deposited structure
Protein structure (pdb format)Metadata
Standardised name
deposited structure
Size
1.498 MB
UUID in database
088eb247
UUID on disk
037ed235
File content
(First 500 lines only)
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 22-DEC-09 2KRS
TITLE SOLUTION NMR STRUCTURE OF SH3 DOMAIN FROM CPF_0587 (FRAGMENT
TITLE 2 415-479) FROM CLOSTRIDIUM PERFRINGENS. NORTHEAST STRUCTURAL
TITLE 3 GENOMICS CONSORTIUM (NESG) TARGET CPR74A.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE ENTEROTOXIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN, RESIDUES 497-561;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PERFRINGENS;
SOURCE 3 ORGANISM_TAXID: 1502;
SOURCE 4 GENE: CPE0606, CPF_0587, ENTD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PMGK;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21-23C
KEYWDS ALL BETA, SH3, ENTD, CPF_0587, CPE0606, STRUCTURAL GENOMICS,
KEYWDS 2 PSI-2, PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL
KEYWDS 3 GENOMICS CONSORTIUM, NESG
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.A.RAMELOT,J.R.CORT,M.MAGLAQUI,C.CICCOSANTI,H.JANJUA,
AUTHOR 2 R.NAIR,B.ROST,T.B.ACTON,R.XIAO,J.K.EVERETT,G.T.MONTELIONE,
AUTHOR 3 M.A.KENNEDY,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 1 26-JAN-10 2KRS 0
JRNL AUTH T.A.RAMELOT,J.R.CORT,M.MAGLAQUI,C.CICCOSANTI,
JRNL AUTH 2 H.JANJUA,R.NAIR,B.ROST,T.B.ACTON,R.XIAO,
JRNL AUTH 3 J.K.EVERETT,G.T.MONTELIONE,M.A.KENNEDY
JRNL TITL SOLUTION NMR STRUCTURE OF SH3 DOMAIN FROM CPF_0587
JRNL TITL 2 (FRAGMENT 415-479) FROM CLOSTRIDIUM PERFRINGENS.
JRNL TITL 3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
JRNL TITL 4 TARGET CPR74A.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NIH-XPLOR HBDB REFINEMENT
REMARK 4
REMARK 4 2KRS COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-DEC-09.
REMARK 100 THE RCSB ID CODE IS RCSB101493.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20 MM MES, 100 MM SODIUM
REMARK 210 CHLORIDE, 5 MM CALCIUM
REMARK 210 CHLORIDE, 10 MM DTT, 0.02 %
REMARK 210 SODIUM AZIDE, 0.8 MM [U-100%
REMARK 210 13C; U-100% 15N] PROTEIN, 95%
REMARK 210 H2O/5% D2O; 20 MM MES, 100 MM
REMARK 210 SODIUM CHLORIDE, 5 MM CALCIUM
REMARK 210 CHLORIDE, 10 MM DTT, 0.02 %
REMARK 210 SODIUM AZIDE, 0.8 MM [U-100%
REMARK 210 13C; U-100% 15N] PROTEIN, 100%
REMARK 210 D2O; 20 MM MES, 100 MM SODIUM
REMARK 210 CHLORIDE, 5 MM CALCIUM
REMARK 210 CHLORIDE, 10 MM DTT, 0.02 %
REMARK 210 SODIUM AZIDE, 0.9 MM [U-5%
REMARK 210 13C; U-100% 15N] PROTEIN, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C
REMARK 210 HSQC; 3D 1H-15N NOESY; 3D 1H-
REMARK 210 13C NOESY ALIPH; 3D HNCO; 3D
REMARK 210 HN(CO)CA; 3D CBCA(CO)NH; 3D
REMARK 210 HNCACB; 3D HBHA(CO)NH; 3D HCCH
REMARK 210 -TOCSY; 3D HCCH-COSY; 3D (H)
REMARK 210 CCH-TOCSY; 4D HCCH NOESY; 3D
REMARK 210 1H-13C NOESY AROM
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 850 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AVANCEIII
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2008, VNMR 6.1C,
REMARK 210 TOPSPIN 2.1.4, AUTOSTRUCTURE
REMARK 210 2.2.1, X-PLOR_NIH 2.20, SPARKY
REMARK 210 3.113, PSVS 1.3, AUTOASSIGN
REMARK 210 2.3.0, PDBSTAT 5.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 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 HH11 ARG A 14 HA SER A 19 1.51
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 2 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 3 ARG A 14 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 3 ARG A 28 NE - CZ - NH1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 3 ARG A 28 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ARG A 46 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 10 ARG A 28 CG - CD - NE ANGL. DEV. = -12.6 DEGREES
REMARK 500 14 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 15 ARG A 46 CD - NE - CZ ANGL. DEV. = -13.5 DEGREES
REMARK 500 17 ARG A 14 CD - NE - CZ ANGL. DEV. = -8.9 DEGREES
REMARK 500 18 ARG A 46 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 18 ARG A 46 NE - CZ - NH2 ANGL. DEV. = 3.5 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 1 SER A 9 -75.12 -119.06
REMARK 500 1 GLU A 64 58.65 -68.52
REMARK 500 1 LEU A 67 -6.38 -148.98
REMARK 500 1 HIS A 70 40.41 38.63
REMARK 500 2 SER A 9 -51.62 -143.68
REMARK 500 2 ASN A 63 -145.11 79.83
REMARK 500 3 SER A 9 -76.73 -130.87
REMARK 500 3 ASN A 30 13.18 59.29
REMARK 500 3 SER A 66 96.65 56.65
REMARK 500 3 GLU A 68 -105.62 -159.38
REMARK 500 3 HIS A 69 85.88 40.42
REMARK 500 3 HIS A 71 120.56 57.11
REMARK 500 3 HIS A 73 94.23 -168.76
REMARK 500 4 PRO A 17 12.27 -69.94
REMARK 500 4 ASN A 30 3.16 59.41
REMARK 500 4 GLU A 64 -170.04 -52.57
REMARK 500 4 LEU A 67 177.32 58.39
REMARK 500 4 HIS A 70 -107.64 48.67
REMARK 500 4 HIS A 71 -47.39 -148.12
REMARK 500 4 HIS A 73 -178.31 56.91
REMARK 500 5 ASN A 30 -27.85 71.03
REMARK 500 5 ASN A 63 -164.75 66.80
REMARK 500 5 GLU A 64 102.73 54.74
REMARK 500 5 SER A 66 -62.71 64.82
REMARK 500 5 LEU A 67 -168.60 56.20
REMARK 500 5 GLU A 68 92.04 54.87
REMARK 500 5 HIS A 73 -95.39 55.16
REMARK 500 6 SER A 9 -57.58 -136.59
REMARK 500 6 ASN A 63 97.74 -40.78
REMARK 500 6 GLU A 64 -95.72 -68.59
REMARK 500 6 HIS A 69 -130.77 -152.47
REMARK 500 6 HIS A 70 -115.52 47.90
REMARK 500 6 HIS A 71 83.83 39.04
REMARK 500 7 SER A 9 -68.47 -130.14
REMARK 500 7 ASN A 29 153.38 -46.65
REMARK 500 7 ILE A 36 -61.31 -93.63
REMARK 500 7 GLU A 64 -26.03 -146.95
REMARK 500 7 SER A 66 18.18 -141.25
REMARK 500 7 HIS A 70 98.65 46.52
REMARK 500 8 SER A 9 -67.19 -125.07
REMARK 500 8 PRO A 17 86.32 -68.32
REMARK 500 8 ASN A 63 91.42 61.69
REMARK 500 8 GLU A 68 92.19 54.31
REMARK 500 9 SER A 66 83.36 51.43
REMARK 500 9 HIS A 70 -173.66 45.02
REMARK 500 10 SER A 9 -53.33 -150.70
REMARK 500 10 ILE A 36 -62.97 -94.71
REMARK 500 10 ASN A 63 -172.17 45.33
REMARK 500 10 GLU A 64 69.32 66.25
REMARK 500 11 SER A 9 -153.84 -136.76
REMARK 500
REMARK 500 THIS ENTRY HAS 91 RAMACHANDRAN OUTLIERS.
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 14 0.15 SIDE CHAIN
REMARK 500 1 ARG A 28 0.17 SIDE CHAIN
REMARK 500 2 ARG A 46 0.20 SIDE CHAIN
REMARK 500 3 ARG A 14 0.21 SIDE CHAIN
REMARK 500 4 ARG A 14 0.10 SIDE CHAIN
REMARK 500 4 ARG A 28 0.14 SIDE CHAIN
REMARK 500 4 ARG A 46 0.21 SIDE CHAIN
REMARK 500 5 ARG A 14 0.29 SIDE CHAIN
REMARK 500 5 ARG A 28 0.12 SIDE CHAIN
REMARK 500 5 ARG A 46 0.11 SIDE CHAIN
REMARK 500 7 ARG A 14 0.20 SIDE CHAIN
REMARK 500 7 ARG A 28 0.12 SIDE CHAIN
REMARK 500 8 ARG A 14 0.14 SIDE CHAIN
REMARK 500 8 ARG A 28 0.20 SIDE CHAIN
REMARK 500 8 ARG A 46 0.13 SIDE CHAIN
REMARK 500 9 ARG A 14 0.27 SIDE CHAIN
REMARK 500 9 ARG A 28 0.09 SIDE CHAIN
REMARK 500 9 ARG A 46 0.28 SIDE CHAIN
REMARK 500 10 ARG A 28 0.25 SIDE CHAIN
REMARK 500 10 ARG A 46 0.11 SIDE CHAIN
REMARK 500 11 ARG A 28 0.10 SIDE CHAIN
REMARK 500 12 ARG A 14 0.20 SIDE CHAIN
REMARK 500 12 ARG A 28 0.12 SIDE CHAIN
REMARK 500 13 ARG A 14 0.16 SIDE CHAIN
REMARK 500 13 ARG A 28 0.14 SIDE CHAIN
REMARK 500 13 ARG A 46 0.10 SIDE CHAIN
REMARK 500 14 ARG A 14 0.11 SIDE CHAIN
REMARK 500 14 ARG A 28 0.26 SIDE CHAIN
REMARK 500 14 ARG A 46 0.25 SIDE CHAIN
REMARK 500 15 ARG A 28 0.11 SIDE CHAIN
REMARK 500 15 ARG A 46 0.33 SIDE CHAIN
REMARK 500 16 ARG A 14 0.11 SIDE CHAIN
REMARK 500 16 ARG A 28 0.10 SIDE CHAIN
REMARK 500 16 ARG A 46 0.09 SIDE CHAIN
REMARK 500 17 ARG A 14 0.29 SIDE CHAIN
REMARK 500 17 ARG A 28 0.08 SIDE CHAIN
REMARK 500 18 ARG A 14 0.23 SIDE CHAIN
REMARK 500 18 ARG A 28 0.14 SIDE CHAIN
REMARK 500 18 ARG A 46 0.32 SIDE CHAIN
REMARK 500 20 ARG A 28 0.18 SIDE CHAIN
REMARK 500 20 ARG A 46 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CPR74A RELATED DB: TARGETDB
REMARK 900 RELATED ID: 16647 RELATED DB: BMRB
DBREF 2KRS A 2 66 UNP Q8XMT2 Q8XMT2_CLOPE 497 561
SEQADV 2KRS MET A 1 UNP Q8XMT2 EXPRESSION TAG
SEQADV 2KRS LEU A 67 UNP Q8XMT2 EXPRESSION TAG
SEQADV 2KRS GLU A 68 UNP Q8XMT2 EXPRESSION TAG
SEQADV 2KRS HIS A 69 UNP Q8XMT2 EXPRESSION TAG
SEQADV 2KRS HIS A 70 UNP Q8XMT2 EXPRESSION TAG
SEQADV 2KRS HIS A 71 UNP Q8XMT2 EXPRESSION TAG
SEQADV 2KRS HIS A 72 UNP Q8XMT2 EXPRESSION TAG
SEQADV 2KRS HIS A 73 UNP Q8XMT2 EXPRESSION TAG
SEQADV 2KRS HIS A 74 UNP Q8XMT2 EXPRESSION TAG
SEQRES 1 A 74 MET GLN GLY VAL VAL LYS VAL ASN SER ALA LEU ASN MET
SEQRES 2 A 74 ARG SER GLY PRO GLY SER ASN TYR GLY VAL ILE GLY THR
SEQRES 3 A 74 LEU ARG ASN ASN ASP LYS VAL GLU ILE ILE LYS GLU VAL
SEQRES 4 A 74 ASP GLY TRP TYR GLU ILE ARG PHE ASN GLY LYS VAL GLY
SEQRES 5 A 74 TYR ALA SER LYS SER TYR ILE THR ILE VAL ASN GLU GLY
SEQRES 6 A 74 SER LEU GLU HIS HIS HIS HIS HIS HIS
SHEET 1 A 5 LYS A 50 ALA A 54 0
SHEET 2 A 5 TRP A 42 PHE A 47 -1 N PHE A 47 O LYS A 50
SHEET 3 A 5 LYS A 32 VAL A 39 -1 N LYS A 37 O GLU A 44
SHEET 4 A 5 GLY A 3 VAL A 5 -1 N GLY A 3 O VAL A 33
SHEET 5 A 5 ILE A 59 ILE A 61 -1 O THR A 60 N VAL A 4
SHEET 1 B 2 ALA A 10 ARG A 14 0
SHEET 2 B 2 VAL A 23 ARG A 28 -1 O LEU A 27 N LEU A 11
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 1 N MET A 1 0.297 15.075 1.325 1.00 0.00
ATOM 2 CA MET A 1 1.120 13.836 1.233 1.00 0.00
ATOM 3 C MET A 1 0.507 12.904 0.194 1.00 0.00
ATOM 4 O MET A 1 -0.706 12.695 0.173 1.00 0.00
ATOM 5 CB MET A 1 1.152 13.147 2.600 1.00 0.00
ATOM 6 CG MET A 1 2.155 11.991 2.573 1.00 0.00
ATOM 7 SD MET A 1 3.836 12.654 2.427 1.00 0.00
ATOM 8 CE MET A 1 4.334 12.451 4.156 1.00 0.00
ATOM 9 H MET A 1 0.728 15.822 0.745 1.00 0.00
ATOM 10 HA MET A 1 2.125 14.094 0.936 1.00 0.00
ATOM 11 HB2 MET A 1 1.446 13.861 3.355 1.00 0.00
ATOM 12 HB3 MET A 1 0.170 12.763 2.832 1.00 0.00
ATOM 13 HG2 MET A 1 2.066 11.417 3.484 1.00 0.00
ATOM 14 HG3 MET A 1 1.945 11.353 1.727 1.00 0.00
ATOM 15 HE1 MET A 1 4.282 11.405 4.424 1.00 0.00
ATOM 16 HE2 MET A 1 3.671 13.024 4.790 1.00 0.00
ATOM 17 HE3 MET A 1 5.344 12.804 4.286 1.00 0.00
ATOM 18 N GLN A 2 1.352 12.346 -0.672 1.00 0.00
ATOM 19 CA GLN A 2 0.881 11.437 -1.716 1.00 0.00
ATOM 20 C GLN A 2 1.931 10.366 -2.008 1.00 0.00
ATOM 21 O GLN A 2 3.037 10.669 -2.454 1.00 0.00
ATOM 22 CB GLN A 2 0.568 12.225 -2.996 1.00 0.00
ATOM 23 CG GLN A 2 1.628 13.311 -3.214 1.00 0.00
ATOM 24 CD GLN A 2 1.392 14.478 -2.260 1.00 0.00
ATOM 25 OE1 GLN A 2 0.272 14.979 -2.157 1.00 0.00
ATOM 26 NE2 GLN A 2 2.386 14.941 -1.552 1.00 0.00
ATOM 27 H GLN A 2 2.309 12.551 -0.609 1.00 0.00
ATOM 28 HA GLN A 2 -0.024 10.948 -1.380 1.00 0.00
ATOM 29 HB2 GLN A 2 0.560 11.555 -3.844 1.00 0.00
ATOM 30 HB3 GLN A 2 -0.403 12.690 -2.902 1.00 0.00
ATOM 31 HG2 GLN A 2 2.608 12.896 -3.034 1.00 0.00
ATOM 32 HG3 GLN A 2 1.572 13.666 -4.232 1.00 0.00
ATOM 33 HE21 GLN A 2 3.276 14.539 -1.636 1.00 0.00
ATOM 34 HE22 GLN A 2 2.243 15.690 -0.937 1.00 0.00
ATOM 35 N GLY A 3 1.570 9.110 -1.756 1.00 0.00
ATOM 36 CA GLY A 3 2.479 7.993 -1.999 1.00 0.00
ATOM 37 C GLY A 3 2.336 7.486 -3.430 1.00 0.00
ATOM 38 O GLY A 3 1.258 7.565 -4.019 1.00 0.00
ATOM 39 H GLY A 3 0.673 8.931 -1.405 1.00 0.00
ATOM 40 HA2 GLY A 3 3.498 8.314 -1.834 1.00 0.00
ATOM 41 HA3 GLY A 3 2.244 7.190 -1.317 1.00 0.00
ATOM 42 N VAL A 4 3.429 6.959 -3.985 1.00 0.00
ATOM 43 CA VAL A 4 3.418 6.432 -5.354 1.00 0.00
ATOM 44 C VAL A 4 3.837 4.965 -5.347 1.00 0.00
ATOM 45 O VAL A 4 4.865 4.605 -4.774 1.00 0.00
ATOM 46 CB VAL A 4 4.386 7.243 -6.226 1.00 0.00
ATOM 47 CG1 VAL A 4 4.571 6.560 -7.586 1.00 0.00
ATOM 48 CG2 VAL A 4 3.820 8.649 -6.437 1.00 0.00
ATOM 49 H VAL A 4 4.260 6.920 -3.464 1.00 0.00
ATOM 50 HA VAL A 4 2.422 6.511 -5.772 1.00 0.00
ATOM 51 HB VAL A 4 5.343 7.312 -5.728 1.00 0.00
ATOM 52 HG11 VAL A 4 5.039 7.249 -8.274 1.00 0.00
ATOM 53 HG12 VAL A 4 3.609 6.262 -7.974 1.00 0.00
ATOM 54 HG13 VAL A 4 5.198 5.688 -7.469 1.00 0.00
ATOM 55 HG21 VAL A 4 2.918 8.589 -7.029 1.00 0.00
ATOM 56 HG22 VAL A 4 4.549 9.257 -6.953 1.00 0.00
ATOM 57 HG23 VAL A 4 3.593 9.094 -5.480 1.00 0.00
ATOM 58 N VAL A 5 3.034 4.123 -5.994 1.00 0.00
ATOM 59 CA VAL A 5 3.328 2.693 -6.065 1.00 0.00
ATOM 60 C VAL A 5 4.102 2.379 -7.335 1.00 0.00
ATOM 61 O VAL A 5 3.672 2.727 -8.436 1.00 0.00
ATOM 62 CB VAL A 5 2.025 1.892 -6.056 1.00 0.00
ATOM 63 CG1 VAL A 5 2.341 0.402 -6.199 1.00 0.00
ATOM 64 CG2 VAL A 5 1.288 2.133 -4.736 1.00 0.00
ATOM 65 H VAL A 5 2.230 4.469 -6.434 1.00 0.00
ATOM 66 HA VAL A 5 3.922 2.402 -5.209 1.00 0.00
ATOM 67 HB VAL A 5 1.403 2.209 -6.881 1.00 0.00
ATOM 68 HG11 VAL A 5 1.453 -0.175 -5.988 1.00 0.00
ATOM 69 HG12 VAL A 5 3.121 0.130 -5.504 1.00 0.00
ATOM 70 HG13 VAL A 5 2.671 0.199 -7.207 1.00 0.00
ATOM 71 HG21 VAL A 5 0.477 1.426 -4.643 1.00 0.00
ATOM 72 HG22 VAL A 5 0.894 3.138 -4.722 1.00 0.00
ATOM 73 HG23 VAL A 5 1.974 2.004 -3.912 1.00 0.00
ATOM 74 N LYS A 6 5.249 1.717 -7.180 1.00 0.00
ATOM 75 CA LYS A 6 6.085 1.353 -8.326 1.00 0.00
ATOM 76 C LYS A 6 6.219 -0.163 -8.418 1.00 0.00
ATOM 77 O LYS A 6 6.862 -0.793 -7.579 1.00 0.00
ATOM 78 CB LYS A 6 7.475 1.990 -8.175 1.00 0.00
ATOM 79 CG LYS A 6 8.192 2.035 -9.540 1.00 0.00
ATOM 80 CD LYS A 6 7.798 3.309 -10.300 1.00 0.00
ATOM 81 CE LYS A 6 8.566 3.374 -11.620 1.00 0.00
ATOM 82 NZ LYS A 6 8.172 4.605 -12.362 1.00 0.00
ATOM 83 H LYS A 6 5.538 1.467 -6.277 1.00 0.00
ATOM 84 HA LYS A 6 5.631 1.713 -9.237 1.00 0.00
ATOM 85 HB2 LYS A 6 7.367 2.994 -7.785 1.00 0.00
ATOM 86 HB3 LYS A 6 8.063 1.405 -7.482 1.00 0.00
ATOM 87 HG2 LYS A 6 9.261 2.031 -9.383 1.00 0.00
ATOM 88 HG3 LYS A 6 7.915 1.170 -10.127 1.00 0.00
ATOM 89 HD2 LYS A 6 6.738 3.300 -10.501 1.00 0.00
ATOM 90 HD3 LYS A 6 8.043 4.174 -9.702 1.00 0.00
ATOM 91 HE2 LYS A 6 9.626 3.399 -11.420 1.00 0.00
ATOM 92 HE3 LYS A 6 8.331 2.505 -12.216 1.00 0.00
ATOM 93 HZ1 LYS A 6 7.138 4.705 -12.344 1.00 0.00
ATOM 94 HZ2 LYS A 6 8.495 4.535 -13.348 1.00 0.00
ATOM 95 HZ3 LYS A 6 8.610 5.435 -11.911 1.00 0.00
ATOM 96 N VAL A 7 5.606 -0.742 -9.448 1.00 0.00
ATOM 97 CA VAL A 7 5.654 -2.189 -9.657 1.00 0.00
ATOM 98 C VAL A 7 5.706 -2.501 -11.149 1.00 0.00
ATOM 99 O VAL A 7 5.101 -1.799 -11.960 1.00 0.00
ATOM 100 CB VAL A 7 4.424 -2.845 -9.028 1.00 0.00
ATOM 101 CG1 VAL A 7 3.160 -2.327 -9.717 1.00 0.00
ATOM 102 CG2 VAL A 7 4.510 -4.366 -9.191 1.00 0.00
ATOM 103 H VAL A 7 5.110 -0.184 -10.082 1.00 0.00
ATOM 104 HA VAL A 7 6.542 -2.590 -9.188 1.00 0.00
ATOM 105 HB VAL A 7 4.385 -2.596 -7.977 1.00 0.00
ATOM 106 HG11 VAL A 7 2.299 -2.565 -9.111 1.00 0.00
ATOM 107 HG12 VAL A 7 3.059 -2.794 -10.686 1.00 0.00
ATOM 108 HG13 VAL A 7 3.229 -1.256 -9.838 1.00 0.00
ATOM 109 HG21 VAL A 7 5.513 -4.698 -8.964 1.00 0.00
ATOM 110 HG22 VAL A 7 4.263 -4.635 -10.207 1.00 0.00
ATOM 111 HG23 VAL A 7 3.814 -4.839 -8.515 1.00 0.00
ATOM 112 N ASN A 8 6.434 -3.552 -11.506 1.00 0.00
ATOM 113 CA ASN A 8 6.560 -3.936 -12.907 1.00 0.00
ATOM 114 C ASN A 8 5.204 -4.339 -13.480 1.00 0.00
ATOM 115 O ASN A 8 4.873 -3.991 -14.614 1.00 0.00
ATOM 116 CB ASN A 8 7.539 -5.104 -13.040 1.00 0.00
ATOM 117 CG ASN A 8 8.962 -4.627 -12.766 1.00 0.00
ATOM 118 OD1 ASN A 8 9.239 -3.429 -12.829 1.00 0.00
ATOM 119 ND2 ASN A 8 9.884 -5.499 -12.462 1.00 0.00
ATOM 120 H ASN A 8 6.899 -4.073 -10.819 1.00 0.00
ATOM 121 HA ASN A 8 6.942 -3.096 -13.466 1.00 0.00
ATOM 122 HB2 ASN A 8 7.276 -5.875 -12.331 1.00 0.00
ATOM 123 HB3 ASN A 8 7.485 -5.504 -14.041 1.00 0.00
ATOM 124 HD21 ASN A 8 9.660 -6.452 -12.412 1.00 0.00
ATOM 125 HD22 ASN A 8 10.801 -5.202 -12.283 1.00 0.00
ATOM 126 N SER A 9 4.422 -5.079 -12.690 1.00 0.00
ATOM 127 CA SER A 9 3.095 -5.535 -13.124 1.00 0.00
ATOM 128 C SER A 9 2.000 -4.985 -12.208 1.00 0.00
ATOM 129 O SER A 9 1.270 -4.067 -12.582 1.00 0.00
ATOM 130 CB SER A 9 3.049 -7.064 -13.113 1.00 0.00
ATOM 131 OG SER A 9 3.834 -7.565 -14.187 1.00 0.00
ATOM 132 H SER A 9 4.744 -5.327 -11.800 1.00 0.00
ATOM 133 HA SER A 9 2.905 -5.193 -14.132 1.00 0.00
ATOM 134 HB2 SER A 9 3.446 -7.432 -12.182 1.00 0.00
ATOM 135 HB3 SER A 9 2.023 -7.392 -13.219 1.00 0.00
ATOM 136 HG SER A 9 4.733 -7.679 -13.870 1.00 0.00
ATOM 137 N ALA A 10 1.887 -5.557 -11.011 1.00 0.00
ATOM 138 CA ALA A 10 0.871 -5.121 -10.052 1.00 0.00
ATOM 139 C ALA A 10 1.277 -5.511 -8.633 1.00 0.00
ATOM 140 O ALA A 10 1.908 -6.546 -8.419 1.00 0.00
ATOM 141 CB ALA A 10 -0.486 -5.740 -10.399 1.00 0.00
ATOM 142 H ALA A 10 2.493 -6.288 -10.769 1.00 0.00
ATOM 143 HA ALA A 10 0.784 -4.046 -10.103 1.00 0.00
ATOM 144 HB1 ALA A 10 -0.363 -6.795 -10.592 1.00 0.00
ATOM 145 HB2 ALA A 10 -0.887 -5.256 -11.279 1.00 0.00
ATOM 146 HB3 ALA A 10 -1.168 -5.601 -9.572 1.00 0.00
ATOM 147 N LEU A 11 0.925 -4.665 -7.664 1.00 0.00
ATOM 148 CA LEU A 11 1.269 -4.912 -6.259 1.00 0.00
ATOM 149 C LEU A 11 0.018 -5.278 -5.469 1.00 0.00
ATOM 150 O LEU A 11 -1.000 -4.598 -5.552 1.00 0.00
ATOM 151 CB LEU A 11 1.900 -3.643 -5.666 1.00 0.00
ATOM 152 CG LEU A 11 2.291 -3.852 -4.191 1.00 0.00
ATOM 153 CD1 LEU A 11 3.379 -4.931 -4.077 1.00 0.00
ATOM 154 CD2 LEU A 11 2.818 -2.523 -3.626 1.00 0.00
ATOM 155 H LEU A 11 0.431 -3.851 -7.898 1.00 0.00
ATOM 156 HA LEU A 11 1.980 -5.723 -6.195 1.00 0.00
ATOM 157 HB2 LEU A 11 2.781 -3.386 -6.233 1.00 0.00
ATOM 158 HB3 LEU A 11 1.189 -2.833 -5.731 1.00 0.00
ATOM 159 HG LEU A 11 1.424 -4.159 -3.625 1.00 0.00
ATOM 160 HD11 LEU A 11 3.930 -4.797 -3.157 1.00 0.00
ATOM 161 HD12 LEU A 11 4.057 -4.856 -4.914 1.00 0.00
ATOM 162 HD13 LEU A 11 2.917 -5.908 -4.075 1.00 0.00
ATOM 163 HD21 LEU A 11 3.474 -2.057 -4.348 1.00 0.00
ATOM 164 HD22 LEU A 11 3.363 -2.710 -2.712 1.00 0.00
ATOM 165 HD23 LEU A 11 1.987 -1.866 -3.420 1.00 0.00
ATOM 166 N ASN A 12 0.101 -6.357 -4.700 1.00 0.00
ATOM 167 CA ASN A 12 -1.037 -6.797 -3.899 1.00 0.00
ATOM 168 C ASN A 12 -1.133 -5.986 -2.607 1.00 0.00
ATOM 169 O ASN A 12 -0.116 -5.597 -2.032 1.00 0.00
ATOM 170 CB ASN A 12 -0.892 -8.284 -3.574 1.00 0.00
ATOM 171 CG ASN A 12 -1.023 -9.109 -4.850 1.00 0.00
ATOM 172 OD1 ASN A 12 -0.539 -10.239 -4.910 1.00 0.00
ATOM 173 ND2 ASN A 12 -1.651 -8.610 -5.880 1.00 0.00
ATOM 174 H ASN A 12 0.938 -6.866 -4.672 1.00 0.00
ATOM 175 HA ASN A 12 -1.944 -6.651 -4.463 1.00 0.00
ATOM 176 HB2 ASN A 12 0.076 -8.460 -3.129 1.00 0.00
ATOM 177 HB3 ASN A 12 -1.663 -8.574 -2.880 1.00 0.00
ATOM 178 HD21 ASN A 12 -2.035 -7.712 -5.833 1.00 0.00
ATOM 179 HD22 ASN A 12 -1.737 -9.135 -6.702 1.00 0.00
ATOM 180 N MET A 13 -2.369 -5.738 -2.156 1.00 0.00
ATOM 181 CA MET A 13 -2.607 -4.972 -0.923 1.00 0.00
ATOM 182 C MET A 13 -3.066 -5.913 0.181 1.00 0.00
ATOM 183 O MET A 13 -3.659 -6.954 -0.096 1.00 0.00
ATOM 184 CB MET A 13 -3.656 -3.887 -1.164 1.00 0.00
ATOM 185 CG MET A 13 -3.716 -2.969 0.059 1.00 0.00
ATOM 186 SD MET A 13 -4.756 -1.535 -0.303 1.00 0.00
ATOM 187 CE MET A 13 -6.332 -2.278 0.172 1.00 0.00
ATOM 188 H MET A 13 -3.136 -6.081 -2.659 1.00 0.00
ATOM 189 HA MET A 13 -1.683 -4.500 -0.612 1.00 0.00
ATOM 190 HB2 MET A 13 -3.388 -3.311 -2.038 1.00 0.00
ATOM 191 HB3 MET A 13 -4.619 -4.347 -1.316 1.00 0.00
ATOM 192 HG2 MET A 13 -4.130 -3.513 0.896 1.00 0.00
ATOM 193 HG3 MET A 13 -2.720 -2.636 0.307 1.00 0.00