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4kf8.pdb
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HEADER STRUCTURAL PROTEIN 26-APR-13 4KF8
TITLE NUP188(AA1445-1827) FROM MYCELIOPHTHORA THERMOPHILA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUP188;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUES 1445-1827);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCELIOPHTHORA THERMOPHILA;
SOURCE 3 ORGANISM_TAXID: 78579;
SOURCE 4 GENE: MYCTH_2303581;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NUCLEOPORIN, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.U.SCHWARTZ,K.R.ANDERSEN
REVDAT 2 14-AUG-13 4KF8 1 JRNL
REVDAT 1 19-JUN-13 4KF8 0
JRNL AUTH K.R.ANDERSEN,E.ONISCHENKO,J.H.TANG,P.KUMAR,J.Z.CHEN,
JRNL AUTH 2 A.ULRICH,J.T.LIPHARDT,K.WEIS,T.U.SCHWARTZ
JRNL TITL SCAFFOLD NUCLEOPORINS NUP188 AND NUP192 SHARE STRUCTURAL AND
JRNL TITL 2 FUNCTIONAL PROPERTIES WITH NUCLEAR TRANSPORT RECEPTORS.
JRNL REF ELIFE V. 2 00745 2013
JRNL REFN ESSN 2050-084X
JRNL PMID 23795296
JRNL DOI 10.7554/ELIFE.00745
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 4.800
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 14536
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.277
REMARK 3 R VALUE (WORKING SET) : 0.275
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.820
REMARK 3 FREE R VALUE TEST SET COUNT : 1137
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 81.1606 - 5.9994 1.00 1789 154 0.2642 0.2401
REMARK 3 2 5.9994 - 4.7620 1.00 1685 157 0.3008 0.3237
REMARK 3 3 4.7620 - 4.1601 1.00 1673 146 0.2540 0.2703
REMARK 3 4 4.1601 - 3.7798 1.00 1656 145 0.2696 0.3321
REMARK 3 5 3.7798 - 3.5088 1.00 1662 131 0.2904 0.3369
REMARK 3 6 3.5088 - 3.3020 1.00 1652 139 0.2792 0.3764
REMARK 3 7 3.3020 - 3.1366 1.00 1655 123 0.3034 0.3676
REMARK 3 8 3.1366 - 3.0000 0.99 1627 142 0.2923 0.3851
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.10
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.003 4423
REMARK 3 ANGLE : 0.769 6040
REMARK 3 CHIRALITY : 0.050 784
REMARK 3 PLANARITY : 0.004 755
REMARK 3 DIHEDRAL : 13.429 1519
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: all
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9167 0.4767 -22.9940
REMARK 3 T TENSOR
REMARK 3 T11: 0.5184 T22: 0.4045
REMARK 3 T33: 0.6971 T12: 0.0430
REMARK 3 T13: 0.0280 T23: 0.0873
REMARK 3 L TENSOR
REMARK 3 L11: 2.0700 L22: 2.0314
REMARK 3 L33: 4.7456 L12: 0.3355
REMARK 3 L13: 1.2671 L23: 1.8348
REMARK 3 S TENSOR
REMARK 3 S11: -0.2882 S12: 0.1770 S13: -0.1812
REMARK 3 S21: 0.0440 S22: 0.1075 S23: 0.5220
REMARK 3 S31: 0.2444 S32: 0.4247 S33: -0.0144
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 4KF8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB079263.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14539
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 81.131
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.02700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.56100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-23% W/V PEG3350, 150 MM TRI-
REMARK 280 AMMONIUM CITRATE, 1 MM DTT, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 -1.000000 0.000000 0.000000 32.14900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.13100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.32550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.13100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.14900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.32550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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. (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 ASN A 1495
REMARK 465 ASN A 1496
REMARK 465 ALA A 1497
REMARK 465 ALA A 1498
REMARK 465 PRO A 1499
REMARK 465 GLN A 1500
REMARK 465 LYS A 1501
REMARK 465 PRO A 1502
REMARK 465 THR A 1503
REMARK 465 ALA A 1504
REMARK 465 GLU A 1505
REMARK 465 SER A 1506
REMARK 465 PRO A 1507
REMARK 465 VAL A 1508
REMARK 465 ALA A 1509
REMARK 465 HIS A 1534
REMARK 465 GLU A 1535
REMARK 465 PRO A 1536
REMARK 465 ASP A 1537
REMARK 465 LEU A 1705
REMARK 465 SER A 1706
REMARK 465 ARG A 1707
REMARK 465 THR A 1708
REMARK 465 VAL A 1709
REMARK 465 PRO A 1710
REMARK 465 LEU A 1711
REMARK 465 SER A 1712
REMARK 465 SER A 1713
REMARK 465 ARG A 1714
REMARK 465 ASP A 1715
REMARK 465 ALA A 1716
REMARK 465 PRO A 1717
REMARK 465 GLY A 1718
REMARK 465 ALA A 1719
REMARK 465 GLY A 1720
REMARK 465 GLU A 1824
REMARK 465 GLU A 1825
REMARK 465 GLU A 1826
REMARK 465 GLU A 1827
REMARK 465 SER B 1445
REMARK 465 ASN B 1495
REMARK 465 ASN B 1496
REMARK 465 ALA B 1497
REMARK 465 ALA B 1498
REMARK 465 PRO B 1499
REMARK 465 GLN B 1500
REMARK 465 LYS B 1501
REMARK 465 PRO B 1502
REMARK 465 THR B 1503
REMARK 465 ALA B 1504
REMARK 465 GLU B 1505
REMARK 465 SER B 1506
REMARK 465 PRO B 1507
REMARK 465 VAL B 1508
REMARK 465 GLU B 1535
REMARK 465 PRO B 1536
REMARK 465 ASP B 1537
REMARK 465 ALA B 1538
REMARK 465 LEU B 1591
REMARK 465 ALA B 1592
REMARK 465 GLU B 1593
REMARK 465 LYS B 1594
REMARK 465 VAL B 1643
REMARK 465 SER B 1644
REMARK 465 PRO B 1645
REMARK 465 PHE B 1646
REMARK 465 THR B 1647
REMARK 465 ASP B 1648
REMARK 465 GLY B 1675
REMARK 465 ALA B 1676
REMARK 465 LEU B 1700
REMARK 465 GLU B 1701
REMARK 465 ALA B 1702
REMARK 465 PRO B 1703
REMARK 465 GLY B 1704
REMARK 465 LEU B 1705
REMARK 465 SER B 1706
REMARK 465 ARG B 1707
REMARK 465 THR B 1708
REMARK 465 VAL B 1709
REMARK 465 PRO B 1710
REMARK 465 LEU B 1711
REMARK 465 SER B 1712
REMARK 465 SER B 1713
REMARK 465 ARG B 1714
REMARK 465 ASP B 1715
REMARK 465 ALA B 1716
REMARK 465 PRO B 1717
REMARK 465 GLY B 1718
REMARK 465 ALA B 1719
REMARK 465 GLY B 1720
REMARK 465 PRO B 1721
REMARK 465 HIS B 1722
REMARK 465 TYR B 1723
REMARK 465 PHE B 1724
REMARK 465 VAL B 1725
REMARK 465 LEU B 1746
REMARK 465 ARG B 1747
REMARK 465 SER B 1748
REMARK 465 GLY B 1749
REMARK 465 ASN B 1750
REMARK 465 ALA B 1751
REMARK 465 ARG B 1752
REMARK 465 ASP B 1753
REMARK 465 ILE B 1754
REMARK 465 PRO B 1755
REMARK 465 GLU B 1756
REMARK 465 VAL B 1757
REMARK 465 VAL B 1758
REMARK 465 TRP B 1759
REMARK 465 ASP B 1760
REMARK 465 SER B 1761
REMARK 465 GLY B 1762
REMARK 465 ALA B 1763
REMARK 465 VAL B 1764
REMARK 465 LEU B 1765
REMARK 465 GLU B 1766
REMARK 465 ASN B 1767
REMARK 465 VAL B 1768
REMARK 465 GLU B 1769
REMARK 465 PHE B 1770
REMARK 465 TRP B 1771
REMARK 465 LEU B 1772
REMARK 465 ALA B 1773
REMARK 465 SER B 1774
REMARK 465 ARG B 1775
REMARK 465 LYS B 1776
REMARK 465 VAL B 1777
REMARK 465 LEU B 1778
REMARK 465 ARG B 1779
REMARK 465 GLU B 1780
REMARK 465 ARG B 1781
REMARK 465 LEU B 1782
REMARK 465 LEU B 1783
REMARK 465 PRO B 1784
REMARK 465 LEU B 1785
REMARK 465 ASN B 1786
REMARK 465 PRO B 1787
REMARK 465 ARG B 1788
REMARK 465 GLU B 1789
REMARK 465 ALA B 1790
REMARK 465 GLU B 1791
REMARK 465 TRP B 1792
REMARK 465 ARG B 1793
REMARK 465 GLY B 1794
REMARK 465 MSE B 1795
REMARK 465 LYS B 1796
REMARK 465 ALA B 1797
REMARK 465 SER B 1798
REMARK 465 GLU B 1799
REMARK 465 GLY B 1800
REMARK 465 SER B 1801
REMARK 465 GLY B 1802
REMARK 465 CYS B 1803
REMARK 465 GLU B 1804
REMARK 465 THR B 1805
REMARK 465 LYS B 1806
REMARK 465 LEU B 1807
REMARK 465 GLU B 1808
REMARK 465 GLU B 1809
REMARK 465 GLU B 1824
REMARK 465 GLU B 1825
REMARK 465 GLU B 1826
REMARK 465 GLU B 1827
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 LYS A1492 CG CD CE NZ
REMARK 470 HIS A1493 CG ND1 CD2 CE1 NE2
REMARK 470 SER A1494 OG
REMARK 470 ARG A1520 CG CD NE CZ NH1 NH2
REMARK 470 HIS A1722 CG ND1 CD2 CE1 NE2
REMARK 470 TYR A1723 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A1775 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1776 CG CD CE NZ
REMARK 470 ARG A1779 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1780 CG CD OE1 OE2
REMARK 470 ARG A1781 CG CD NE CZ NH1 NH2
REMARK 470 ASN A1786 CG OD1 ND2
REMARK 470 ARG A1788 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1789 CG CD OE1 OE2
REMARK 470 GLU A1791 CG CD OE1 OE2
REMARK 470 ARG A1793 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1796 CG CD CE NZ
REMARK 470 GLU A1799 CG CD OE1 OE2
REMARK 470 CYS A1803 SG
REMARK 470 GLU A1804 CG CD OE1 OE2
REMARK 470 LYS A1806 CG CD CE NZ
REMARK 470 LYS B1482 CG CD CE NZ
REMARK 470 GLN B1579 CG CD OE1 NE2
REMARK 470 TRP B1587 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B1587 CZ3 CH2
REMARK 470 ASP B1596 CG OD1 OD2
REMARK 470 ARG B1639 CG CD NE CZ NH1 NH2
REMARK 470 ASN B1642 CG OD1 ND2
REMARK 470 ASN B1649 CG OD1 ND2
REMARK 470 TYR B1656 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B1674 CG CD1 CD2
REMARK 470 THR B1677 OG1 CG2
REMARK 470 GLU B1681 CG CD OE1 OE2
REMARK 470 PHE B1689 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B1694 CG CD NE CZ NH1 NH2
REMARK 470 ARG B1699 CG CD NE CZ NH1 NH2
REMARK 470 ARG B1741 CG CD NE CZ NH1 NH2
REMARK 470 VAL B1742 CG1 CG2
REMARK 470 LEU B1743 CG CD1 CD2
REMARK 470 LYS B1810 CG CD CE NZ
REMARK 470 VAL B1812 CG1 CG2
REMARK 470 LEU B1815 CG CD1 CD2
REMARK 470 GLU B1816 CG CD OE1 OE2
REMARK 470 ILE B1818 CG1 CG2 CD1
REMARK 470 ARG B1819 CG CD NE CZ NH1 NH2
REMARK 470 ASP B1820 CG OD1 OD2
REMARK 470 VAL B1821 CG1 CG2
REMARK 470 LEU B1822 CG CD1 CD2
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 GLN B 1553 OG SER B 1557 2.18
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 GLN A1473 7.20 82.70
REMARK 500 VAL A1521 -62.50 -106.26
REMARK 500 ALA A1539 -1.53 62.36
REMARK 500 GLU A1562 -3.75 71.98
REMARK 500 CYS A1564 57.00 -106.37
REMARK 500 VAL A1577 -111.00 41.69
REMARK 500 SER A1588 -58.03 -16.68
REMARK 500 ALA A1592 31.52 -165.80
REMARK 500 PRO A1597 75.40 -64.94
REMARK 500 PHE A1646 68.15 -108.39
REMARK 500 LEU A1671 29.52 -77.08
REMARK 500 ALA A1673 32.88 -91.91
REMARK 500 ILE A1678 -20.82 52.97
REMARK 500 SER A1798 -77.05 -78.60
REMARK 500 GLU A1799 -122.97 53.30
REMARK 500 ASP B1466 -71.74 -66.40
REMARK 500 THR B1491 -156.72 -70.95
REMARK 500 LYS B1492 -9.67 70.04
REMARK 500 VAL B1521 -62.10 -99.95
REMARK 500 ALA B1530 49.80 -70.36
REMARK 500 ALA B1531 50.41 -141.45
REMARK 500 ALA B1650 63.97 -154.48
REMARK 500 ALA B1673 68.85 -117.60
REMARK 500 ILE B1678 27.93 46.43
REMARK 500 VAL B1728 -37.41 -130.58
REMARK 500 ALA B1729 -31.96 -38.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KF7 RELATED DB: PDB
DBREF 4KF8 A 1445 1827 UNP G2QD05 G2QD05_THIHA 1445 1827
DBREF 4KF8 B 1445 1827 UNP G2QD05 G2QD05_THIHA 1445 1827
SEQRES 1 A 383 SER LEU LEU PRO LYS ASP ILE SER GLN LEU LEU SER LEU
SEQRES 2 A 383 VAL SER ALA THR ILE ASN GLY VAL ASP ASN PRO TRP SER
SEQRES 3 A 383 LYS ASP GLN ILE SER TYR PHE ARG THR LEU LEU LYS VAL
SEQRES 4 A 383 LEU PHE VAL VAL LEU ARG GLY THR LYS HIS SER ASN ASN
SEQRES 5 A 383 ALA ALA PRO GLN LYS PRO THR ALA GLU SER PRO VAL ALA
SEQRES 6 A 383 VAL THR GLN LEU VAL LEU THR THR LEU ASP ARG VAL VAL
SEQRES 7 A 383 ALA ARG SER PHE ARG ASN LEU ALA ALA LEU VAL HIS GLU
SEQRES 8 A 383 PRO ASP ALA ALA THR THR PRO GLU ASP LEU ALA LEU ILE
SEQRES 9 A 383 THR ALA ILE LEU GLN ALA CYS LEU SER VAL PRO GLY ILE
SEQRES 10 A 383 GLU GLN CYS GLN LEU GLN VAL LEU ASN ILE MSE SER SER
SEQRES 11 A 383 HIS ASN VAL LEU GLN VAL ALA THR SER LEU PHE SER TRP
SEQRES 12 A 383 SER ASP ARG LEU ALA GLU LYS GLY ASP PRO ILE TYR GLY
SEQRES 13 A 383 GLU LEU ALA LEU LEU LEU LEU LEU GLU LEU SER ALA LEU
SEQRES 14 A 383 PRO ALA LEU ALA GLU GLN LEU ALA CYS ASP GLY LEU LEU
SEQRES 15 A 383 GLY HIS LEU THR SER ALA ASN LEU ALA GLY PHE MSE ARG
SEQRES 16 A 383 ARG ALA ASN VAL SER PRO PHE THR ASP ASN ALA GLY ALA
SEQRES 17 A 383 ALA ARG CYS TYR ALA ILE TRP ALA LYS GLY ILE LEU PRO
SEQRES 18 A 383 LEU LEU LEU ASN ILE LEU GLY ALA LEU GLY ALA THR ILE
SEQRES 19 A 383 ALA PRO GLU VAL ALA PHE VAL LEU ASN GLN PHE PRO ASN
SEQRES 20 A 383 LEU LEU ARG SER SER VAL ASP ARG LEU GLU ALA PRO GLY
SEQRES 21 A 383 LEU SER ARG THR VAL PRO LEU SER SER ARG ASP ALA PRO
SEQRES 22 A 383 GLY ALA GLY PRO HIS TYR PHE VAL ALA LEU VAL ALA LEU
SEQRES 23 A 383 SER GLU VAL HIS SER LEU ALA LEU LEU THR ARG VAL LEU
SEQRES 24 A 383 ALA ALA LEU ARG SER GLY ASN ALA ARG ASP ILE PRO GLU
SEQRES 25 A 383 VAL VAL TRP ASP SER GLY ALA VAL LEU GLU ASN VAL GLU
SEQRES 26 A 383 PHE TRP LEU ALA SER ARG LYS VAL LEU ARG GLU ARG LEU
SEQRES 27 A 383 LEU PRO LEU ASN PRO ARG GLU ALA GLU TRP ARG GLY MSE
SEQRES 28 A 383 LYS ALA SER GLU GLY SER GLY CYS GLU THR LYS LEU GLU
SEQRES 29 A 383 GLU LYS ALA VAL GLY LEU LEU GLU GLY ILE ARG ASP VAL
SEQRES 30 A 383 LEU ALA GLU GLU GLU GLU
SEQRES 1 B 383 SER LEU LEU PRO LYS ASP ILE SER GLN LEU LEU SER LEU
SEQRES 2 B 383 VAL SER ALA THR ILE ASN GLY VAL ASP ASN PRO TRP SER
SEQRES 3 B 383 LYS ASP GLN ILE SER TYR PHE ARG THR LEU LEU LYS VAL
SEQRES 4 B 383 LEU PHE VAL VAL LEU ARG GLY THR LYS HIS SER ASN ASN
SEQRES 5 B 383 ALA ALA PRO GLN LYS PRO THR ALA GLU SER PRO VAL ALA
SEQRES 6 B 383 VAL THR GLN LEU VAL LEU THR THR LEU ASP ARG VAL VAL
SEQRES 7 B 383 ALA ARG SER PHE ARG ASN LEU ALA ALA LEU VAL HIS GLU
SEQRES 8 B 383 PRO ASP ALA ALA THR THR PRO GLU ASP LEU ALA LEU ILE
SEQRES 9 B 383 THR ALA ILE LEU GLN ALA CYS LEU SER VAL PRO GLY ILE
SEQRES 10 B 383 GLU GLN CYS GLN LEU GLN VAL LEU ASN ILE MSE SER SER
SEQRES 11 B 383 HIS ASN VAL LEU GLN VAL ALA THR SER LEU PHE SER TRP
SEQRES 12 B 383 SER ASP ARG LEU ALA GLU LYS GLY ASP PRO ILE TYR GLY
SEQRES 13 B 383 GLU LEU ALA LEU LEU LEU LEU LEU GLU LEU SER ALA LEU
SEQRES 14 B 383 PRO ALA LEU ALA GLU GLN LEU ALA CYS ASP GLY LEU LEU
SEQRES 15 B 383 GLY HIS LEU THR SER ALA ASN LEU ALA GLY PHE MSE ARG
SEQRES 16 B 383 ARG ALA ASN VAL SER PRO PHE THR ASP ASN ALA GLY ALA
SEQRES 17 B 383 ALA ARG CYS TYR ALA ILE TRP ALA LYS GLY ILE LEU PRO
SEQRES 18 B 383 LEU LEU LEU ASN ILE LEU GLY ALA LEU GLY ALA THR ILE
SEQRES 19 B 383 ALA PRO GLU VAL ALA PHE VAL LEU ASN GLN PHE PRO ASN
SEQRES 20 B 383 LEU LEU ARG SER SER VAL ASP ARG LEU GLU ALA PRO GLY
SEQRES 21 B 383 LEU SER ARG THR VAL PRO LEU SER SER ARG ASP ALA PRO
SEQRES 22 B 383 GLY ALA GLY PRO HIS TYR PHE VAL ALA LEU VAL ALA LEU
SEQRES 23 B 383 SER GLU VAL HIS SER LEU ALA LEU LEU THR ARG VAL LEU
SEQRES 24 B 383 ALA ALA LEU ARG SER GLY ASN ALA ARG ASP ILE PRO GLU
SEQRES 25 B 383 VAL VAL TRP ASP SER GLY ALA VAL LEU GLU ASN VAL GLU
SEQRES 26 B 383 PHE TRP LEU ALA SER ARG LYS VAL LEU ARG GLU ARG LEU
SEQRES 27 B 383 LEU PRO LEU ASN PRO ARG GLU ALA GLU TRP ARG GLY MSE
SEQRES 28 B 383 LYS ALA SER GLU GLY SER GLY CYS GLU THR LYS LEU GLU
SEQRES 29 B 383 GLU LYS ALA VAL GLY LEU LEU GLU GLY ILE ARG ASP VAL
SEQRES 30 B 383 LEU ALA GLU GLU GLU GLU
MODRES 4KF8 MSE A 1572 MET SELENOMETHIONINE
MODRES 4KF8 MSE A 1638 MET SELENOMETHIONINE
MODRES 4KF8 MSE A 1795 MET SELENOMETHIONINE
MODRES 4KF8 MSE B 1572 MET SELENOMETHIONINE
MODRES 4KF8 MSE B 1638 MET SELENOMETHIONINE
HET MSE A1572 8
HET MSE A1638 8
HET MSE A1795 8
HET MSE B1572 8
HET MSE B1638 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 5(C5 H11 N O2 SE)
HELIX 1 1 ASP A 1450 VAL A 1465 1 16
HELIX 2 2 GLN A 1473 THR A 1491 1 19
HELIX 3 3 THR A 1511 VAL A 1521 1 11
HELIX 4 4 VAL A 1521 LEU A 1529 1 9
HELIX 5 5 THR A 1541 VAL A 1558 1 18
HELIX 6 6 CYS A 1564 HIS A 1575 1 12
HELIX 7 7 VAL A 1577 SER A 1588 1 12
HELIX 8 8 ASP A 1589 ALA A 1592 5 4
HELIX 9 9 PRO A 1597 ALA A 1612 1 16
HELIX 10 10 LEU A 1613 ASP A 1623 1 11
HELIX 11 11 GLY A 1624 ALA A 1632 1 9
HELIX 12 12 ASN A 1633 MSE A 1638 1 6
HELIX 13 13 ASN A 1649 LYS A 1661 1 13
HELIX 14 14 GLY A 1662 LEU A 1671 1 10
HELIX 15 15 GLY A 1672 LEU A 1674 5 3
HELIX 16 16 ILE A 1678 ASN A 1687 1 10
HELIX 17 17 PHE A 1689 ARG A 1699 1 11
HELIX 18 18 LEU A 1727 SER A 1748 1 22
HELIX 19 19 ASP A 1760 ALA A 1773 1 14
HELIX 20 20 SER A 1774 LEU A 1782 1 9
HELIX 21 21 ASN A 1786 MSE A 1795 1 10
HELIX 22 22 THR A 1805 ALA A 1823 1 19
HELIX 23 23 ASP B 1450 ASN B 1463 1 14
HELIX 24 24 GLN B 1473 GLY B 1490 1 18
HELIX 25 25 VAL B 1510 VAL B 1521 1 12
HELIX 26 26 VAL B 1521 ALA B 1530 1 10
HELIX 27 27 THR B 1541 LEU B 1556 1 16
HELIX 28 28 SER B 1557 GLN B 1563 5 7
HELIX 29 29 CYS B 1564 HIS B 1575 1 12
HELIX 30 30 ASN B 1576 SER B 1588 1 13
HELIX 31 31 PRO B 1597 SER B 1611 1 15
HELIX 32 32 LEU B 1613 GLY B 1624 1 12
HELIX 33 33 GLY B 1624 SER B 1631 1 8
HELIX 34 34 ALA B 1632 ARG B 1639 1 8
HELIX 35 35 ALA B 1652 GLY B 1662 1 11
HELIX 36 36 GLY B 1662 GLY B 1672 1 11
HELIX 37 37 ILE B 1678 GLN B 1688 1 11
HELIX 38 38 PHE B 1689 SER B 1695 1 7
HELIX 39 39 VAL B 1728 ALA B 1745 1 18
HELIX 40 40 ALA B 1811 ALA B 1823 1 13
LINK C ILE A1571 N MSE A1572 1555 1555 1.33
LINK C MSE A1572 N SER A1573 1555 1555 1.33
LINK C PHE A1637 N MSE A1638 1555 1555 1.33
LINK C MSE A1638 N ARG A1639 1555 1555 1.33
LINK C GLY A1794 N MSE A1795 1555 1555 1.33
LINK C MSE A1795 N LYS A1796 1555 1555 1.33
LINK C ILE B1571 N MSE B1572 1555 1555 1.33
LINK C MSE B1572 N SER B1573 1555 1555 1.33
LINK C PHE B1637 N MSE B1638 1555 1555 1.33
LINK C MSE B1638 N ARG B1639 1555 1555 1.33
CRYST1 64.298 66.651 162.262 90.00 90.00 90.00 P 21 21 21 8
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 0.015553 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015004 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006163 0.00000
ATOM 1 N SER A1445 37.778 26.425 -19.846 1.00114.16 N
ANISOU 1 N SER A1445 14731 18412 10234 -8071 -1003 724 N
ATOM 2 CA SER A1445 36.357 26.207 -20.097 1.00116.75 C
ANISOU 2 CA SER A1445 15358 18142 10858 -7797 -1168 925 C
ATOM 3 C SER A1445 35.578 26.052 -18.794 1.00115.92 C
ANISOU 3 C SER A1445 15249 17672 11125 -7407 -1310 882 C
ATOM 4 O SER A1445 36.109 25.563 -17.794 1.00116.84 O
ANISOU 4 O SER A1445 14964 18151 11280 -7218 -1235 659 O
ATOM 5 CB SER A1445 36.150 24.976 -20.983 1.00112.37 C
ANISOU 5 CB SER A1445 14521 17876 10299 -7599 -1023 909 C
ATOM 6 OG SER A1445 36.636 23.804 -20.351 1.00108.85 O
ANISOU 6 OG SER A1445 13485 17960 9914 -7270 -856 657 O
ATOM 7 N LEU A1446 34.317 26.475 -18.810 1.00109.71 N
ANISOU 7 N LEU A1446 14913 16182 10591 -7267 -1533 1078 N
ATOM 8 CA LEU A1446 33.460 26.379 -17.634 1.00105.66 C
ANISOU 8 CA LEU A1446 14458 15267 10421 -6814 -1665 1038 C
ATOM 9 C LEU A1446 32.588 25.132 -17.691 1.00101.84 C
ANISOU 9 C LEU A1446 13785 14722 10186 -6145 -1554 1046 C
ATOM 10 O LEU A1446 32.809 24.245 -18.516 1.00100.81 O
ANISOU 10 O LEU A1446 13398 14948 9959 -6121 -1391 1037 O
ATOM 11 CB LEU A1446 32.574 27.621 -17.505 1.00105.36 C
ANISOU 11 CB LEU A1446 15033 14471 10527 -6931 -1970 1208 C
ATOM 12 CG LEU A1446 33.259 28.962 -17.236 1.00105.84 C
ANISOU 12 CG LEU A1446 15375 14442 10399 -7288 -2062 1209 C
ATOM 13 CD1 LEU A1446 32.229 30.082 -17.196 1.00100.18 C
ANISOU 13 CD1 LEU A1446 15271 12943 9848 -7215 -2368 1371 C
ATOM 14 CD2 LEU A1446 34.053 28.911 -15.938 1.00108.75 C
ANISOU 14 CD2 LEU A1446 15412 15152 10756 -7265 -1997 964 C
ATOM 15 N LEU A1447 31.595 25.074 -16.811 1.00 97.45 N
ANISOU 15 N LEU A1447 13361 13722 9945 -5617 -1640 1050 N
ATOM 16 CA LEU A1447 30.666 23.951 -16.779 1.00 89.80 C
ANISOU 16 CA LEU A1447 12253 12641 9227 -5007 -1543 1062 C
ATOM 17 C LEU A1447 29.622 24.070 -17.884 1.00 87.05 C
ANISOU 17 C LEU A1447 12228 11863 8985 -5035 -1665 1266 C
ATOM 18 O LEU A1447 29.151 25.167 -18.181 1.00 92.32 O
ANISOU 18 O LEU A1447 13340 12068 9669 -5298 -1902 1401 O
ATOM 19 CB LEU A1447 29.989 23.851 -15.412 1.00 84.54 C
ANISOU 19 CB LEU A1447 11594 11698 8830 -4471 -1572 980 C
ATOM 20 CG LEU A1447 30.875 23.326 -14.281 1.00 81.48 C
ANISOU 20 CG LEU A1447 10825 11767 8368 -4262 -1421 770 C
ATOM 21 CD1 LEU A1447 30.082 23.219 -12.989 1.00 76.51 C
ANISOU 21 CD1 LEU A1447 10248 10834 7989 -3740 -1447 713 C
ATOM 22 CD2 LEU A1447 31.480 21.981 -14.662 1.00 67.27 C
ANISOU 22 CD2 LEU A1447 8589 10508 6461 -4082 -1192 682 C
ATOM 23 N PRO A1448 29.260 22.934 -18.499 1.00 80.79 N
ANISOU 23 N PRO A1448 11225 11213 8257 -4753 -1521 1281 N
ATOM 24 CA PRO A1448 28.287 22.917 -19.597 1.00 79.20 C
ANISOU 24 CA PRO A1448 11283 10661 8146 -4755 -1627 1454 C
ATOM 25 C PRO A1448 26.910 23.412 -19.163 1.00 76.37 C
ANISOU 25 C PRO A1448 11259 9652 8104 -4424 -1835 1527 C
ATOM 26 O PRO A1448 26.346 22.919 -18.187 1.00 74.65 O
ANISOU 26 O PRO A1448 10904 9336 8124 -3932 -1771 1431 O
ATOM 27 CB PRO A1448 28.225 21.436 -19.990 1.00 65.23 C
ANISOU 27 CB PRO A1448 9145 9219 6421 -4411 -1402 1390 C
ATOM 28 CG PRO A1448 28.718 20.698 -18.792 1.00 63.73 C
ANISOU 28 CG PRO A1448 8594 9336 6284 -4043 -1230 1203 C
ATOM 29 CD PRO A1448 29.753 21.584 -18.180 1.00 66.25 C
ANISOU 29 CD PRO A1448 8905 9862 6406 -4400 -1270 1122 C
ATOM 30 N LYS A1449 26.381 24.389 -19.892 1.00 77.64 N
ANISOU 30 N LYS A1449 11864 9385 8251 -4698 -2088 1687 N
ATOM 31 CA LYS A1449 25.071 24.948 -19.593 1.00 75.55 C
ANISOU 31 CA LYS A1449 11927 8506 8271 -4390 -2327 1732 C
ATOM 32 C LYS A1449 24.099 24.619 -20.722 1.00 67.15 C
ANISOU 32 C LYS A1449 11004 7207 7304 -4280 -2417 1857 C
ATOM 33 O LYS A1449 22.891 24.533 -20.511 1.00 87.53 O
ANISOU 33 O LYS A1449 13669 9419 10170 -3863 -2525 1841 O
ATOM 34 CB LYS A1449 25.175 26.461 -19.402 1.00 71.07 C
ANISOU 34 CB LYS A1449 11820 7554 7631 -4737 -2617 1792 C
ATOM 35 CG LYS A1449 26.530 26.918 -18.889 1.00 73.14 C
ANISOU 35 CG LYS A1449 11989 8164 7638 -5155 -2537 1720 C
ATOM 36 CD LYS A1449 26.520 28.387 -18.505 1.00 94.02 C
ANISOU 36 CD LYS A1449 15105 10363 10257 -5433 -2835 1755 C
ATOM 37 CE LYS A1449 25.627 28.629 -17.298 1.00 87.96 C
ANISOU 37 CE LYS A1449 14398 9221 9803 -4904 -2947 1627 C
ATOM 38 NZ LYS A1449 25.717 30.034 -16.814 1.00 87.35 N
ANISOU 38 NZ LYS A1449 14757 8736 9695 -5149 -3235 1619 N
ATOM 39 N ASP A1450 24.643 24.439 -21.921 1.00 83.48 N
ANISOU 39 N ASP A1450 13079 9518 9119 -4666 -2371 1964 N
ATOM 40 CA ASP A1450 23.853 24.052 -23.083 1.00 81.11 C
ANISOU 40 CA ASP A1450 12888 9067 8864 -4598 -2442 2078 C
ATOM 41 C ASP A1450 23.869 22.540 -23.256 1.00 78.78 C
ANISOU 41 C ASP A1450 12131 9172 8629 -4288 -2151 1983 C
ATOM 42 O ASP A1450 24.709 21.849 -22.682 1.00 77.76 O
ANISOU 42 O ASP A1450 11628 9489 8429 -4227 -1902 1852 O
ATOM 43 CB ASP A1450 24.402 24.709 -24.352 1.00 88.70 C
ANISOU 43 CB ASP A1450 14154 10061 9486 -5210 -2564 2254 C
ATOM 44 CG ASP A1450 24.133 26.201 -24.405 1.00 97.64 C
ANISOU 44 CG ASP A1450 15778 10765 10556 -5319 -2881 2315 C
ATOM 45 OD1 ASP A1450 24.934 26.973 -23.837 1.00 76.69 O
ANISOU 45 OD1 ASP A1450 13201 8188 7750 -5576 -2893 2278 O
ATOM 46 OD2 ASP A1450 23.123 26.601 -25.022 1.00 75.39 O
ANISOU 46 OD2 ASP A1450 13250 7564 7832 -5120 -3122 2377 O
ATOM 47 N ILE A1451 22.938 22.032 -24.055 1.00 78.72 N
ANISOU 47 N ILE A1451 12166 8995 8749 -4085 -2202 2040 N
ATOM 48 CA ILE A1451 22.885 20.609 -24.355 1.00 72.42 C
ANISOU 48 CA ILE A1451 10986 8523 8006 -3816 -1955 1958 C
ATOM 49 C ILE A1451 23.999 20.258 -25.340 1.00 75.91 C
ANISOU 49 C ILE A1451 11286 9459 8096 -4225 -1810 1978 C
ATOM 50 O ILE A1451 24.449 19.114 -25.410 1.00 78.47 O
ANISOU 50 O ILE A1451 11236 10196 8383 -4069 -1567 1862 O
ATOM 51 CB ILE A1451 21.504 20.211 -24.917 1.00 60.34 C
ANISOU 51 CB ILE A1451 9548 6654 6724 -3492 -2069 1996 C
ATOM 52 CG1 ILE A1451 21.427 18.705 -25.180 1.00 69.36 C
ANISOU 52 CG1 ILE A1451 10315 8104 7936 -3214 -1818 1902 C
ATOM 53 CG2 ILE A1451 21.198 21.003 -26.178 1.00 62.89 C
ANISOU 53 CG2 ILE A1451 10268 6728 6898 -3825 -2334 2171 C
ATOM 54 CD1 ILE A1451 21.643 17.855 -23.955 1.00 55.70 C
ANISOU 54 CD1 ILE A1451 8245 6569 6348 -2857 -1580 1748 C
ATOM 55 N SER A1452 24.457 21.262 -26.081 1.00 77.41 N
ANISOU 55 N SER A1452 11788 9609 8015 -4756 -1963 2115 N
ATOM 56 CA SER A1452 25.537 21.081 -27.043 1.00 84.33 C
ANISOU 56 CA SER A1452 12549 10980 8513 -5222 -1827 2131 C
ATOM 57 C SER A1452 26.892 21.047 -26.343 1.00 85.60 C
ANISOU 57 C SER A1452 12400 11645 8479 -5425 -1624 1986 C
ATOM 58 O SER A1452 27.777 20.277 -26.720 1.00 86.90 O
ANISOU 58 O SER A1452 12205 12374 8438 -5523 -1396 1867 O
ATOM 59 CB SER A1452 25.517 22.200 -28.084 1.00 95.79 C
ANISOU 59 CB SER A1452 14486 12196 9715 -5763 -2067 2345 C
ATOM 60 OG SER A1452 25.674 23.468 -27.469 1.00103.17 O
ANISOU 60 OG SER A1452 15720 12860 10620 -5891 -2250 2363 O
ATOM 61 N GLN A1453 27.050 21.891 -25.328 1.00 81.91 N
ANISOU 61 N GLN A1453 12066 10984 8074 -5474 -1720 1975 N
ATOM 62 CA GLN A1453 28.272 21.911 -24.534 1.00 81.58 C
ANISOU 62 CA GLN A1453 11729 11394 7873 -5630 -1554 1820 C
ATOM 63 C GLN A1453 28.377 20.638 -23.701 1.00 72.61 C
ANISOU 63 C GLN A1453 10121 10553 6914 -5076 -1327 1618 C
ATOM 64 O GLN A1453 29.472 20.187 -23.363 1.00 71.30 O
ANISOU 64 O GLN A1453 9587 10924 6579 -5130 -1140 1450 O
ATOM 65 CB GLN A1453 28.299 23.138 -23.621 1.00 86.52 C
ANISOU 65 CB GLN A1453 12646 11682 8546 -5785 -1739 1853 C
ATOM 66 CG GLN A1453 28.508 24.457 -24.344 1.00 88.09 C
ANISOU 66 CG GLN A1453 13315 11659 8497 -6362 -1952 2021 C
ATOM 67 CD GLN A1453 28.356 25.650 -23.422 1.00 86.98 C
ANISOU 67 CD GLN A1453 13501 11102 8446 -6371 -2163 2031 C
ATOM 68 OE1 GLN A1453 27.646 25.586 -22.419 1.00 75.10 O
ANISOU 68 OE1 GLN A1453 12006 9266 7262 -6007 -2240 1988 O
ATOM 69 NE2 GLN A1453 29.025 26.747 -23.757 1.00 81.41 N
ANISOU 69 NE2 GLN A1453 13062 10426 7445 -6751 -2252 2071 N
ATOM 70 N LEU A1454 27.227 20.066 -23.366 1.00 69.18 N
ANISOU 70 N LEU A1454 9710 9764 6812 -4548 -1356 1628 N
ATOM 71 CA LEU A1454 27.192 18.806 -22.644 1.00 71.85 C
ANISOU 71 CA LEU A1454 9673 10309 7317 -4025 -1157 1469 C
ATOM 72 C LEU A1454 27.623 17.691 -23.581 1.00 74.70 C
ANISOU 72 C LEU A1454 9748 11100 7536 -4006 -981 1398 C
ATOM 73 O LEU A1454 28.320 16.760 -23.184 1.00 61.10 O
ANISOU 73 O LEU A1454 7660 9793 5762 -3787 -795 1226 O
ATOM 74 CB LEU A1454 25.786 18.539 -22.107 1.00 69.08 C
ANISOU 74 CB LEU A1454 9448 9458 7340 -3534 -1231 1506 C
ATOM 75 CG LEU A1454 25.570 17.242 -21.327 1.00 56.51 C
ANISOU 75 CG LEU A1454 7547 7987 5935 -3002 -1039 1375 C
ATOM 76 CD1 LEU A1454 26.509 17.157 -20.129 1.00 56.65 C
ANISOU 76 CD1 LEU A1454 7344 8305 5874 -2912 -928 1234 C
ATOM 77 CD2 LEU A1454 24.122 17.147 -20.886 1.00 54.50 C
ANISOU 77 CD2 LEU A1454 7446 7237 6023 -2619 -1117 1420 C
ATOM 78 N LEU A1455 27.207 17.805 -24.837 1.00 78.93 N
ANISOU 78 N LEU A1455 10468 11526 7995 -4226 -1061 1522 N
ATOM 79 CA LEU A1455 27.546 16.825 -25.860 1.00 80.46 C
ANISOU 79 CA LEU A1455 10428 12105 8037 -4237 -915 1454 C
ATOM 80 C LEU A1455 29.037 16.867 -26.177 1.00 77.85 C
ANISOU 80 C LEU A1455 9835 12416 7328 -4635 -772 1329 C
ATOM 81 O LEU A1455 29.665 15.828 -26.369 1.00 76.86 O
ANISOU 81 O LEU A1455 9339 12760 7105 -4471 -588 1149 O
ATOM 82 CB LEU A1455 26.725 17.082 -27.125 1.00 85.23 C
ANISOU 82 CB LEU A1455 11333 12423 8626 -4413 -1062 1626 C
ATOM 83 CG LEU A1455 26.836 16.082 -28.276 1.00 63.44 C
ANISOU 83 CG LEU A1455 8386 9979 5739 -4395 -941 1567 C
ATOM 84 CD1 LEU A1455 26.468 14.679 -27.821 1.00 60.54 C
ANISOU 84 CD1 LEU A1455 7725 9659 5619 -3814 -795 1415 C
ATOM 85 CD2 LEU A1455 25.945 16.523 -29.416 1.00 64.24 C
ANISOU 85 CD2 LEU A1455 8846 9733 5829 -4577 -1132 1755 C
ATOM 86 N SER A1456 29.593 18.074 -26.228 1.00 76.72 N
ANISOU 86 N SER A1456 9886 12294 6968 -5161 -863 1410 N
ATOM 87 CA SER A1456 31.023 18.256 -26.463 1.00 80.47 C
ANISOU 87 CA SER A1456 10105 13400 7069 -5610 -726 1280 C
ATOM 88 C SER A1456 31.841 17.614 -25.355 1.00 81.67 C
ANISOU 88 C SER A1456 9823 13959 7250 -5296 -569 1030 C
ATOM 89 O SER A1456 32.815 16.910 -25.617 1.00 87.41 O
ANISOU 89 O SER A1456 10145 15302 7766 -5313 -393 820 O
ATOM 90 CB SER A1456 31.376 19.743 -26.539 1.00 86.16 C
ANISOU 90 CB SER A1456 11167 13985 7585 -6239 -872 1425 C
ATOM 91 OG SER A1456 30.728 20.374 -27.626 1.00 98.90 O
ANISOU 91 OG SER A1456 13216 15244 9118 -6567 -1039 1661 O
ATOM 92 N LEU A1457 31.436 17.866 -24.115 1.00 79.36 N
ANISOU 92 N LEU A1457 9621 13326 7208 -4994 -647 1040 N
ATOM 93 CA LEU A1457 32.173 17.398 -22.949 1.00 75.61 C
ANISOU 93 CA LEU A1457 8798 13177 6753 -4702 -538 825 C
ATOM 94 C LEU A1457 32.124 15.880 -22.820 1.00 73.34 C
ANISOU 94 C LEU A1457 8184 13101 6583 -4128 -393 667 C
ATOM 95 O LEU A1457 33.120 15.248 -22.466 1.00 72.66 O
ANISOU 95 O LEU A1457 7712 13539 6358 -3991 -268 437 O
ATOM 96 CB LEU A1457 31.626 18.057 -21.683 1.00 75.04 C
ANISOU 96 CB LEU A1457 8949 12644 6917 -4515 -666 890 C
ATOM 97 CG LEU A1457 32.297 17.710 -20.355 1.00 66.54 C
ANISOU 97 CG LEU A1457 7582 11834 5864 -4212 -589 692 C
ATOM 98 CD1 LEU A1457 33.732 18.200 -20.327 1.00 69.96 C
ANISOU 98 CD1 LEU A1457 7769 12846 5966 -4659 -533 532 C
ATOM 99 CD2 LEU A1457 31.504 18.305 -19.210 1.00 64.96 C
ANISOU 99 CD2 LEU A1457 7650 11109 5922 -3989 -718 776 C
ATOM 100 N VAL A1458 30.963 15.301 -23.108 1.00 75.74 N
ANISOU 100 N VAL A1458 8651 12988 7137 -3792 -425 780 N
ATOM 101 CA VAL A1458 30.791 13.854 -23.042 1.00 61.70 C
ANISOU 101 CA VAL A1458 6636 11323 5485 -3266 -306 654 C
ATOM 102 C VAL A1458 31.578 13.172 -24.154 1.00 76.07 C
ANISOU 102 C VAL A1458 8176 13683 7045 -3399 -187 506 C
ATOM 103 O VAL A1458 32.215 12.141 -23.935 1.00 75.12 O
ANISOU 103 O VAL A1458 7722 13946 6872 -3075 -75 289 O
ATOM 104 CB VAL A1458 29.304 13.453 -23.119 1.00 58.85 C
ANISOU 104 CB VAL A1458 6528 10380 5454 -2933 -370 808 C
ATOM 105 CG1 VAL A1458 29.157 11.963 -23.383 1.00 71.77 C
ANISOU 105 CG1 VAL A1458 7958 12140 7170 -2505 -253 691 C
ATOM 106 CG2 VAL A1458 28.589 13.843 -21.837 1.00 57.07 C
ANISOU 106 CG2 VAL A1458 6480 9716 5489 -2681 -444 880 C
ATOM 107 N SER A1459 31.543 13.767 -25.343 1.00 80.21 N
ANISOU 107 N SER A1459 8849 14238 7390 -3872 -224 616 N
ATOM 108 CA SER A1459 32.284 13.243 -26.485 1.00 85.57 C
ANISOU 108 CA SER A1459 9274 15456 7781 -4068 -106 475 C
ATOM 109 C SER A1459 33.789 13.417 -26.305 1.00 78.84 C
ANISOU 109 C SER A1459 8052 15300 6605 -4335 6 243 C
ATOM 110 O SER A1459 34.563 12.526 -26.631 1.00 80.14 O
ANISOU 110 O SER A1459 7834 16007 6610 -4184 136 -9 O
ATOM 111 CB SER A1459 31.819 13.905 -27.783 1.00 99.82 C
ANISOU 111 CB SER A1459 11378 17097 9452 -4537 -184 674 C
ATOM 112 OG SER A1459 31.916 15.315 -27.697 1.00111.09 O
ANISOU 112 OG SER A1459 13095 18348 10765 -5051 -302 845 O
ATOM 113 N ALA A1460 34.205 14.564 -25.781 1.00 73.64 N
ANISOU 113 N ALA A1460 7499 14635 5848 -4725 -53 304 N
ATOM 114 CA ALA A1460 35.616 14.783 -25.486 1.00 75.16 C
ANISOU 114 CA ALA A1460 7321 15489 5746 -4989 46 67 C
ATOM 115 C ALA A1460 36.104 13.773 -24.451 1.00 92.48 C
ANISOU 115 C ALA A1460 9143 17949 8047 -4390 111 -193 C
ATOM 116 O ALA A1460 37.271 13.385 -24.445 1.00 94.04 O
ANISOU 116 O ALA A1460 8904 18819 8009 -4405 218 -482 O
ATOM 117 CB ALA A1460 35.845 16.201 -24.995 1.00112.72 C
ANISOU 117 CB ALA A1460 12310 20095 10422 -5490 -53 194 C
ATOM 118 N THR A1461 35.194 13.345 -23.583 1.00 88.82 N
ANISOU 118 N THR A1461 8858 16962 7928 -3861 38 -96 N
ATOM 119 CA THR A1461 35.516 12.406 -22.516 1.00 82.73 C
ANISOU 119 CA THR A1461 7832 16331 7269 -3273 70 -293 C
ATOM 120 C THR A1461 35.619 10.969 -23.027 1.00 83.14 C
ANISOU 120 C THR A1461 7641 16626 7325 -2830 155 -473 C
ATOM 121 O THR A1461 36.424 10.182 -22.528 1.00 86.32 O
ANISOU 121 O THR A1461 7707 17438 7653 -2474 196 -737 O
ATOM 122 CB THR A1461 34.470 12.483 -21.393 1.00 75.95 C
ANISOU 122 CB THR A1461 7283 14820 6753 -2906 -26 -113 C
ATOM 123 OG1 THR A1461 34.296 13.851 -21.001 1.00 78.47 O
ANISOU 123 OG1 THR A1461 7864 14872 7080 -3308 -126 48 O
ATOM 124 CG2 THR A1461 34.901 11.663 -20.184 1.00 74.57 C
ANISOU 124 CG2 THR A1461 6889 14800 6645 -2364 -7 -298 C
ATOM 125 N ILE A1462 34.809 10.628 -24.026 1.00 77.50 N
ANISOU 125 N ILE A1462 7104 15652 6690 -2840 160 -344 N
ATOM 126 CA ILE A1462 34.832 9.277 -24.586 1.00 77.35 C
ANISOU 126 CA ILE A1462 6894 15814 6681 -2437 227 -512 C
ATOM 127 C ILE A1462 36.147 8.987 -25.319 1.00 80.42 C
ANISOU 127 C ILE A1462 6843 17003 6711 -2612 333 -823 C
ATOM 128 O ILE A1462 36.668 7.872 -25.261 1.00 77.67 O
ANISOU 128 O ILE A1462 6201 16982 6326 -2172 372 -1090 O
ATOM 129 CB ILE A1462 33.606 8.996 -25.508 1.00 81.78 C
ANISOU 129 CB ILE A1462 7753 15903 7416 -2420 200 -308 C
ATOM 130 CG1 ILE A1462 33.362 7.492 -25.647 1.00 79.47 C
ANISOU 130 CG1 ILE A1462 7353 15591 7251 -1857 235 -453 C
ATOM 131 CG2 ILE A1462 33.760 9.642 -26.876 1.00 86.20 C
ANISOU 131 CG2 ILE A1462 8350 16677 7724 -2995 224 -249 C
ATOM 132 CD1 ILE A1462 32.601 6.896 -24.490 1.00 86.67 C
ANISOU 132 CD1 ILE A1462 8439 16007 8486 -1340 187 -371 C
ATOM 133 N ASN A1463 36.690 9.999 -25.989 1.00 82.05 N
ANISOU 133 N ASN A1463 7008 17528 6641 -3258 372 -801 N
ATOM 134 CA ASN A1463 37.934 9.836 -26.727 1.00 99.75 C
ANISOU 134 CA ASN A1463 8812 20581 8508 -3510 494 -1105 C
ATOM 135 C ASN A1463 39.125 9.726 -25.789 1.00106.94 C
ANISOU 135 C ASN A1463 9310 22031 9290 -3352 519 -1409 C
ATOM 136 O ASN A1463 40.160 9.166 -26.149 1.00120.10 O
ANISOU 136 O ASN A1463 10602 24316 10715 -3252 581 -1752 O
ATOM 137 CB ASN A1463 38.139 10.990 -27.710 1.00106.07 C
ANISOU 137 CB ASN A1463 9726 21552 9024 -4311 537 -969 C
ATOM 138 CG ASN A1463 37.768 10.617 -29.131 1.00107.00 C
ANISOU 138 CG ASN A1463 9909 21720 9026 -4459 592 -932 C
ATOM 139 OD1 ASN A1463 38.598 10.112 -29.887 1.00106.54 O
ANISOU 139 OD1 ASN A1463 9592 22175 8714 -4451 650 -1214 O
ATOM 140 ND2 ASN A1463 36.513 10.861 -29.503 1.00103.16 N
ANISOU 140 ND2 ASN A1463 9887 20559 8751 -4487 490 -607 N
ATOM 141 N GLY A1464 38.968 10.262 -24.584 1.00 95.92 N
ANISOU 141 N GLY A1464 8068 20321 8057 -3273 430 -1295 N
ATOM 142 CA GLY A1464 40.031 10.245 -23.599 1.00101.17 C
ANISOU 142 CA GLY A1464 8379 21449 8613 -3123 425 -1563 C
ATOM 143 C GLY A1464 40.311 8.862 -23.045 1.00104.23 C
ANISOU 143 C GLY A1464 8515 21994 9093 -2357 399 -1825 C
ATOM 144 O GLY A1464 41.411 8.596 -22.565 1.00111.54 O
ANISOU 144 O GLY A1464 9071 23462 9848 -2177 397 -2146 O
ATOM 145 N VAL A1465 39.314 7.983 -23.107 1.00 98.47 N
ANISOU 145 N VAL A1465 8045 20741 8628 -1892 360 -1688 N
ATOM 146 CA VAL A1465 39.463 6.623 -22.597 1.00 90.24 C
ANISOU 146 CA VAL A1465 6861 19739 7687 -1156 313 -1898 C
ATOM 147 C VAL A1465 40.502 5.854 -23.404 1.00 89.84 C
ANISOU 147 C VAL A1465 6340 20425 7370 -1036 376 -2299 C
ATOM 148 O VAL A1465 40.311 5.588 -24.588 1.00 89.17 O
ANISOU 148 O VAL A1465 6237 20435 7207 -1193 450 -2316 O
ATOM 149 CB VAL A1465 38.120 5.863 -22.572 1.00 83.28 C
ANISOU 149 CB VAL A1465 6388 18119 7136 -759 267 -1654 C
ATOM 150 CG1 VAL A1465 38.348 4.380 -22.322 1.00 76.68 C
ANISOU 150 CG1 VAL A1465 5422 17361 6353 -58 219 -1890 C
ATOM 151 CG2 VAL A1465 37.206 6.450 -21.509 1.00 70.25 C
ANISOU 151 CG2 VAL A1465 5128 15819 5747 -738 199 -1341 C
ATOM 152 N ASP A1466 41.603 5.514 -22.742 1.00105.06 N
ANISOU 152 N ASP A1466 7982 22785 9152 -739 312 -2619 N
ATOM 153 CA ASP A1466 42.756 4.887 -23.380 1.00123.42 C
ANISOU 153 CA ASP A1466 10061 25631 11202 -612 281 -3010 C
ATOM 154 C ASP A1466 42.408 3.599 -24.119 1.00126.70 C
ANISOU 154 C ASP A1466 10491 25947 11703 -168 249 -3115 C
ATOM 155 O ASP A1466 42.542 3.518 -25.341 1.00133.56 O
ANISOU 155 O ASP A1466 11293 27031 12424 -425 304 -3197 O
ATOM 156 CB ASP A1466 43.844 4.616 -22.336 1.00136.84 C
ANISOU 156 CB ASP A1466 11572 27638 12782 -245 168 -3306 C
ATOM 157 CG ASP A1466 43.288 4.007 -21.059 1.00141.96 C
ANISOU 157 CG ASP A1466 12370 27864 13705 365 56 -3202 C
ATOM 158 OD1 ASP A1466 42.882 4.772 -20.157 1.00136.37 O
ANISOU 158 OD1 ASP A1466 11763 26929 13122 226 60 -2982 O
ATOM 159 OD2 ASP A1466 43.252 2.762 -20.960 1.00148.80 O
ANISOU 159 OD2 ASP A1466 13279 28605 14654 976 -52 -3335 O
ATOM 160 N ASN A1467 41.958 2.597 -23.375 1.00122.37 N
ANISOU 160 N ASN A1467 10059 25052 11384 493 152 -3109 N
ATOM 161 CA ASN A1467 41.656 1.299 -23.957 1.00125.66 C
ANISOU 161 CA ASN A1467 10538 25318 11889 965 98 -3222 C
ATOM 162 C ASN A1467 40.239 0.839 -23.641 1.00122.18 C
ANISOU 162 C ASN A1467 10415 24222 11787 1267 127 -2921 C
ATOM 163 O ASN A1467 39.996 0.225 -22.601 1.00127.67 O
ANISOU 163 O ASN A1467 11270 24589 12651 1785 21 -2885 O
ATOM 164 CB ASN A1467 42.674 0.262 -23.486 1.00130.82 C
ANISOU 164 CB ASN A1467 11067 26203 12436 1542 -89 -3587 C
ATOM 165 CG ASN A1467 44.053 0.499 -24.062 1.00138.76 C
ANISOU 165 CG ASN A1467 11730 27907 13088 1288 -113 -3949 C
ATOM 166 OD1 ASN A1467 44.199 0.826 -25.240 1.00148.76 O
ANISOU 166 OD1 ASN A1467 12868 29455 14197 855 -19 -4000 O
ATOM 167 ND2 ASN A1467 45.076 0.338 -23.232 1.00136.35 N
ANISOU 167 ND2 ASN A1467 11278 27891 12636 1551 -239 -4209 N
ATOM 168 N PRO A1468 39.293 1.152 -24.538 1.00107.82 N
ANISOU 168 N PRO A1468 8802 22104 10061 907 230 -2672 N
ATOM 169 CA PRO A1468 37.902 0.714 -24.396 1.00101.07 C
ANISOU 169 CA PRO A1468 8441 20425 9537 1097 190 -2344 C
ATOM 170 C PRO A1468 37.789 -0.793 -24.601 1.00107.18 C
ANISOU 170 C PRO A1468 9257 21072 10395 1712 113 -2532 C
ATOM 171 O PRO A1468 38.664 -1.384 -25.239 1.00115.17 O
ANISOU 171 O PRO A1468 9922 22641 11199 1892 111 -2901 O
ATOM 172 CB PRO A1468 37.186 1.446 -25.538 1.00 95.40 C
ANISOU 172 CB PRO A1468 7870 19559 8817 516 290 -2115 C