
FORMUL 5 EDO C2 H6 O2
FORMUL 6 HOH *184(H2 O)
HELIX 1 1 THR A 111 SER A 123 1 13
HELIX 2 2 PRO A 127 ASP A 133 1 7
HELIX 3 3 MET A 134 SER A 138 5 5
HELIX 4 4 ASP A 165 HIS A 173 1 9
HELIX 5 5 PHE A 208 ALA A 211 5 4
HELIX 6 6 SER A 225 TYR A 239 1 15
HELIX 7 7 HIS A 246 THR A 249 5 4
HELIX 8 8 HIS A 292 LYS A 306 1 15
HELIX 9 9 SER A 312 TRP A 318 1 7
HELIX 10 10 TRP A 358 GLN A 360 5 3
HELIX 11 11 GLU A 361 HIS A 372 1 12
HELIX 12 12 HIS A 372 ARG A 385 1 14
HELIX 13 13 ARG A 385 SER A 392 1 8
HELIX 14 14 THR A 393 HIS A 397 5 5
SHEET 1 A 7 GLN A 140 ARG A 141 0
SHEET 2 A 7 SER A 150 TRP A 161 -1 O SER A 157 N GLN A 140
SHEET 3 A 7 LEU A 333 VAL A 338 1 O LEU A 335 N ALA A 152
SHEET 4 A 7 ALA A 198 PRO A 206 -1 N CYS A 202 O VAL A 334
SHEET 5 A 7 LEU A 277 GLN A 287 -1 O GLY A 286 N ARG A 199
SHEET 6 A 7 CYS A 260 CYS A 268 -1 N TYR A 267 O ARG A 283
SHEET 7 A 7 GLY A 241 ASN A 244 -1 N GLY A 241 O ILE A 263
SHEET 1 B 7 ILE A 178 VAL A 186 0
SHEET 2 B 7 LYS A 83 TYR A 92 -1 N LEU A 89 O LEU A 181
SHEET 3 B 7 SER A 150 TRP A 161 -1 O LEU A 158 N ILE A 86
SHEET 4 B 7 LEU A 333 VAL A 338 1 O LEU A 335 N ALA A 152
SHEET 5 B 7 ALA A 198 PRO A 206 -1 N CYS A 202 O VAL A 334
SHEET 6 B 7 LEU A 277 GLN A 287 -1 O GLY A 286 N ARG A 199
SHEET 7 B 7 PHE A 272 ARG A 274 -1 N PHE A 272 O PHE A 279
SSBOND 1 CYS A 142 CYS A 196 1555 1555 2.05
SSBOND 2 CYS A 260 CYS A 260 1555 10775 2.01
SITE 1 AC1 3 ALA A 143 ARG A 144 ARG A 199
SITE 1 AC2 3 LYS A 85 SER A 138 ARG A 223
SITE 1 AC3 3 ASP A 146 HOH A 761 HOH A 779
SITE 1 AC4 6 ASP A 146 HIS A 292 ARG A 295 LYS A 327
SITE 2 AC4 6 HOH A 734 HOH A 755
CRYST1 51.950 51.950 445.490 90.00 90.00 120.00 P 65 2 2 12
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 0.019249 0.011114 0.000000 0.00000
SCALE2 0.000000 0.022227 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002245 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
