HEADER RNA BINDING PROTEIN 01-NOV-05 2EVZ
TITLE STRUCTURE OF RNA BINDING DOMAINS 3 AND 4 OF POLYPYRIMIDINE TRACT
TITLE 2 BINDING PROTEIN
CAVEAT 2EVZ CHIRALITY ERROR AT THE CA CENTER OF ASP A 100 IN MODEL 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYPYRIMIDINE TRACT-BINDING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA BINDING DOMAINS 3 AND 4;
COMPND 5 SYNONYM: PTB, HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN I, HNRNP I, 57
COMPND 6 KDA RNA-BINDING PROTEIN PPTB-1;
COMPND 7 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: PTBP1, PTB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)C+RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A+
KEYWDS ALPHA-BETA SANDWICH, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.H.ALLAIN,S.D.AUWETER
REVDAT 4 09-MAR-22 2EVZ 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2EVZ 1 VERSN
REVDAT 2 24-JAN-06 2EVZ 1 JRNL
REVDAT 1 17-JAN-06 2EVZ 0
JRNL AUTH F.VITALI,A.HENNING,F.C.OBERSTRASS,Y.HARGOUS,S.D.AUWETER,
JRNL AUTH 2 M.ERAT,F.H.ALLAIN
JRNL TITL STRUCTURE OF THE TWO MOST C-TERMINAL RNA RECOGNITION MOTIFS
JRNL TITL 2 OF PTB USING SEGMENTAL ISOTOPE LABELING
JRNL REF EMBO J. V. 25 150 2006
JRNL REFN ISSN 0261-4189
JRNL PMID 16362043
JRNL DOI 10.1038/SJ.EMBOJ.7600911
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0, AMBER 7.0
REMARK 3 AUTHORS : PETER GUENTERT (CYANA), DAVID A. CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EVZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035159.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 20MM NACL, 10MM NA-PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM PTB RBD34 15N; 20MM NACL;
REMARK 210 10MM SODIUM PHOSPHATE; 90% H2O,
REMARK 210 10% D2O; 1MM PTB RBD34 15N, 13C;
REMARK 210 20MM NACL; 10MM SODIUM PHOSPHATE;
REMARK 210 90% H2O, 10% D2O; 1MM PTB RBD34
REMARK 210 15N; 20MM NACL; 10MM SODIUM
REMARK 210 PHOSPHATE; 100% D2O; 1MM PTB
REMARK 210 RBD34 15N, 13C; 20MM NACL; 10MM
REMARK 210 SODIUM PHOSPHATE; 100% D2O; 1MM
REMARK 210 PTB RBD3 15N, 13C, RBD4
REMARK 210 UNLABELED; 20MM NACL; 10MM
REMARK 210 SODIUM PHOSPHATE; 100% D2O; 1MM
REMARK 210 PTB RBD3 UNLABELED, RBD4 13C,
REMARK 210 15N; 20MM NACL; 10MM SODIUM
REMARK 210 PHOSPHATE; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HNCOCA; CBCACONH; HNCACB;
REMARK 210 3D_15N-SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HCCH-TOCSY; 2D
REMARK 210 NOESY; 2D F1-EDITED, F2-FITERED
REMARK 210 NOESY; 3D_13C-SEPARATED HALF-
REMARK 210 FILTERED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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: MONOMERIC
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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
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 C ASN A 72 H GLY A 73 1.56
REMARK 500 H ASN A 190 O LEU A 199 1.58
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 1 PRO A 6 CA PRO A 6 C 0.131
REMARK 500 1 ASN A 13 CA ASN A 13 CB 0.176
REMARK 500 1 VAL A 15 N VAL A 15 CA -0.148
REMARK 500 1 VAL A 15 CB VAL A 15 CG2 0.212
REMARK 500 1 VAL A 18 N VAL A 18 CA 0.128
REMARK 500 1 VAL A 18 C VAL A 18 O 0.116
REMARK 500 1 SER A 19 CA SER A 19 CB 0.107
REMARK 500 1 SER A 19 CB SER A 19 OG -0.110
REMARK 500 1 GLU A 24 C GLU A 24 O -0.128
REMARK 500 1 ARG A 25 C ARG A 25 O 0.170
REMARK 500 1 VAL A 26 CA VAL A 26 C 0.157
REMARK 500 1 GLN A 29 C SER A 30 N 0.154
REMARK 500 1 PHE A 32 CB PHE A 32 CG 0.107
REMARK 500 1 PHE A 32 CG PHE A 32 CD1 0.142
REMARK 500 1 PHE A 35 CE2 PHE A 35 CD2 0.159
REMARK 500 1 GLY A 36 N GLY A 36 CA -0.091
REMARK 500 1 TYR A 38 CE1 TYR A 38 CZ 0.088
REMARK 500 1 ASP A 40 CB ASP A 40 CG 0.140
REMARK 500 1 ASP A 40 CA ASP A 40 C 0.162
REMARK 500 1 GLN A 42 CG GLN A 42 CD 0.162
REMARK 500 1 ARG A 43 CD ARG A 43 NE 0.111
REMARK 500 1 VAL A 44 CA VAL A 44 CB -0.239
REMARK 500 1 LEU A 47 N LEU A 47 CA 0.139
REMARK 500 1 PHE A 48 CG PHE A 48 CD1 0.148
REMARK 500 1 GLU A 52 CD GLU A 52 OE1 0.073
REMARK 500 1 GLU A 52 CD GLU A 52 OE2 -0.078
REMARK 500 1 VAL A 56 CA VAL A 56 CB -0.140
REMARK 500 1 ALA A 59 CA ALA A 59 CB 0.161
REMARK 500 1 ASP A 60 N ASP A 60 CA 0.166
REMARK 500 1 ASP A 60 CA ASP A 60 CB 0.167
REMARK 500 1 ASN A 62 CB ASN A 62 CG 0.165
REMARK 500 1 ASN A 62 CA ASN A 62 C 0.188
REMARK 500 1 GLN A 63 CD GLN A 63 OE1 0.138
REMARK 500 1 GLN A 65 CA GLN A 65 CB 0.147
REMARK 500 1 LEU A 66 N LEU A 66 CA -0.131
REMARK 500 1 HIS A 70 CB HIS A 70 CG 0.113
REMARK 500 1 HIS A 74 CG HIS A 74 CD2 0.066
REMARK 500 1 HIS A 74 CE1 HIS A 74 NE2 -0.101
REMARK 500 1 HIS A 77 CE1 HIS A 77 NE2 -0.071
REMARK 500 1 SER A 86 CA SER A 86 CB 0.090
REMARK 500 1 VAL A 91 CB VAL A 91 CG1 0.132
REMARK 500 1 GLU A 96 CA GLU A 96 CB 0.153
REMARK 500 1 ASP A 100 CA ASP A 100 CB 0.135
REMARK 500 1 ASP A 100 CB ASP A 100 CG 0.180
REMARK 500 1 GLN A 101 C GLY A 102 N 0.139
REMARK 500 1 ASP A 106 N ASP A 106 CA -0.123
REMARK 500 1 SER A 110 C SER A 110 O 0.126
REMARK 500 1 LEU A 112 C LEU A 112 O 0.130
REMARK 500 1 PHE A 115 CG PHE A 115 CD1 0.104
REMARK 500 1 GLY A 119 N GLY A 119 CA 0.145
REMARK 500
REMARK 500 THIS ENTRY HAS 253 BOND DEVIATIONS.
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 1 ARG A 2 CD - NE - CZ ANGL. DEV. = 12.6 DEGREES
REMARK 500 1 ILE A 3 CA - C - N ANGL. DEV. = 14.0 DEGREES
REMARK 500 1 LEU A 8 CA - C - O ANGL. DEV. = 14.9 DEGREES
REMARK 500 1 ALA A 11 N - CA - CB ANGL. DEV. = 16.6 DEGREES
REMARK 500 1 GLY A 12 CA - C - N ANGL. DEV. = -13.5 DEGREES
REMARK 500 1 ASN A 13 N - CA - CB ANGL. DEV. = -16.3 DEGREES
REMARK 500 1 SER A 14 CA - C - N ANGL. DEV. = 17.8 DEGREES
REMARK 500 1 SER A 14 O - C - N ANGL. DEV. = -23.5 DEGREES
REMARK 500 1 VAL A 15 C - N - CA ANGL. DEV. = 16.0 DEGREES
REMARK 500 1 LEU A 16 CB - CG - CD1 ANGL. DEV. = -12.6 DEGREES
REMARK 500 1 LEU A 17 CA - C - O ANGL. DEV. = 13.0 DEGREES
REMARK 500 1 VAL A 18 C - N - CA ANGL. DEV. = 16.8 DEGREES
REMARK 500 1 VAL A 18 CA - CB - CG2 ANGL. DEV. = -11.9 DEGREES
REMARK 500 1 SER A 19 N - CA - CB ANGL. DEV. = -11.7 DEGREES
REMARK 500 1 ASN A 20 CA - C - O ANGL. DEV. = 14.2 DEGREES
REMARK 500 1 ASN A 20 O - C - N ANGL. DEV. = -12.2 DEGREES
REMARK 500 1 LEU A 21 N - CA - CB ANGL. DEV. = -12.6 DEGREES
REMARK 500 1 LEU A 21 CA - CB - CG ANGL. DEV. = 26.0 DEGREES
REMARK 500 1 LEU A 21 CB - CG - CD1 ANGL. DEV. = 19.8 DEGREES
REMARK 500 1 ASN A 22 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 1 ASN A 22 O - C - N ANGL. DEV. = -12.6 DEGREES
REMARK 500 1 PRO A 23 C - N - CA ANGL. DEV. = 11.8 DEGREES
REMARK 500 1 PRO A 23 C - N - CD ANGL. DEV. = -14.6 DEGREES
REMARK 500 1 GLU A 24 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 1 GLU A 24 CA - C - O ANGL. DEV. = 15.3 DEGREES
REMARK 500 1 ARG A 25 NH1 - CZ - NH2 ANGL. DEV. = -14.6 DEGREES
REMARK 500 1 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ARG A 25 NE - CZ - NH2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 VAL A 26 CG1 - CB - CG2 ANGL. DEV. = -16.1 DEGREES
REMARK 500 1 VAL A 26 CA - CB - CG2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 1 THR A 27 CA - CB - CG2 ANGL. DEV. = 12.1 DEGREES
REMARK 500 1 LEU A 31 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 1 LEU A 31 O - C - N ANGL. DEV. = -10.2 DEGREES
REMARK 500 1 PHE A 32 CB - CG - CD2 ANGL. DEV. = -13.4 DEGREES
REMARK 500 1 PHE A 32 CB - CG - CD1 ANGL. DEV. = 13.6 DEGREES
REMARK 500 1 LEU A 34 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 1 LEU A 34 CB - CG - CD1 ANGL. DEV. = -11.3 DEGREES
REMARK 500 1 LEU A 34 CB - CG - CD2 ANGL. DEV. = 17.0 DEGREES
REMARK 500 1 PHE A 35 CD1 - CE1 - CZ ANGL. DEV. = -12.5 DEGREES
REMARK 500 1 PHE A 35 CE1 - CZ - CE2 ANGL. DEV. = 18.0 DEGREES
REMARK 500 1 PHE A 35 CZ - CE2 - CD2 ANGL. DEV. = -13.5 DEGREES
REMARK 500 1 VAL A 37 CG1 - CB - CG2 ANGL. DEV. = -11.0 DEGREES
REMARK 500 1 VAL A 37 CA - CB - CG2 ANGL. DEV. = 24.5 DEGREES
REMARK 500 1 TYR A 38 CB - CG - CD2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 TYR A 38 CD1 - CG - CD2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 1 TYR A 38 CG - CD2 - CE2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 1 TYR A 38 O - C - N ANGL. DEV. = 11.8 DEGREES
REMARK 500 1 ASP A 40 CB - CG - OD1 ANGL. DEV. = 12.1 DEGREES
REMARK 500 1 ASP A 40 CB - CG - OD2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 1 GLN A 42 CA - C - O ANGL. DEV. = 15.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 688 ANGLE DEVIATIONS.
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 1 ARG A 2 75.43 -58.31
REMARK 500 1 ILE A 3 -136.71 -116.76
REMARK 500 1 ALA A 4 19.16 43.91
REMARK 500 1 ILE A 5 38.49 -169.95
REMARK 500 1 LEU A 8 -68.02 32.52
REMARK 500 1 ALA A 9 -74.35 -64.50
REMARK 500 1 ASN A 13 -6.73 -146.99
REMARK 500 1 SER A 14 -60.03 65.67
REMARK 500 1 VAL A 15 88.97 -48.81
REMARK 500 1 ASN A 20 34.12 88.06
REMARK 500 1 PRO A 23 -71.25 -34.76
REMARK 500 1 VAL A 41 125.29 -33.80
REMARK 500 1 PHE A 48 -64.41 -8.37
REMARK 500 1 ASN A 49 16.63 -153.11
REMARK 500 1 LYS A 50 -70.87 -90.44
REMARK 500 1 ASP A 60 -166.97 175.46
REMARK 500 1 ASN A 72 89.15 -47.29
REMARK 500 1 LYS A 75 62.10 32.18
REMARK 500 1 PRO A 80 79.18 -49.50
REMARK 500 1 ILE A 81 141.88 -37.10
REMARK 500 1 THR A 84 -153.85 -136.32
REMARK 500 1 SER A 86 -36.89 -140.92
REMARK 500 1 LYS A 87 -34.45 57.77
REMARK 500 1 HIS A 88 79.58 -29.08
REMARK 500 1 GLN A 89 -97.69 30.53
REMARK 500 1 LEU A 93 122.31 -26.78
REMARK 500 1 PRO A 94 -87.88 -102.62
REMARK 500 1 GLU A 96 -73.09 -36.44
REMARK 500 1 ASP A 100 -6.01 -8.67
REMARK 500 1 GLN A 101 -59.16 -164.95
REMARK 500 1 ASN A 109 60.23 -102.53
REMARK 500 1 HIS A 113 -108.91 45.39
REMARK 500 1 ARG A 114 -24.56 116.08
REMARK 500 1 PHE A 115 -84.26 -76.21
REMARK 500 1 LYS A 121 85.12 -158.04
REMARK 500 1 ILE A 126 -53.77 -8.78
REMARK 500 1 PHE A 127 108.15 43.23
REMARK 500 1 PRO A 129 88.82 1.47
REMARK 500 1 ASN A 137 100.64 59.85
REMARK 500 1 SER A 141 -62.26 -108.65
REMARK 500 1 PHE A 151 1.68 -57.83
REMARK 500 1 VAL A 158 70.53 7.87
REMARK 500 1 PHE A 164 -162.44 -37.04
REMARK 500 1 LYS A 166 -95.72 22.90
REMARK 500 1 ASP A 167 -70.29 -2.61
REMARK 500 1 ARG A 168 81.08 78.86
REMARK 500 1 LYS A 169 -69.72 -127.45
REMARK 500 1 MET A 170 159.88 -38.03
REMARK 500 1 MET A 175 -171.75 -52.99
REMARK 500 1 GLU A 179 -36.37 -28.26
REMARK 500
REMARK 500 THIS ENTRY HAS 672 RAMACHANDRAN OUTLIERS.
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 PRO A 94 ARG A 95 1 -141.27
REMARK 500 PRO A 128 PRO A 129 19 -145.08
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 1 ARG A 2 0.10 SIDE CHAIN
REMARK 500 1 ARG A 25 0.14 SIDE CHAIN
REMARK 500 1 PHE A 32 0.08 SIDE CHAIN
REMARK 500 1 TYR A 38 0.12 SIDE CHAIN
REMARK 500 1 PHE A 48 0.13 SIDE CHAIN
REMARK 500 1 ASN A 49 0.07 SIDE CHAIN
REMARK 500 1 ASN A 53 0.09 SIDE CHAIN
REMARK 500 1 HIS A 70 0.14 SIDE CHAIN
REMARK 500 1 ASN A 72 0.10 SIDE CHAIN
REMARK 500 1 HIS A 74 0.19 SIDE CHAIN
REMARK 500 1 HIS A 77 0.07 SIDE CHAIN
REMARK 500 1 ARG A 82 0.29 SIDE CHAIN
REMARK 500 1 HIS A 88 0.18 SIDE CHAIN
REMARK 500 1 ARG A 95 0.36 SIDE CHAIN
REMARK 500 1 HIS A 113 0.13 SIDE CHAIN
REMARK 500 1 PHE A 115 0.09 SIDE CHAIN
REMARK 500 1 PHE A 123 0.10 SIDE CHAIN
REMARK 500 1 ASN A 125 0.08 SIDE CHAIN
REMARK 500 1 PHE A 127 0.16 SIDE CHAIN
REMARK 500 1 HIS A 134 0.10 SIDE CHAIN
REMARK 500 1 GLU A 145 0.08 SIDE CHAIN
REMARK 500 1 ASP A 146 0.10 SIDE CHAIN
REMARK 500 1 PHE A 161 0.14 SIDE CHAIN
REMARK 500 1 PHE A 163 0.09 SIDE CHAIN
REMARK 500 1 GLU A 179 0.07 SIDE CHAIN
REMARK 500 1 GLU A 180 0.08 SIDE CHAIN
REMARK 500 1 HIS A 189 0.10 SIDE CHAIN
REMARK 500 1 HIS A 191 0.19 SIDE CHAIN
REMARK 500 1 HIS A 197 0.21 SIDE CHAIN
REMARK 500 1 ARG A 200 0.26 SIDE CHAIN
REMARK 500 10 ARG A 43 0.09 SIDE CHAIN
REMARK 500 13 ARG A 43 0.10 SIDE CHAIN
REMARK 500 18 ARG A 114 0.09 SIDE CHAIN
REMARK 500 19 ARG A 2 0.12 SIDE CHAIN
REMARK 500 19 ASN A 20 0.08 SIDE CHAIN
REMARK 500 19 ARG A 25 0.16 SIDE CHAIN
REMARK 500 19 TYR A 38 0.11 SIDE CHAIN
REMARK 500 19 PHE A 48 0.12 SIDE CHAIN
REMARK 500 19 ASN A 53 0.10 SIDE CHAIN
REMARK 500 19 HIS A 70 0.12 SIDE CHAIN
REMARK 500 19 HIS A 74 0.09 SIDE CHAIN
REMARK 500 19 HIS A 77 0.13 SIDE CHAIN
REMARK 500 19 ARG A 82 0.13 SIDE CHAIN
REMARK 500 19 ARG A 95 0.11 SIDE CHAIN
REMARK 500 19 TYR A 107 0.11 SIDE CHAIN
REMARK 500 19 ASN A 122 0.09 SIDE CHAIN
REMARK 500 19 PHE A 123 0.13 SIDE CHAIN
REMARK 500 19 GLN A 124 0.09 SIDE CHAIN
REMARK 500 19 PHE A 151 0.18 SIDE CHAIN
REMARK 500 19 PHE A 161 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 82 PLANE DEVIATIONS.
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 1 ALA A 9 -11.92
REMARK 500 1 ASN A 13 18.13
REMARK 500 1 SER A 14 12.87
REMARK 500 1 ARG A 25 -10.01
REMARK 500 1 PHE A 32 10.77
REMARK 500 1 GLY A 36 -16.71
REMARK 500 1 LEU A 47 -12.54
REMARK 500 1 PHE A 48 -13.29
REMARK 500 1 LYS A 51 10.11
REMARK 500 1 ALA A 54 15.48
REMARK 500 1 LEU A 55 11.34
REMARK 500 1 ASP A 60 12.61
REMARK 500 1 MET A 68 -21.24
REMARK 500 1 HIS A 70 15.56
REMARK 500 1 SER A 86 -13.26
REMARK 500 1 GLN A 92 14.01
REMARK 500 1 GLY A 97 -13.80
REMARK 500 1 ASP A 100 14.01
REMARK 500 1 GLY A 102 15.70
REMARK 500 1 THR A 104 -24.67
REMARK 500 1 GLN A 124 13.96
REMARK 500 1 ALA A 131 12.71
REMARK 500 1 LEU A 135 13.35
REMARK 500 1 ASN A 137 -13.73
REMARK 500 1 SER A 152 -16.17
REMARK 500 1 VAL A 158 11.91
REMARK 500 1 LYS A 159 -15.84
REMARK 500 1 MET A 170 -10.55
REMARK 500 1 GLU A 180 10.89
REMARK 500 1 ALA A 181 -12.21
REMARK 500 1 VAL A 182 -10.04
REMARK 500 1 LEU A 185 18.12
REMARK 500 1 ILE A 186 13.21
REMARK 500 1 HIS A 198 -12.27
REMARK 500 19 ALA A 9 14.40
REMARK 500 19 VAL A 18 11.96
REMARK 500 19 SER A 19 -11.99
REMARK 500 19 ASN A 20 -10.81
REMARK 500 19 ILE A 33 10.27
REMARK 500 19 GLY A 39 10.19
REMARK 500 19 LYS A 45 -18.36
REMARK 500 19 MET A 58 -13.43
REMARK 500 19 ASP A 60 10.58
REMARK 500 19 ASN A 62 -15.34
REMARK 500 19 HIS A 74 -16.69
REMARK 500 19 GLY A 78 -12.85
REMARK 500 19 LYS A 79 16.74
REMARK 500 19 SER A 86 -13.44
REMARK 500 19 ASP A 100 13.61
REMARK 500 19 LEU A 112 -12.24
REMARK 500
REMARK 500 THIS ENTRY HAS 96 MAIN CHAIN PLANARITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2EVZ A 1 208 UNP P26599 PTBP1_HUMAN 324 531
SEQADV 2EVZ MET A -20 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ GLY A -19 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ SER A -18 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ SER A -17 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ HIS A -16 UNP P26599 EXPRESSION TAG
SEQADV 2EVZ HIS A -15 UNP P26599 EXPRESSION TAG
SEQADV 2EVZ HIS A -14 UNP P26599 EXPRESSION TAG
SEQADV 2EVZ HIS A -13 UNP P26599 EXPRESSION TAG
SEQADV 2EVZ HIS A -12 UNP P26599 EXPRESSION TAG
SEQADV 2EVZ HIS A -11 UNP P26599 EXPRESSION TAG
SEQADV 2EVZ SER A -10 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ SER A -9 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ GLY A -8 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ LEU A -7 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ VAL A -6 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ PRO A -5 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ ARG A -4 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ GLY A -3 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ SER A -2 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ HIS A -1 UNP P26599 CLONING ARTIFACT
SEQADV 2EVZ MET A 0 UNP P26599 CLONING ARTIFACT
SEQRES 1 A 229 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 229 LEU VAL PRO ARG GLY SER HIS MET GLY ARG ILE ALA ILE
SEQRES 3 A 229 PRO GLY LEU ALA GLY ALA GLY ASN SER VAL LEU LEU VAL
SEQRES 4 A 229 SER ASN LEU ASN PRO GLU ARG VAL THR PRO GLN SER LEU
SEQRES 5 A 229 PHE ILE LEU PHE GLY VAL TYR GLY ASP VAL GLN ARG VAL
SEQRES 6 A 229 LYS ILE LEU PHE ASN LYS LYS GLU ASN ALA LEU VAL GLN
SEQRES 7 A 229 MET ALA ASP GLY ASN GLN ALA GLN LEU ALA MET SER HIS
SEQRES 8 A 229 LEU ASN GLY HIS LYS LEU HIS GLY LYS PRO ILE ARG ILE
SEQRES 9 A 229 THR LEU SER LYS HIS GLN ASN VAL GLN LEU PRO ARG GLU
SEQRES 10 A 229 GLY GLN GLU ASP GLN GLY LEU THR LYS ASP TYR GLY ASN
SEQRES 11 A 229 SER PRO LEU HIS ARG PHE LYS LYS PRO GLY SER LYS ASN
SEQRES 12 A 229 PHE GLN ASN ILE PHE PRO PRO SER ALA THR LEU HIS LEU
SEQRES 13 A 229 SER ASN ILE PRO PRO SER VAL SER GLU GLU ASP LEU LYS
SEQRES 14 A 229 VAL LEU PHE SER SER ASN GLY GLY VAL VAL LYS GLY PHE
SEQRES 15 A 229 LYS PHE PHE GLN LYS ASP ARG LYS MET ALA LEU ILE GLN
SEQRES 16 A 229 MET GLY SER VAL GLU GLU ALA VAL GLN ALA LEU ILE ASP
SEQRES 17 A 229 LEU HIS ASN HIS ASP LEU GLY GLU ASN HIS HIS LEU ARG
SEQRES 18 A 229 VAL SER PHE SER LYS SER THR ILE
HELIX 1 1 THR A 27 GLY A 39 1 13
HELIX 2 2 ASP A 60 ASN A 72 1 13
HELIX 3 3 ARG A 95 ASP A 100 1 6
HELIX 4 4 SER A 143 ASN A 154 1 12
HELIX 5 5 SER A 177 HIS A 189 1 13
SHEET 1 A 5 ARG A 82 LEU A 85 0
SHEET 2 A 5 VAL A 15 SER A 19 -1 N SER A 19 O ARG A 82
SHEET 3 A 5 ASN A 53 GLN A 57 -1 O VAL A 56 N LEU A 16
SHEET 4 A 5 ARG A 43 ILE A 46 -1 N ARG A 43 O GLN A 57
SHEET 5 A 5 THR A 104 LYS A 105 -1 O LYS A 105 N VAL A 44
SHEET 1 B 4 GLY A 160 PHE A 163 0
SHEET 2 B 4 ALA A 171 GLN A 174 -1 O LEU A 172 N LYS A 162
SHEET 3 B 4 LEU A 133 SER A 136 -1 N LEU A 133 O ILE A 173
SHEET 4 B 4 ARG A 200 PHE A 203 -1 O ARG A 200 N SER A 136
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
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END