HEADER METAL BINDING PROTEIN 17-NOV-11 2LLS
TITLE SOLUTION STRUCTURE OF HUMAN APO-S100A1 C85M
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN S100-A1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: S-100 PROTEIN ALPHA CHAIN, S-100 PROTEIN SUBUNIT ALPHA, S100
COMPND 5 CALCIUM-BINDING PROTEIN A1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: S100A1, S100A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET-30A+
KEYWDS S100 PROTEIN FAMILY, CALCIUM BINDING PROTEIN, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.BUDZINSKA,L.JAREMKO,M.JAREMKO,K.ZDANOWSKI,I.ZHUKOV,A.BIERZYNSKI,
AUTHOR 2 A.EJCHART
REVDAT 2 14-JUN-23 2LLS 1 REMARK SEQADV
REVDAT 1 19-DEC-12 2LLS 0
JRNL AUTH M.BUDZINSKA,L.JAREMKO,M.JAREMKO,K.ZDANOWSKI,I.ZHUKOV,
JRNL AUTH 2 A.BIERZYNSKI,A.EJCHART
JRNL TITL CHEMICAL SHIFT ASSIGNMENTS AND SOLUTION STRUCTURE OF HUMAN
JRNL TITL 2 APO-S100A1 C85M MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH 2.26
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LLS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000102538.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310; 310
REMARK 210 PH : 6.8; 7.2
REMARK 210 IONIC STRENGTH : 50; 50
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 50 MM TRIS-D11, 10 % D2O, 50 MM
REMARK 210 SODIUM CHLORIDE, 1 MM [U-99% 13C;
REMARK 210 U-99% 15N] S100A1C85M, 90 % H2O,
REMARK 210 90% H2O/10% D2O; 50 MM TRIS-D11,
REMARK 210 50 MM SODIUM CHLORIDE, 1 MM [U-
REMARK 210 99% 13C; U-99% 15N] S100A1C85M,
REMARK 210 100 % D2O, 100% D2O; 50 MM TRIS-
REMARK 210 D11, 10 % D2O, 50 MM SODIUM
REMARK 210 CHLORIDE, 1 MM [U-99% 15N]
REMARK 210 S100A1C85M, 90 % H2O, 90% H2O/10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-15N HSQC
REMARK 210 NH2 ONLY; 2D 1H-13C HSQC
REMARK 210 ALIPHATIC; 2D 1H-13C HSQC
REMARK 210 AROMATIC; 3D CBCA(CO)NH; 3D HNCO;
REMARK 210 3D HNCA; 3D HNCACB; 3D HN(CO)CA;
REMARK 210 3D HBHA(CO)NH; 3D HCCH-TOCSY;
REMARK 210 3D 1H-15N NOESY; 3D 1H-13C NOESY
REMARK 210 ALIPHATIC; 3D 1H-13C NOESY
REMARK 210 AROMATIC; 2D 1H-15N
REMARK 210 HETERONUCLEAR NOE; 2D 1H-15N T1
REMARK 210 RELAXATION; 2D 1H-15N T2
REMARK 210 RELAXATION
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 500 MHZ; 700 MHZ; 800
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITYPLUS; VARIAN NMR
REMARK 210 SYSTEM
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA, NMRPIPE, SPARKY, CARA,
REMARK 210 MARS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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 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 HZ3 LYS A 30 O LEU A 61 1.34
REMARK 500 HZ3 LYS A 25 OH TYR A 26 1.35
REMARK 500 O GLU B 35 HG1 THR B 39 1.36
REMARK 500 OD2 ASP B 52 HZ1 LYS B 56 1.37
REMARK 500 O LYS A 30 HZ1 LYS A 34 1.37
REMARK 500 OD1 ASP B 46 HZ2 LYS B 49 1.37
REMARK 500 O ALA B 17 HZ3 LYS B 21 1.38
REMARK 500 OD1 ASN B 86 HE1 TRP B 90 1.39
REMARK 500 O GLU A 35 HG1 THR A 39 1.40
REMARK 500 HZ2 LYS A 59 OD2 ASP A 62 1.40
REMARK 500 O LYS B 30 HZ2 LYS B 34 1.40
REMARK 500 O LEU B 28 H VAL B 69 1.41
REMARK 500 HZ2 LYS A 27 OD2 ASP A 70 1.42
REMARK 500 O THR A 6 HG1 THR A 10 1.42
REMARK 500 O ASP A 70 H TYR A 74 1.42
REMARK 500 O PHE B 88 H ASN B 92 1.42
REMARK 500 O THR A 39 HG SER A 42 1.42
REMARK 500 HZ1 LYS B 59 OD2 ASP B 62 1.42
REMARK 500 HZ3 LYS B 27 OE1 GLU B 68 1.43
REMARK 500 OD1 ASP A 46 HZ1 LYS A 49 1.43
REMARK 500 OD2 ASP A 52 HZ1 LYS A 56 1.43
REMARK 500 O GLU A 32 H LEU A 36 1.44
REMARK 500 OE1 GLU B 22 HG SER B 29 1.44
REMARK 500 O VAL B 78 HG1 THR B 82 1.44
REMARK 500 O GLU A 3 H ALA A 7 1.44
REMARK 500 O THR B 6 HG1 THR B 10 1.45
REMARK 500 O THR A 82 H ASN A 86 1.46
REMARK 500 O PHE A 89 HG SER A 93 1.46
REMARK 500 O VAL A 78 HG1 THR A 82 1.47
REMARK 500 O GLU B 32 H LEU B 36 1.47
REMARK 500 O VAL B 83 H ASN B 87 1.48
REMARK 500 O LYS A 59 H ASP A 62 1.48
REMARK 500 O ILE A 12 H HIS A 16 1.49
REMARK 500 O GLU B 3 H ALA B 7 1.50
REMARK 500 O LEU B 4 H MET B 8 1.50
REMARK 500 HD1 HIS B 18 OE1 GLU B 32 1.51
REMARK 500 O VAL B 76 H ALA B 80 1.51
REMARK 500 O LEU B 41 H LEU B 45 1.51
REMARK 500 O LEU A 4 H MET A 8 1.52
REMARK 500 HZ3 LYS B 30 O LEU B 61 1.52
REMARK 500 O ASP B 55 H LYS B 59 1.52
REMARK 500 HE2 HIS A 18 OE2 GLU A 40 1.53
REMARK 500 HD1 HIS A 18 OE1 GLU A 32 1.53
REMARK 500 O LYS A 56 H GLU A 60 1.53
REMARK 500 OE2 GLU A 91 HH TYR B 26 1.54
REMARK 500 HH TYR A 26 OE2 GLU B 91 1.55
REMARK 500 OE2 GLU A 22 HG SER A 29 1.56
REMARK 500 H SER B 2 OE2 GLU B 5 1.56
REMARK 500 O ILE B 12 H HIS B 16 1.56
REMARK 500 H1 GLY A 1 OE1 GLU A 5 1.56
REMARK 500
REMARK 500 THIS ENTRY HAS 1318 CLOSE CONTACTS
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 TYR A 26 90.67 -168.12
REMARK 500 1 LEU A 41 39.36 -99.46
REMARK 500 1 GLN A 48 46.57 -147.83
REMARK 500 1 ASP A 70 -161.63 -122.79
REMARK 500 1 TYR B 26 93.76 -162.40
REMARK 500 1 LEU B 41 40.23 -95.43
REMARK 500 1 ASN B 64 36.07 -82.05
REMARK 500 2 GLU A 22 -3.13 -162.68
REMARK 500 2 LYS A 25 -72.75 -140.92
REMARK 500 2 TRP A 90 -82.12 -61.35
REMARK 500 2 GLU A 91 -82.05 -109.42
REMARK 500 2 ASN A 92 -154.06 -143.54
REMARK 500 2 GLU B 22 -68.37 -165.88
REMARK 500 2 ASP B 24 -158.83 36.03
REMARK 500 2 LEU B 41 44.08 -88.18
REMARK 500 2 GLN B 48 55.71 -119.86
REMARK 500 2 ASN B 64 37.14 -74.79
REMARK 500 2 TRP B 90 -83.29 -81.39
REMARK 500 2 GLU B 91 -83.14 -108.19
REMARK 500 3 LYS A 21 -82.40 -95.86
REMARK 500 3 ASP A 24 -154.90 -82.54
REMARK 500 3 LEU A 41 31.48 -94.86
REMARK 500 3 ASP A 52 -43.66 66.60
REMARK 500 3 ASP A 70 -162.50 -105.48
REMARK 500 3 LYS B 21 -75.81 -79.66
REMARK 500 3 LYS B 25 -94.27 35.26
REMARK 500 3 ASN B 64 35.01 -80.87
REMARK 500 4 ASP A 24 162.92 64.88
REMARK 500 4 TYR A 26 94.08 -167.55
REMARK 500 4 LYS A 31 -67.34 -91.63
REMARK 500 4 LEU A 41 41.03 -97.58
REMARK 500 4 GLU A 91 -64.65 -107.75
REMARK 500 4 TYR B 26 94.61 -166.04
REMARK 500 5 LEU A 41 44.78 -88.35
REMARK 500 5 ASP A 52 -30.65 62.17
REMARK 500 5 TYR B 26 90.40 -161.07
REMARK 500 5 LEU B 41 37.20 -97.31
REMARK 500 5 ASP B 52 -51.44 66.76
REMARK 500 5 ASN B 92 101.05 -48.65
REMARK 500 6 ASP A 24 -68.03 63.58
REMARK 500 6 LYS A 25 -87.88 -178.99
REMARK 500 6 LEU A 41 39.32 -95.59
REMARK 500 6 TRP A 90 -83.42 -85.66
REMARK 500 6 LEU B 41 34.57 -95.10
REMARK 500 6 TRP B 90 -72.38 -90.26
REMARK 500 7 LYS A 31 -73.87 -77.97
REMARK 500 7 LEU A 41 44.50 -87.20
REMARK 500 7 ASP A 52 -40.75 58.39
REMARK 500 7 LEU B 41 45.07 -91.87
REMARK 500 7 ASN B 64 6.36 -67.82
REMARK 500
REMARK 500 THIS ENTRY HAS 115 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18087 RELATED DB: BMRB
REMARK 900 RELATED ID: 2LP3 RELATED DB: PDB
DBREF 2LLS A 1 93 UNP P23297 S10A1_HUMAN 2 94
DBREF 2LLS B 1 93 UNP P23297 S10A1_HUMAN 2 94
SEQADV 2LLS MET A 85 UNP P23297 CYS 86 ENGINEERED MUTATION
SEQADV 2LLS MET B 85 UNP P23297 CYS 86 ENGINEERED MUTATION
SEQRES 1 A 93 GLY SER GLU LEU GLU THR ALA MET GLU THR LEU ILE ASN
SEQRES 2 A 93 VAL PHE HIS ALA HIS SER GLY LYS GLU GLY ASP LYS TYR
SEQRES 3 A 93 LYS LEU SER LYS LYS GLU LEU LYS GLU LEU LEU GLN THR
SEQRES 4 A 93 GLU LEU SER GLY PHE LEU ASP ALA GLN LYS ASP VAL ASP
SEQRES 5 A 93 ALA VAL ASP LYS VAL MET LYS GLU LEU ASP GLU ASN GLY
SEQRES 6 A 93 ASP GLY GLU VAL ASP PHE GLN GLU TYR VAL VAL LEU VAL
SEQRES 7 A 93 ALA ALA LEU THR VAL ALA MET ASN ASN PHE PHE TRP GLU
SEQRES 8 A 93 ASN SER
SEQRES 1 B 93 GLY SER GLU LEU GLU THR ALA MET GLU THR LEU ILE ASN
SEQRES 2 B 93 VAL PHE HIS ALA HIS SER GLY LYS GLU GLY ASP LYS TYR
SEQRES 3 B 93 LYS LEU SER LYS LYS GLU LEU LYS GLU LEU LEU GLN THR
SEQRES 4 B 93 GLU LEU SER GLY PHE LEU ASP ALA GLN LYS ASP VAL ASP
SEQRES 5 B 93 ALA VAL ASP LYS VAL MET LYS GLU LEU ASP GLU ASN GLY
SEQRES 6 B 93 ASP GLY GLU VAL ASP PHE GLN GLU TYR VAL VAL LEU VAL
SEQRES 7 B 93 ALA ALA LEU THR VAL ALA MET ASN ASN PHE PHE TRP GLU
SEQRES 8 B 93 ASN SER
HELIX 1 1 SER A 2 GLY A 23 1 22
HELIX 2 2 SER A 29 LEU A 41 1 13
HELIX 3 3 LEU A 41 GLN A 48 1 8
HELIX 4 4 VAL A 51 LEU A 61 1 11
HELIX 5 5 ASP A 62 GLY A 67 5 6
HELIX 6 6 ASP A 70 ASN A 92 1 23
HELIX 7 7 SER B 2 GLY B 23 1 22
HELIX 8 8 LYS B 30 LEU B 41 1 12
HELIX 9 9 LEU B 41 GLN B 48 1 8
HELIX 10 10 VAL B 51 ASN B 64 1 14
HELIX 11 11 ASP B 70 ASN B 92 1 23
SHEET 1 A 2 LEU B 28 SER B 29 0
SHEET 2 A 2 GLU B 68 VAL B 69 -1 O VAL B 69 N LEU B 28
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
