HEADER TRANSCRIPTION 07-JUL-08 2RPQ
TITLE SOLUTION STRUCTURE OF A SUMO-INTERACTING MOTIF OF MBD1-CONTAINING
TITLE 2 CHROMATIN-ASSOCIATED FACTOR 1 BOUND TO SUMO-3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SMALL UBIQUITIN-RELATED MODIFIER 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SUMO-2, UBIQUITIN-LIKE PROTEIN SMT3B, SMT3 HOMOLOG 2,
COMPND 5 SENTRIN-2, HSMT3, SUMO-3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ACTIVATING TRANSCRIPTION FACTOR 7-INTERACTING PROTEIN 1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 938-981;
COMPND 11 SYNONYM: ATFA-ASSOCIATED MODULATOR, HAM, ATF-INTERACTING PROTEIN,
COMPND 12 ATF-IP, MBD1-CONTAINING CHROMATIN-ASSOCIATED FACTOR 1, P621;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PGEX-4T;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: THIS ENTITY IS CHEMICALLY SYNTHESIZED.
KEYWDS SUMO, SIM, NUCLEUS, UBL CONJUGATION PATHWAY, ACTIVATOR, HOST-VIRUS
KEYWDS 2 INTERACTION, PHOSPHOPROTEIN, REPRESSOR, TRANSCRIPTION, TRANSCRIPTION
KEYWDS 3 REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.SEKIYAMA,T.IKEGAMI,T.YAMANE,M.IKEGUCHI,Y.UCHIMURA,D.BABA,
AUTHOR 2 M.ARIYOSHI,H.TOCHIO,H.SAITOH,M.SHIRAKAWA
REVDAT 3 09-DEC-15 2RPQ 1 JRNL VERSN
REVDAT 2 24-FEB-09 2RPQ 1 VERSN
REVDAT 1 07-OCT-08 2RPQ 0
JRNL AUTH N.SEKIYAMA,T.IKEGAMI,T.YAMANE,M.IKEGUCHI,Y.UCHIMURA,D.BABA,
JRNL AUTH 2 M.ARIYOSHI,H.TOCHIO,H.SAITOH,M.SHIRAKAWA
JRNL TITL STRUCTURE OF THE SMALL UBIQUITIN-LIKE MODIFIER
JRNL TITL 2 (SUMO)-INTERACTING MOTIF OF MBD1-CONTAINING
JRNL TITL 3 CHROMATIN-ASSOCIATED FACTOR 1 BOUND TO SUMO-3
JRNL REF J.BIOL.CHEM. V. 283 35966 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18842587
JRNL DOI 10.1074/JBC.M802528200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS, MARBLE
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,
REMARK 3 JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN (CNS),
REMARK 3 IKEGUCHI, M. (MARBLE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2RPQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUL-08.
REMARK 100 THE RCSB ID CODE IS RCSB150136.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7 MM [U-100% 13C; U-100% 15N]
REMARK 210 SIMMCAF1, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D CBCA(CO)NH; 3D C(CO)NH; 3D
REMARK 210 HNCO; 3D HNCACB; 3D HBHA(CO)NH;
REMARK 210 3D HCCH-TOCSY; 3D 1H-15N NOESY;
REMARK 210 3D 1H-13C NOESY; 3D HCACO
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY B 933
REMARK 465 SER B 934
REMARK 465 PRO B 935
REMARK 465 GLU B 936
REMARK 465 PHE B 937
REMARK 465 LYS B 938
REMARK 465 THR B 939
REMARK 465 ILE B 940
REMARK 465 ASP B 941
REMARK 465 ALA B 942
REMARK 465 SER B 943
REMARK 465 VAL B 944
REMARK 465 SER B 945
REMARK 465 LYS B 946
REMARK 465 LYS B 947
REMARK 465 ALA B 948
REMARK 465 ALA B 949
REMARK 465 ASP B 950
REMARK 465 SER B 951
REMARK 465 THR B 952
REMARK 465 SER B 953
REMARK 465 GLN B 954
REMARK 465 CYS B 955
REMARK 465 GLY B 956
REMARK 465 LYS B 957
REMARK 465 ALA B 958
REMARK 465 THR B 959
REMARK 465 GLY B 960
REMARK 465 SER B 961
REMARK 465 ASP B 962
REMARK 465 SER B 963
REMARK 465 SER B 964
REMARK 465 SER B 976
REMARK 465 GLY B 977
REMARK 465 ALA B 978
REMARK 465 SER B 979
REMARK 465 GLN B 980
REMARK 465 ASP B 981
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 TYR A 47 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 1 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 PHE A 60 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 PHE A 60 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 2 PHE A 32 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 2 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 2 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 ARG A 61 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 TYR A 47 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 3 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 3 ARG A 61 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 ARG A 61 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 4 TYR A 47 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 4 TYR A 47 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 4 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 4 ARG A 61 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 4 VAL B 966 CA - CB - CG2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 5 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 5 PHE A 60 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 5 VAL B 966 CG1 - CB - CG2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 7 TYR A 47 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 7 TYR A 47 CB - CG - CD1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 7 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 7 ARG A 61 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 GLY A 64 C - N - CA ANGL. DEV. = 16.7 DEGREES
REMARK 500 7 VAL B 966 CA - CB - CG2 ANGL. DEV. = 10.8 DEGREES
REMARK 500 8 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 8 PHE A 60 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 8 PHE A 60 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 9 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 9 ARG A 50 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 9 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 10 PHE A 60 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 10 PHE A 60 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 10 ARG A 61 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 11 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 11 ARG A 50 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 12 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 12 LEU A 53 N - CA - C ANGL. DEV. = 17.0 DEGREES
REMARK 500 12 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 12 PHE A 60 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 12 PHE A 60 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 12 VAL B 966 CA - CB - CG2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 13 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 13 TYR A 47 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 13 TYR A 47 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 73 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 LYS A 7 11.18 -157.32
REMARK 500 1 ASN A 14 91.88 13.22
REMARK 500 1 ASN A 15 40.76 79.85
REMARK 500 1 ASP A 16 27.25 83.93
REMARK 500 1 VAL B 966 -97.77 -97.06
REMARK 500 1 MET B 971 25.49 -153.72
REMARK 500 1 ASP B 973 153.06 66.46
REMARK 500 2 MET B 971 26.46 84.89
REMARK 500 2 ASP B 973 28.24 -147.38
REMARK 500 3 GLU A 4 123.83 74.90
REMARK 500 3 ASN A 15 66.50 -104.99
REMARK 500 3 THR B 970 -106.66 -88.73
REMARK 500 3 MET B 971 -45.98 78.59
REMARK 500 3 ASP B 973 -146.76 50.69
REMARK 500 4 VAL B 966 -100.33 -96.41
REMARK 500 4 MET B 971 -68.13 -149.22
REMARK 500 4 ASP B 972 -75.90 -123.27
REMARK 500 5 GLN A 90 113.53 71.02
REMARK 500 5 MET B 971 123.56 101.45
REMARK 500 5 GLU B 974 48.01 -86.90
REMARK 500 6 ASN A 15 33.00 -176.18
REMARK 500 6 GLN A 89 -155.94 -107.66
REMARK 500 6 THR B 970 -145.12 -92.90
REMARK 500 6 MET B 971 103.78 80.32
REMARK 500 6 ASP B 972 -170.07 49.42
REMARK 500 6 ASP B 973 159.73 75.29
REMARK 500 7 PRO A 6 158.27 -45.77
REMARK 500 7 LYS A 11 62.10 -104.04
REMARK 500 7 GLN A 25 -65.72 76.20
REMARK 500 7 ASP A 26 22.86 -153.57
REMARK 500 7 ASP A 63 -127.04 59.67
REMARK 500 7 GLU A 81 56.36 -140.36
REMARK 500 7 VAL B 966 -110.69 -90.78
REMARK 500 7 THR B 970 -126.86 -95.07
REMARK 500 7 MET B 971 -40.29 78.76
REMARK 500 7 ASP B 973 32.50 -142.63
REMARK 500 8 ASN A 15 -75.85 -127.43
REMARK 500 8 THR B 970 -106.96 -94.09
REMARK 500 8 MET B 971 -60.99 79.12
REMARK 500 8 GLU B 974 -139.83 43.53
REMARK 500 9 PRO A 6 60.21 -100.38
REMARK 500 9 HIS A 37 31.09 -98.11
REMARK 500 9 GLN A 90 -14.16 -148.94
REMARK 500 9 MET B 971 92.30 116.52
REMARK 500 9 ASP B 972 -54.70 -173.68
REMARK 500 9 ASP B 973 20.51 -152.95
REMARK 500 9 GLU B 974 -81.21 67.96
REMARK 500 10 GLN A 90 121.14 -16.65
REMARK 500 10 MET B 971 50.88 101.72
REMARK 500 10 ASP B 972 -10.97 -153.97
REMARK 500
REMARK 500 THIS ENTRY HAS 99 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 ASP B 972 ASP B 973 1 -144.90
REMARK 500 LYS A 33 ILE A 34 3 -148.05
REMARK 500 ASP B 972 ASP B 973 6 146.59
REMARK 500 PHE A 62 ASP A 63 7 -144.91
REMARK 500 VAL B 966 ILE B 967 16 -146.66
REMARK 500 ASP B 972 ASP B 973 16 147.12
REMARK 500 ARG A 61 PHE A 62 17 -122.14
REMARK 500 GLN A 65 PRO A 66 17 148.22
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 50 0.12 SIDE CHAIN
REMARK 500 1 ARG A 59 0.10 SIDE CHAIN
REMARK 500 2 ARG A 50 0.09 SIDE CHAIN
REMARK 500 4 ARG A 61 0.09 SIDE CHAIN
REMARK 500 5 ARG A 50 0.14 SIDE CHAIN
REMARK 500 7 ARG A 56 0.08 SIDE CHAIN
REMARK 500 10 ARG A 59 0.09 SIDE CHAIN
REMARK 500 12 ARG A 59 0.07 SIDE CHAIN
REMARK 500 14 ARG A 36 0.08 SIDE CHAIN
REMARK 500 14 TYR A 47 0.06 SIDE CHAIN
REMARK 500 15 ARG A 59 0.08 SIDE CHAIN
REMARK 500 16 PHE A 32 0.13 SIDE CHAIN
REMARK 500 18 PHE A 32 0.08 SIDE CHAIN
REMARK 500 19 ARG A 59 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 1 ASN A 14 23.8 L L OUTSIDE RANGE
REMARK 500 1 LEU A 40 23.6 L L OUTSIDE RANGE
REMARK 500 3 LEU A 40 23.7 L L OUTSIDE RANGE
REMARK 500 3 LEU A 43 23.3 L L OUTSIDE RANGE
REMARK 500 3 ASP A 80 24.0 L L OUTSIDE RANGE
REMARK 500 4 LEU A 40 23.2 L L OUTSIDE RANGE
REMARK 500 5 LEU A 43 24.6 L L OUTSIDE RANGE
REMARK 500 6 LEU A 40 22.8 L L OUTSIDE RANGE
REMARK 500 6 ASP A 80 23.9 L L OUTSIDE RANGE
REMARK 500 7 LEU A 40 23.5 L L OUTSIDE RANGE
REMARK 500 8 LEU A 40 24.3 L L OUTSIDE RANGE
REMARK 500 8 ASP A 80 24.6 L L OUTSIDE RANGE
REMARK 500 9 LEU A 40 24.9 L L OUTSIDE RANGE
REMARK 500 9 MET B 971 24.4 L L OUTSIDE RANGE
REMARK 500 10 ASP A 80 22.2 L L OUTSIDE RANGE
REMARK 500 11 GLN A 90 23.3 L L OUTSIDE RANGE
REMARK 500 12 ARG A 50 24.1 L L OUTSIDE RANGE
REMARK 500 12 LEU A 53 10.2 L L OUTSIDE RANGE
REMARK 500 13 LEU A 40 24.4 L L OUTSIDE RANGE
REMARK 500 13 MET B 971 24.1 L L OUTSIDE RANGE
REMARK 500 14 ASP A 80 25.0 L L OUTSIDE RANGE
REMARK 500 15 LEU A 40 22.9 L L OUTSIDE RANGE
REMARK 500 15 PRO A 66 23.2 L L OUTSIDE RANGE
REMARK 500 16 ASP A 80 24.5 L L OUTSIDE RANGE
REMARK 500 16 MET B 971 24.3 L L OUTSIDE RANGE
REMARK 500 17 PHE A 62 64.4 L L OUTSIDE RANGE
REMARK 500 17 ASP A 80 24.7 L L OUTSIDE RANGE
REMARK 500 17 GLN A 90 24.9 L L OUTSIDE RANGE
REMARK 500 18 LEU A 40 24.3 L L OUTSIDE RANGE
REMARK 500 20 LEU A 40 24.1 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2RPQ A 1 93 UNP P61956 SUMO2_HUMAN 1 93
DBREF 2RPQ B 938 981 UNP Q6VMQ6 MCAF1_HUMAN 938 981
SEQADV 2RPQ GLY B 933 UNP Q6VMQ6 EXPRESSION TAG
SEQADV 2RPQ SER B 934 UNP Q6VMQ6 EXPRESSION TAG
SEQADV 2RPQ PRO B 935 UNP Q6VMQ6 EXPRESSION TAG
SEQADV 2RPQ GLU B 936 UNP Q6VMQ6 EXPRESSION TAG
SEQADV 2RPQ PHE B 937 UNP Q6VMQ6 EXPRESSION TAG
SEQRES 1 A 93 MET ALA ASP GLU LYS PRO LYS GLU GLY VAL LYS THR GLU
SEQRES 2 A 93 ASN ASN ASP HIS ILE ASN LEU LYS VAL ALA GLY GLN ASP
SEQRES 3 A 93 GLY SER VAL VAL GLN PHE LYS ILE LYS ARG HIS THR PRO
SEQRES 4 A 93 LEU SER LYS LEU MET LYS ALA TYR CYS GLU ARG GLN GLY
SEQRES 5 A 93 LEU SER MET ARG GLN ILE ARG PHE ARG PHE ASP GLY GLN
SEQRES 6 A 93 PRO ILE ASN GLU THR ASP THR PRO ALA GLN LEU GLU MET
SEQRES 7 A 93 GLU ASP GLU ASP THR ILE ASP VAL PHE GLN GLN GLN THR
SEQRES 8 A 93 GLY GLY
SEQRES 1 B 49 GLY SER PRO GLU PHE LYS THR ILE ASP ALA SER VAL SER
SEQRES 2 B 49 LYS LYS ALA ALA ASP SER THR SER GLN CYS GLY LYS ALA
SEQRES 3 B 49 THR GLY SER ASP SER SER GLY VAL ILE ASP LEU THR MET
SEQRES 4 B 49 ASP ASP GLU GLU SER GLY ALA SER GLN ASP
HELIX 1 1 PRO A 39 GLY A 52 1 14
SHEET 1 A 6 GLN A 65 ILE A 67 0
SHEET 2 A 6 ILE A 58 PHE A 62 -1 N PHE A 62 O GLN A 65
SHEET 3 A 6 GLU A 81 GLN A 88 -1 O ASP A 85 N ARG A 61
SHEET 4 A 6 HIS A 17 ALA A 23 1 N ALA A 23 O ILE A 84
SHEET 5 A 6 VAL A 29 LYS A 35 -1 O PHE A 32 N LEU A 20
CISPEP 1 MET A 1 ALA A 2 2 -16.32
CISPEP 2 ASP A 63 GLY A 64 7 7.29
CISPEP 3 MET A 1 ALA A 2 9 -12.34
CISPEP 4 PRO A 66 ILE A 67 15 17.77
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