Header list of 1o4x.pdb file
Complete list - 27 20 Bytes
HEADER TRANSCRIPTION/DNA 17-JUL-03 1O4X
TITLE TERNARY COMPLEX OF THE DNA BINDING DOMAINS OF THE OCT1 AND SOX2
TITLE 2 TRANSCRIPTION FACTORS WITH A 19MER OLIGONUCLEOTIDE FROM THE HOXB1
TITLE 3 REGULATORY ELEMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*TP*GP*TP*CP*TP*TP*TP*GP*TP*CP*AP*TP*GP*CP*TP*AP*AP*TP
COMPND 3 *G)-3';
COMPND 4 CHAIN: C;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 5'-D(*CP*AP*TP*TP*AP*GP*CP*AP*TP*GP*AP*CP*AP*AP*AP*GP*AP*CP
COMPND 9 *A)-3';
COMPND 10 CHAIN: D;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: TRANSCRIPTION FACTOR OCT-1;
COMPND 14 CHAIN: A;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: TRANSCRIPTION FACTOR SOX-2;
COMPND 18 CHAIN: B;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 MOL_ID: 4;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: SOX2;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OCT1, POU, POUS, POUHD, SOX2, HMG-BOX, TRANSCRIPTION FACTORS, DNA,
KEYWDS 2 PROTEIN-DNA COMPLEX, TRANSCRIPTION-DNA COMPLEX
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,D.C.WILLIAMS
REVDAT 3 27-OCT-21 1O4X 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1O4X 1 VERSN
REVDAT 1 27-JAN-04 1O4X 0
JRNL AUTH D.C.WILLIAMS,M.CAI,G.M.CLORE
JRNL TITL MOLECULAR BASIS FOR SYNERGISTIC TRANSCRIPTIONAL ACTIVATION
JRNL TITL 2 BY OCT1 AND SOX2 REVEALED FROM THE SOLUTION STRUCTURE OF THE
JRNL TITL 3 42-KDA OCT1.SOX2.HOXB1-DNA TERNARY TRANSCRIPTION FACTOR
JRNL TITL 4 COMPLEX.
JRNL REF J.BIOL.CHEM. V. 279 1449 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14559893
JRNL DOI 10.1074/JBC.M309790200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH (HTTP://NMR.CIT.NIH.GOV/XPLOR_NIH)
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA, CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED BY CONJOINED RIGID BODY/TORSION
REMARK 3 ANGLE DYNAMICS (SCHWIETERS & CLORE (2001) J.MAGN.RESON 152, 288-
REMARK 3 302). THE TARGET FUNCTION COMPRISES TERMS FOR THE DIPOLAR COUPLING
REMARK 3 RESTRAINTS (CLORE ET AL. J.MAGN.RESON. 131, 159-162 (1998);
REMARK 3 J.MAGN.RESON. 133, 216- 221(1998)), INTERMOLECULAR NOE RESTRAINTS
REMARK 3 AND TORSION ANGLE RESTRAINTS. THE NON-BONDED TERMS INCLUDE A
REMARK 3 QUARTIC VAN DER WAALS REPULSION TERM (NILGES ET AL. (1988) FEBS
REMARK 3 LETT. 229, 129-136), RADIUS OF GYRATION RESTRAINTS
REMARK 3 (KUSZEWSKI ET AL. (1999) J.AM.CHEM.SOC 121, 2337-2338) AT THE
REMARK 3 PROTEIN-PROTEIN AND PROTEIN-DNA INTERFACES, AND DATABASE TORSION
REMARK 3 ANGLE AND BASE-BASE POSITIONAL POTENTIALS OF MEAN FORCE (KUSZEWSKI
REMARK 3 ET AL. (2001) J.AM.CHEM.SOC 123, 3903-3918; CLORE & KUSZEWSKI
REMARK 3 (2003) J.AM.CHEM.SOC. 125, 1518-1525). THE STARTING COORDINATES
REMARK 3 FOR THE POUHD AND POUS DOMAINS OF OCT1 ARE TAKEN FROM THE 1.9 A
REMARK 3 RESOLUTION CRYSTAL STRUCTURE OF THE OCT1/MORE-DNA COMPLEX (1E3O)
REMARK 3 AND PLACED IN THE ORIENTATION OF THE 2.7 A RESOLUTION CRYSTAL
REMARK 3 STRUCTURE OF THE OCT1/PORE-DNA COMPLEX (1HFO) (REMENYI ET AL.
REMARK 3 (2001) MOL.CELL 8, 569-580). THE STARTING COORDINATES FOR SOX2 ARE
REMARK 3 DERIVED FROM THE NMR STRUCTURE OF THE RELATED BINARY SRY-DNA
REMARK 3 COMPLEX (1J46) (MURPHY ET AL. (2001) J.MOL.BIOL. 312, 481-499).
REMARK 3 THE STARTING COORDINATES FOR THE 19MER DNA WERE BUILT AS FOLLOWS:
REMARK 3 THE POUS AND POUHD HEMI-BINDING SITES (B.P. 11-14 AND 17-19,
REMARK 3 RESPECTIVELY) WERE DERIVED FROM THE 1.9 A RESIOLUTION STRUCTURE OF
REMARK 3 THE OCT1/MORE-DNA COMPLEX (1E3O); THE
REMARK 3 SOX2 BINDING SITE (B.P. 1-10) WAS DERIVED FROM THE NMR STRUCTURE
REMARK 3 OF THE BINARY SRY/DNA COMPLEX (1J46); AND THE INTERVENING
REMARK 3 SEQUENCES (B.P. 15-16) AND REGIONS CONTAINING SUBSTITUTIONS (B.P.
REMARK 3 1, 4 AND 10) WERE DERIVED FROM CLASSICAL DNA. THE RESULTING MODEL
REMARK 3 WAS SUBJECTED TO REGULARIZATION. THE STRATEGY USED IN THE
REMARK 3 CONJOINED RIGID BODY/TORSION ANGLE DYNAMICS CALCULATIONS IS AS
REMARK 3 FOLLOWS: THERE ARE 4 RIGID BODIES: (1) BACKBONE AND NON-
REMARK 3 INTERFACIAL SIDE CHAINS OF POUHD + B.P. 17-19 OF THE DNA (2)
REMARK 3 BACKBONE AND NON-INTERFACIAL SIDE CHAINS OF POUS; (3) BACKBONE AND
REMARK 3 NON-INTERFACIAL SIDE CHAINS OF SOX2 + B.P. 1-4 OF THE DNA; (4) THE
REMARK 3 AXIS OF THE DIPOLAR COUPLING ALIGNMENT TENSOR. RIGID BODIES 1-3
REMARK 3 HAVE ROTATIONAL AND TRANSLATIONAL DEGREES OF FREEDOM, WHILE RIGID
REMARK 3 BODY 4 IS GIVEN ONLY ROTATIONAL DEGREES OF FREEDOM. THE FOLLOWING
REMARK 3 SIDE CHAINS WERE GIVEN TORSIONAL DEGREES OF FREEDOM: (1) POUHD: 10
REMARK 3 RESIDUES AT POUHD-DNA INTERFACE (RESIDUES 107, 108, 113, 144, 147,
REMARK 3 148, 151, 154, 155 AND 158) WITH 24 SIDE C
REMARK 3 AIN TORSION ANGLES RESTRAINED TO WITHIN A RANGE OF +/-20 DEGREES
REMARK 3 OF VALUES IN BINARY OCT1/DNA COMPLEXES (2) POUS: (A) 6 RESIDUES AT
REMARK 3 POUS/SOX2 INTERFACE (RESIDUES 14, 17, 18, 21, 26 AND 52); (B) 14
REMARK 3 RESIDUES AT POUS/DNA INTERFACE (RESIDUES 20, 27, 41, 42, 44, 45,
REMARK 3 46, 48, 49, 54, 58, 59, 62 AND 63) WITH 35 SIDE CHAIN TORSION
REMARK 3 ANGLES RESTRAINED TO WITHIN A RANGE OF +/-20 DEGREES OF VALUES IN
REMARK 3 BINARY OCT1/DNA COMPLEXES (3) SOX2: (A) 7 RESIDUES AT POUS/SOX2
REMARK 3 INTERFACE (RESIDUES 59, 62, 63, 66, 67, 71,
REMARK 3 73); (B) 18 RESIDUES AT SOX2/DNA INTERFACE (RESIDUES 4, 6, 7, 8, 9,
REMARK 3 10, 12, 13 17, 31, 35, 43, 44, 51, 55, 76, 78, 79) WITH 35 SIDE
REMARK 3 CHAIN TORSION ANGLES RESTRAINED TO WITHIN A RANGE OF +/-20 DEGREES
REMARK 3 OF VALUES IN BINARY SRY/DNA COMPLEXES. BASE PAIRS 5-16 OF THE DNA
REMARK 3 WERE GIVEN TORSIONAL DEGREES OF FREEDOM WITH 220 LOOSE BACKBONE
REMARK 3 PHOSPHODIESTER TORSION ANGLE RESTRAINTS TO PREVENT LOCAL MIRROR
REMARK 3 IMAGES (MURPHY ET AL. (2001) J.MOL.BIOL. 312, 481-499).
REMARK 3 THE NUMBERING SYSTEM IS AS FOLLOWS:
REMARK 3 OCT1 POUS DOMAIN: 5-79
REMARK 3 OCT1 POUHD DOMAIN: 110-163
REMARK 3 SOX-2 HMG-BOX: 206-282
REMARK 3 RESIDUES 1-4, 80-109, 201-205 AND 283-288 ARE DISORDERED
REMARK 3 IN SOLUTION AND THUS NOT INCLUDED IN THE COORDINATES.
REMARK 3
REMARK 3 IN THIS ENTRY THE LAST COLUMN REPRESENTS THE AVERAGE RMS
REMARK 3 DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED ANNEALING
REMARK 3 STRUCTURES AND THE MEAN COORDINATE POSITIONS. IT IS
REMARK 3 IMPORTANT TO NOTE THAT SINCE THE BACKBONE AND NON-
REMARK 3 INTERFACIAL SIECHAINS OF THE THREE PROTEIN DOMAINS ARE
REMARK 3 TREATED AS RIGID BODIES, THESE NUMBERS DO NOT TAKE INTO
REMARK 3 ACCOUNT THE ERRORS IN THE X-RAY COORDINATES OF OCT1 OR
REMARK 3 THE NMR COORDINATES OF THE HOMOLOGOUS SRY.
REMARK 3
REMARK 3 RESIDUE NUMBERING: THIS FOLLOWS THE NUMBERING USED
REMARK 3 PREVIOUS STRUCTURAL WORK ON THE BINARY OCT1/DNA
REMARK 3 COMPLEX (KLEMM ET AL. (1994) CELL 77, 21-32;
REMARK 3 REMENYI ET AL. MOL.CELL (2001) 8, 569-580);
REMARK 3 AND THE BINARY SRY/DNA COMPLEX (MURPHY ET AL.
REMARK 3 (2001) J.MOL.BIOL. 312, 481-499).
REMARK 3
REMARK 3 THE SIDECHAINS OF K18, Q22, K262, R265 AND K276 ARE IN
REMARK 3 MULTIPLE CONFORMATIONS.
REMARK 3
REMARK 3 EXPERIMENTAL NMR RESTRAINTS:
REMARK 3 RESIDUAL DIPOLAR COUPLINGS: 345
REMARK 3 (1) SOX2: 51 NH, 39 NC', 49 CAC'
REMARK 3 (2) POUS: 39 NH, 33 NC', 34 CAC'
REMARK 3 (3) POUHD: 39 NH, 34 NC', 27 CAC'
REMARK 3 INTERMOLECULAR NOE-DERIVED INTERPROTON DISTANCE
REMARK 3 RESTRAINTS:
REMARK 3 67 (16, 48 AND 3 AT POUS/SOX2, SOX2/DNA
REMARK 3 AND POUHD/DNA INTERFACES)
REMARK 3 TORSION ANGLE RESTRAINTS: 21
REMARK 3 (18 AT POUS/SOX2 INTERFACE AND 3 AT SOX2/DNA
REMARK 3 INTERFACE).
REMARK 3 NH DIPOLAR COUPLING R-FACTORS
REMARK 3 TERNARY COMPLEX INDIVIDUAL DOMAINS
REMARK 3 SOX2 17.7% 16.5%
REMARK 3 POUS 16.7% 16.2%
REMARK 3 POUHD 17.7% 17.5%
REMARK 3 (THE VALUES GIVEN FOR THE INDIVIDUAL DOMAINS
REMARK 3 ARE CALCULATED USING A SEPARATED ALIGNMENT
REMARK 3 TENSOR FOR EACH DOMAIN AND ARE SIMPLY LISTED
REMARK 3 FOR REFERENCE. THE VALUES FOR THE TERNARY
REMARK 3 COMPLEX (USING THE RESTRAINED REGULARIZED MEAN
REMARK 3 COORDINATES) MAKE USE OF A SINGLE ALIGNMENT
REMARK 3 TENSOR FOR THE ENTIRE COMPLEX).
REMARK 3 NON-EXPERIMENTAL RESTRAINTS:
REMARK 3 (1) 220 LOOSE TORSION ANGLE RESTRAINTS FOR THE
REMARK 3 SUGAR-PHOSPHATE BACKBONE
REMARK 3 (2) 106 LOOSE TORSION ANGLE RESTRAINTS FOR SIDE CHAINS
REMARK 3 AT PROTEIN-DNA INTERFACES
REMARK 3 (3) 35 LOOSE DISTANCE RESTRAINTS AT THE POUS/DNA AND
REMARK 3 POUHD/DNA INTERFACES TO PRESERVE HYDROGEN BONDING
REMARK 3 INTERCATIONS AND SALT BRIDGES TO BASES AND PHOSPHATES
REMARK 3 (4) WEAK NCS RESTRAINT TO PROVIDE A TRANSLATIONAL RESTRANT
REMARK 3 BETWEEN POUS AND POUHD.
REMARK 4
REMARK 4 1O4X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000001808.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.00
REMARK 210 PH : 6.50
REMARK 210 IONIC STRENGTH : 10 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1) TRIPLE RESONANCE FOR
REMARK 210 ASSIGNMENT OF PROTEIN; (2)
REMARK 210 QUANTITATIVE J CORRELATION FOR
REMARK 210 COUPLING CONSTANTS; (3) 3D
REMARK 210 HETERONUCLEAR SEPARATED;
REMARK 210 FILTERED NOE EXPTS; (4) IPAP
REMARK 210 EXPERIMENTS; TRIPLE RESONANC FOR
REMARK 210 DIPOLAR COUPLINGS. DIPOLAR
REMARK 210 COUPLINGS WERE MEASURED IN PHAGE
REMARK 210 PF1
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ; 800
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600; DRX600; DRX750;
REMARK 210 DRX800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : CONJOINED RIGID BODY/TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : REGULARIZED MEAN STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: C, D, A, 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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 ASN A 80
REMARK 465 LEU A 81
REMARK 465 SER A 82
REMARK 465 SER A 83
REMARK 465 ASP A 84
REMARK 465 SER A 85
REMARK 465 SER A 86
REMARK 465 LEU A 87
REMARK 465 SER A 88
REMARK 465 SER A 89
REMARK 465 PRO A 90
REMARK 465 SER A 91
REMARK 465 ALA A 92
REMARK 465 LEU A 93
REMARK 465 ASN A 94
REMARK 465 SER A 95
REMARK 465 PRO A 96
REMARK 465 GLY A 97
REMARK 465 ILE A 98
REMARK 465 GLU A 99
REMARK 465 GLY A 100
REMARK 465 LEU A 101
REMARK 465 SER A 102
REMARK 465 GLU A 103
REMARK 465 ARG A 104
REMARK 465 ARG A 105
REMARK 465 LYS A 106
REMARK 465 LYS A 107
REMARK 465 ARG A 108
REMARK 465 THR A 109
REMARK 465 PRO A 164
REMARK 465 PRO A 165
REMARK 465 SER A 166
REMARK 465 SER A 167
REMARK 465 GLY B 201
REMARK 465 SER B 202
REMARK 465 HIS B 203
REMARK 465 MET B 204
REMARK 465 PRO B 205
REMARK 465 THR B 283
REMARK 465 LYS B 284
REMARK 465 THR B 285
REMARK 465 LEU B 286
REMARK 465 MET B 287
REMARK 465 LYS B 288
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 RES CSSEQI ATOMS
REMARK 470 GLU A 5 CG CD OE1 OE2
REMARK 470 GLU A 79 O
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 LYS A 128 CG CD CE NZ
REMARK 470 GLU A 132 CG CD OE1 OE2
REMARK 470 LYS A 145 CG CD CE NZ
REMARK 470 ASN A 163 O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 B 251 HH12 ARG B 255 0.84
REMARK 500 HD12 LEU A 13 HD2 LYS A 68 1.24
REMARK 500 HE21 GLN A 31 O GLN A 48 1.28
REMARK 500 HE2 MET B 233 HH22 ARG B 241 1.32
REMARK 500 HH12 ARG A 24 HB2 GLN A 31 1.33
REMARK 500 OD1 ASN B 213 H MET B 216 1.44
REMARK 500 O SER B 219 H ARG B 223 1.50
REMARK 500 OE2 GLU B 251 NH1 ARG B 255 1.54
REMARK 500 O GLY A 28 HZ3 LYS B 262 1.56
REMARK 500 NE2 GLN A 31 O GLN A 48 1.62
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 DA C 311 N1 - C2 - N3 ANGL. DEV. = -3.0 DEGREES
REMARK 500 DA D 321 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 DT D 322 C6 - C5 - C7 ANGL. DEV. = -3.8 DEGREES
REMARK 500 DA D 324 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 DA D 330 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 DA D 332 N1 - C2 - N3 ANGL. DEV. = -3.2 DEGREES
REMARK 500 DA D 333 N1 - C2 - N3 ANGL. DEV. = -3.0 DEGREES
REMARK 500 DA D 334 N1 - C2 - N3 ANGL. DEV. = -3.0 DEGREES
REMARK 500 DA D 336 N1 - C2 - N3 ANGL. DEV. = -3.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 155 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1O4X A 5 167 UNP P14859 PO2F1_HUMAN 303 465
DBREF 1O4X B 206 288 UNP P48431 SOX2_HUMAN 39 121
DBREF 1O4X C 301 319 PDB 1O4X 1O4X 301 319
DBREF 1O4X D 320 338 PDB 1O4X 1O4X 320 338
SEQADV 1O4X GLY A 1 UNP P14859 CLONING ARTIFACT
SEQADV 1O4X SER A 2 UNP P14859 CLONING ARTIFACT
SEQADV 1O4X HIS A 3 UNP P14859 CLONING ARTIFACT
SEQADV 1O4X MET A 4 UNP P14859 CLONING ARTIFACT
SEQADV 1O4X ALA A 65 UNP P14859 CYS 363 ENGINEERED MUTATION
SEQADV 1O4X GLY B 201 UNP P48431 CLONING ARTIFACT
SEQADV 1O4X SER B 202 UNP P48431 CLONING ARTIFACT
SEQADV 1O4X HIS B 203 UNP P48431 CLONING ARTIFACT
SEQADV 1O4X MET B 204 UNP P48431 CLONING ARTIFACT
SEQADV 1O4X PRO B 205 UNP P48431 CLONING ARTIFACT
SEQRES 1 C 19 DT DG DT DC DT DT DT DG DT DC DA DT DG
SEQRES 2 C 19 DC DT DA DA DT DG
SEQRES 1 D 19 DC DA DT DT DA DG DC DA DT DG DA DC DA
SEQRES 2 D 19 DA DA DG DA DC DA
SEQRES 1 A 167 GLY SER HIS MET GLU GLU PRO SER ASP LEU GLU GLU LEU
SEQRES 2 A 167 GLU GLN PHE ALA LYS THR PHE LYS GLN ARG ARG ILE LYS
SEQRES 3 A 167 LEU GLY PHE THR GLN GLY ASP VAL GLY LEU ALA MET GLY
SEQRES 4 A 167 LYS LEU TYR GLY ASN ASP PHE SER GLN THR THR ILE SER
SEQRES 5 A 167 ARG PHE GLU ALA LEU ASN LEU SER PHE LYS ASN MET ALA
SEQRES 6 A 167 LYS LEU LYS PRO LEU LEU GLU LYS TRP LEU ASN ASP ALA
SEQRES 7 A 167 GLU ASN LEU SER SER ASP SER SER LEU SER SER PRO SER
SEQRES 8 A 167 ALA LEU ASN SER PRO GLY ILE GLU GLY LEU SER GLU ARG
SEQRES 9 A 167 ARG LYS LYS ARG THR SER ILE GLU THR ASN ILE ARG VAL
SEQRES 10 A 167 ALA LEU GLU LYS SER PHE LEU GLU ASN GLN LYS PRO THR
SEQRES 11 A 167 SER GLU GLU ILE THR MET ILE ALA ASP GLN LEU ASN MET
SEQRES 12 A 167 GLU LYS GLU VAL ILE ARG VAL TRP PHE CYS ASN ARG ARG
SEQRES 13 A 167 GLN LYS GLU LYS ARG ILE ASN PRO PRO SER SER
SEQRES 1 B 88 GLY SER HIS MET PRO ASP ARG VAL LYS ARG PRO MET ASN
SEQRES 2 B 88 ALA PHE MET VAL TRP SER ARG GLY GLN ARG ARG LYS MET
SEQRES 3 B 88 ALA GLN GLU ASN PRO LYS MET HIS ASN SER GLU ILE SER
SEQRES 4 B 88 LYS ARG LEU GLY ALA GLU TRP LYS LEU LEU SER GLU THR
SEQRES 5 B 88 GLU LYS ARG PRO PHE ILE ASP GLU ALA LYS ARG LEU ARG
SEQRES 6 B 88 ALA LEU HIS MET LYS GLU HIS PRO ASP TYR LYS TYR ARG
SEQRES 7 B 88 PRO ARG ARG LYS THR LYS THR LEU MET LYS
HELIX 1 1 ASP A 9 LEU A 27 1 19
HELIX 2 2 THR A 30 GLY A 43 1 14
HELIX 3 3 SER A 47 LEU A 57 1 11
HELIX 4 4 SER A 60 GLU A 79 1 20
HELIX 5 5 GLU A 112 ASN A 126 1 15
HELIX 6 6 THR A 130 ASN A 142 1 13
HELIX 7 7 GLU A 144 LYS A 160 1 17
HELIX 8 8 ASN B 213 ASN B 230 1 18
HELIX 9 9 HIS B 234 LYS B 247 1 14
HELIX 10 10 SER B 250 HIS B 272 1 23
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 27 20 Bytes