HEADER METAL BINDING PROTEIN 22-OCT-10 2L50
TITLE SOLUTION STRUCTURE OF APO S100A16
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN S100-A16;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AGING-ASSOCIATED GENE 13 PROTEIN, PROTEIN S100-F, S100
COMPND 5 CALCIUM-BINDING PROTEIN A16;
COMPND 6 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: S100A16, S100F, AAG13;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET21A
KEYWDS METAL BINDING PROTEIN, APOS100A16, EF-HAND PROTEIN, S100 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR E.BABINI,I.BERTINI,V.BORSI,V.CALDERONE,X.HU,C.LUCHINAT,G.PARIGI
REVDAT 5 14-JUN-23 2L50 1 REMARK
REVDAT 4 05-FEB-20 2L50 1 REMARK
REVDAT 3 16-FEB-11 2L50 1 JRNL
REVDAT 2 08-DEC-10 2L50 1 JRNL
REVDAT 1 03-NOV-10 2L50 0
SPRSDE 03-NOV-10 2L50 2L0U
JRNL AUTH E.BABINI,I.BERTINI,V.BORSI,V.CALDERONE,X.HU,C.LUCHINAT,
JRNL AUTH 2 G.PARIGI
JRNL TITL STRUCTURAL CHARACTERIZATION OF HUMAN S100A16, A LOW-AFFINITY
JRNL TITL 2 CALCIUM BINDER.
JRNL REF J.BIOL.INORG.CHEM. V. 16 243 2011
JRNL REFN ISSN 0949-8257
JRNL PMID 21046186
JRNL DOI 10.1007/S00775-010-0721-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 10.0, WHAT IF
REMARK 3 AUTHORS : CASE, DARDEN, CHEATHAM, III, SIMMERLING, WANG,
REMARK 3 DUKE, LUO, ... AND KOLLM (AMBER), VRIEND (WHAT IF)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2L50 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000101964.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6 MM [U-100% 13C; U-100% 15N]
REMARK 210 APOS100A16, 90% H2O/10% D2O; 0.6
REMARK 210 MM [U-100% 15N] APOS100A16, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 2D 1H-1H NOESY; 3D CBCA(CO)NH;
REMARK 210 3D HNCO; 3D HNCA; 3D HNCACB; 3D
REMARK 210 HBHA(CO)NH; 3D HCCH-TOCSY; 3D 1H-
REMARK 210 15N NOESY; 3D 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 700 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AMBER 10.0, CYANA 2.1, MOLMOL,
REMARK 210 PROCHECKNMR, TALOS, TOPSPIN 2.0,
REMARK 210 XEASY, CARA, WHAT IF
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 350
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 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
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 PHE A 19 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 1 PHE B 122 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 5 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 5 ARG B 142 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 7 ARG A 39 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 7 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 7 ARG B 142 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 ARG B 142 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 7 ARG B 176 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 10 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 10 ARG B 159 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 12 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 12 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 12 ARG B 159 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 12 ARG B 159 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 13 ARG B 176 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 16 ARG B 159 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 18 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 18 ARG B 159 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 18 ARG B 176 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 19 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 21 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 21 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 22 ARG B 142 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 23 ARG A 73 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 23 ARG B 159 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 25 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 25 TYR B 108 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 26 ARG B 159 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 27 ARG B 159 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 29 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 29 ARG B 159 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 30 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 30 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 30 ARG B 142 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 30 ARG B 159 NE - CZ - NH1 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 CYS A 4 -23.38 69.05
REMARK 500 1 TYR A 5 102.07 65.17
REMARK 500 1 PHE A 19 -61.59 -98.80
REMARK 500 1 LYS A 25 -52.10 71.91
REMARK 500 1 LEU A 28 -7.43 -39.65
REMARK 500 1 VAL A 29 -44.96 -130.37
REMARK 500 1 SER A 51 -47.21 -159.19
REMARK 500 1 ASP A 52 -26.78 -37.72
REMARK 500 1 THR A 53 -25.01 71.79
REMARK 500 1 GLU A 98 0.85 -69.34
REMARK 500 1 GLN A 99 -60.84 -120.93
REMARK 500 1 GLN A 100 1.06 54.99
REMARK 500 1 SER A 102 38.40 -158.80
REMARK 500 1 CYS B 107 -23.43 69.91
REMARK 500 1 TYR B 108 102.03 65.35
REMARK 500 1 PHE B 122 -63.75 -95.17
REMARK 500 1 LYS B 128 -52.60 77.19
REMARK 500 1 LEU B 131 -13.39 -20.99
REMARK 500 1 VAL B 132 -47.32 -132.59
REMARK 500 1 SER B 154 -47.29 -160.94
REMARK 500 1 ASP B 155 -27.69 -37.72
REMARK 500 1 THR B 156 -22.17 71.71
REMARK 500 1 GLN B 202 -57.80 -120.23
REMARK 500 1 GLN B 203 1.18 56.11
REMARK 500 1 SER B 205 43.71 -159.68
REMARK 500 2 ASP A 3 -117.53 -55.39
REMARK 500 2 CYS A 4 -95.70 -96.77
REMARK 500 2 TYR A 5 153.42 140.95
REMARK 500 2 SER A 24 -81.44 -175.10
REMARK 500 2 LYS A 25 -60.43 179.85
REMARK 500 2 LYS A 32 -52.91 -173.23
REMARK 500 2 GLU A 45 -74.35 -74.64
REMARK 500 2 LEU A 46 32.68 -74.77
REMARK 500 2 SER A 51 -82.52 54.86
REMARK 500 2 ASN A 69 -34.28 -135.99
REMARK 500 2 THR A 87 31.89 -75.97
REMARK 500 2 GLN A 99 -61.20 -132.41
REMARK 500 2 GLN A 100 14.12 57.32
REMARK 500 2 SER A 101 32.70 -158.89
REMARK 500 2 ASP B 106 -117.88 -50.50
REMARK 500 2 CYS B 107 -96.68 -98.60
REMARK 500 2 TYR B 108 150.26 135.44
REMARK 500 2 SER B 127 -80.47 176.83
REMARK 500 2 LYS B 128 -60.24 178.25
REMARK 500 2 ASN B 134 126.60 -39.58
REMARK 500 2 LYS B 135 -55.87 -171.27
REMARK 500 2 GLU B 148 -74.23 -74.27
REMARK 500 2 LEU B 149 33.61 -75.11
REMARK 500 2 SER B 154 -82.13 56.75
REMARK 500 2 ASN B 172 -35.02 -136.34
REMARK 500
REMARK 500 THIS ENTRY HAS 697 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 SER A 2 ASP A 3 1 -133.48
REMARK 500 TYR A 26 SER A 27 1 -143.20
REMARK 500 SER B 105 ASP B 106 1 -134.02
REMARK 500 TYR B 129 SER B 130 1 -142.40
REMARK 500 SER A 2 ASP A 3 2 113.00
REMARK 500 ARG A 73 ILE A 74 2 148.47
REMARK 500 SER B 105 ASP B 106 2 109.46
REMARK 500 SER A 2 ASP A 3 3 140.75
REMARK 500 SER B 105 ASP B 106 3 138.82
REMARK 500 SER A 2 ASP A 3 4 -134.68
REMARK 500 SER B 105 ASP B 106 4 -134.52
REMARK 500 SER A 2 ASP A 3 5 -132.18
REMARK 500 SER B 105 ASP B 106 5 -132.25
REMARK 500 SER A 2 ASP A 3 6 -134.18
REMARK 500 GLY A 72 ARG A 73 6 149.68
REMARK 500 SER B 105 ASP B 106 6 -135.28
REMARK 500 TYR A 26 SER A 27 7 -140.69
REMARK 500 TYR B 129 SER B 130 7 -140.89
REMARK 500 HIS B 173 ASP B 174 7 149.06
REMARK 500 SER A 2 ASP A 3 8 -133.29
REMARK 500 SER B 105 ASP B 106 8 -138.07
REMARK 500 PHE B 179 ASP B 180 8 149.58
REMARK 500 SER A 2 ASP A 3 9 -148.68
REMARK 500 ASP A 52 THR A 53 9 147.70
REMARK 500 SER B 105 ASP B 106 9 -125.18
REMARK 500 ASP B 155 THR B 156 9 148.67
REMARK 500 SER A 2 ASP A 3 10 -131.00
REMARK 500 SER A 51 ASP A 52 10 136.97
REMARK 500 SER B 105 ASP B 106 10 -131.70
REMARK 500 SER B 154 ASP B 155 10 138.03
REMARK 500 SER A 2 ASP A 3 11 135.58
REMARK 500 SER B 105 ASP B 106 11 137.87
REMARK 500 ILE A 33 SER A 34 12 148.40
REMARK 500 GLY A 72 ARG A 73 12 146.45
REMARK 500 SER B 105 ASP B 106 12 138.53
REMARK 500 ASP B 155 THR B 156 12 -134.38
REMARK 500 GLY B 175 ARG B 176 12 131.81
REMARK 500 SER A 102 SER A 103 13 -149.24
REMARK 500 SER B 205 SER B 206 13 -148.62
REMARK 500 SER A 2 ASP A 3 14 -133.19
REMARK 500 SER A 51 ASP A 52 14 -146.07
REMARK 500 SER A 102 SER A 103 14 145.40
REMARK 500 SER B 105 ASP B 106 14 -133.76
REMARK 500 SER B 154 ASP B 155 14 -144.98
REMARK 500 SER B 205 SER B 206 14 139.84
REMARK 500 SER A 2 ASP A 3 15 139.43
REMARK 500 LYS A 32 ILE A 33 15 133.12
REMARK 500 SER A 102 SER A 103 15 -137.27
REMARK 500 SER B 105 ASP B 106 15 137.06
REMARK 500 LYS B 135 ILE B 136 15 136.06
REMARK 500
REMARK 500 THIS ENTRY HAS 101 NON CIS, NON-TRANS OMEGA 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 56 0.18 SIDE CHAIN
REMARK 500 1 ARG B 159 0.19 SIDE CHAIN
REMARK 500 2 TYR A 5 0.10 SIDE CHAIN
REMARK 500 2 TYR B 108 0.10 SIDE CHAIN
REMARK 500 3 ARG B 159 0.14 SIDE CHAIN
REMARK 500 4 PHE A 76 0.08 SIDE CHAIN
REMARK 500 4 PHE B 179 0.08 SIDE CHAIN
REMARK 500 6 ARG B 159 0.10 SIDE CHAIN
REMARK 500 7 TYR A 5 0.09 SIDE CHAIN
REMARK 500 7 ARG A 39 0.16 SIDE CHAIN
REMARK 500 7 HIS A 95 0.12 SIDE CHAIN
REMARK 500 7 TYR B 108 0.12 SIDE CHAIN
REMARK 500 7 ARG B 142 0.14 SIDE CHAIN
REMARK 500 7 HIS B 198 0.14 SIDE CHAIN
REMARK 500 9 ARG A 73 0.08 SIDE CHAIN
REMARK 500 9 PHE A 76 0.09 SIDE CHAIN
REMARK 500 9 PHE B 179 0.08 SIDE CHAIN
REMARK 500 10 ARG A 56 0.08 SIDE CHAIN
REMARK 500 10 ARG A 73 0.08 SIDE CHAIN
REMARK 500 10 PHE A 76 0.10 SIDE CHAIN
REMARK 500 10 TYR B 125 0.07 SIDE CHAIN
REMARK 500 10 ARG B 176 0.08 SIDE CHAIN
REMARK 500 10 PHE B 179 0.10 SIDE CHAIN
REMARK 500 11 ARG A 56 0.09 SIDE CHAIN
REMARK 500 12 ARG A 56 0.13 SIDE CHAIN
REMARK 500 12 ARG B 159 0.09 SIDE CHAIN
REMARK 500 14 ARG A 39 0.10 SIDE CHAIN
REMARK 500 14 PHE A 76 0.12 SIDE CHAIN
REMARK 500 14 ARG B 142 0.10 SIDE CHAIN
REMARK 500 14 ARG B 159 0.20 SIDE CHAIN
REMARK 500 14 PHE B 179 0.11 SIDE CHAIN
REMARK 500 15 ARG A 73 0.08 SIDE CHAIN
REMARK 500 15 TYR A 79 0.10 SIDE CHAIN
REMARK 500 15 ARG B 176 0.10 SIDE CHAIN
REMARK 500 16 TYR A 22 0.07 SIDE CHAIN
REMARK 500 16 HIS A 95 0.10 SIDE CHAIN
REMARK 500 16 HIS B 198 0.09 SIDE CHAIN
REMARK 500 18 PHE A 76 0.08 SIDE CHAIN
REMARK 500 18 PHE B 179 0.08 SIDE CHAIN
REMARK 500 18 TYR B 182 0.09 SIDE CHAIN
REMARK 500 19 ARG B 176 0.12 SIDE CHAIN
REMARK 500 20 ARG A 56 0.16 SIDE CHAIN
REMARK 500 20 TYR B 108 0.07 SIDE CHAIN
REMARK 500 20 ARG B 159 0.17 SIDE CHAIN
REMARK 500 20 PHE B 179 0.07 SIDE CHAIN
REMARK 500 23 ARG B 159 0.14 SIDE CHAIN
REMARK 500 23 ARG B 176 0.13 SIDE CHAIN
REMARK 500 24 HIS A 95 0.09 SIDE CHAIN
REMARK 500 24 HIS B 151 0.08 SIDE CHAIN
REMARK 500 24 TYR B 182 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 17261 RELATED DB: BMRB
REMARK 900 RELATED ID: 2L51 RELATED DB: PDB
DBREF 2L50 A 2 103 UNP Q96FQ6 S10AG_HUMAN 2 103
DBREF 2L50 B 105 206 UNP Q96FQ6 S10AG_HUMAN 2 103
SEQRES 1 A 102 SER ASP CYS TYR THR GLU LEU GLU LYS ALA VAL ILE VAL
SEQRES 2 A 102 LEU VAL GLU ASN PHE TYR LYS TYR VAL SER LYS TYR SER
SEQRES 3 A 102 LEU VAL LYS ASN LYS ILE SER LYS SER SER PHE ARG GLU
SEQRES 4 A 102 MET LEU GLN LYS GLU LEU ASN HIS MET LEU SER ASP THR
SEQRES 5 A 102 GLY ASN ARG LYS ALA ALA ASP LYS LEU ILE GLN ASN LEU
SEQRES 6 A 102 ASP ALA ASN HIS ASP GLY ARG ILE SER PHE ASP GLU TYR
SEQRES 7 A 102 TRP THR LEU ILE GLY GLY ILE THR GLY PRO ILE ALA LYS
SEQRES 8 A 102 LEU ILE HIS GLU GLN GLU GLN GLN SER SER SER
SEQRES 1 B 102 SER ASP CYS TYR THR GLU LEU GLU LYS ALA VAL ILE VAL
SEQRES 2 B 102 LEU VAL GLU ASN PHE TYR LYS TYR VAL SER LYS TYR SER
SEQRES 3 B 102 LEU VAL LYS ASN LYS ILE SER LYS SER SER PHE ARG GLU
SEQRES 4 B 102 MET LEU GLN LYS GLU LEU ASN HIS MET LEU SER ASP THR
SEQRES 5 B 102 GLY ASN ARG LYS ALA ALA ASP LYS LEU ILE GLN ASN LEU
SEQRES 6 B 102 ASP ALA ASN HIS ASP GLY ARG ILE SER PHE ASP GLU TYR
SEQRES 7 B 102 TRP THR LEU ILE GLY GLY ILE THR GLY PRO ILE ALA LYS
SEQRES 8 B 102 LEU ILE HIS GLU GLN GLU GLN GLN SER SER SER
HELIX 1 1 THR A 6 LYS A 21 1 16
HELIX 2 2 SER A 34 SER A 36 5 3
HELIX 3 3 SER A 37 LEU A 46 1 10
HELIX 4 4 THR A 53 ALA A 68 1 16
HELIX 5 5 SER A 75 THR A 87 1 13
HELIX 6 6 GLY A 88 GLU A 98 1 11
HELIX 7 7 THR B 109 LYS B 124 1 16
HELIX 8 8 SER B 137 LEU B 149 1 13
HELIX 9 9 THR B 156 ALA B 171 1 16
HELIX 10 10 SER B 178 THR B 190 1 13
HELIX 11 11 GLY B 191 GLU B 201 1 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 LINES ARE NOT SHOWN.)
END
