HEADER METAL BINDING PROTEIN 02-DEC-08 2KBM
TITLE CA-S100A1 INTERACTING WITH TRTK12
CAVEAT 2KBM ARG X 2 HAS WRONG CHIRALITY AT ATOM CA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA-2;
COMPND 3 CHAIN: X, Y;
COMPND 4 SYNONYM: CAPZ ALPHA-2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROTEIN S100-A1;
COMPND 8 CHAIN: A, B;
COMPND 9 SYNONYM: S100 CALCIUM-BINDING PROTEIN A1, S-100 PROTEIN ALPHA
COMPND 10 SUBUNIT, S-100 PROTEIN ALPHA CHAIN;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: CAPZA2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET21A;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 11 ORGANISM_COMMON: RAT;
SOURCE 12 ORGANISM_TAXID: 10116;
SOURCE 13 GENE: S100A1;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR: PET21A
KEYWDS S100, EF-HAND, PROTEIN-PROTEIN INTERACTION, CONFORMATIONAL CHANGE,
KEYWDS 2 CAPZ, ACETYLATION, ACTIN CAPPING, ACTIN-BINDING, CALCIUM, CYTOPLASM,
KEYWDS 3 METAL-BINDING, ZINC, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.T.WRIGHT,K.M.VARNEY,B.R.CANNON,M.MORGAN,D.J.WEBER
REVDAT 2 08-AUG-18 2KBM 1 CAVEAT REMARK LINK
REVDAT 1 10-FEB-09 2KBM 0
JRNL AUTH N.T.WRIGHT,M.T.MORGAN,B.R.CANNON,K.M.VARNEY,D.J.WEBER
JRNL TITL SOLUTION STRUCTURE OF CA-S100A1-TRTK12
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, X-PLOR_NIH
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE (X
REMARK 3 -PLOR_NIH), SCHWIETERS, KUSZEWSKI, TJANDRA AND
REMARK 3 CLORE (X-PLOR_NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KBM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000100918.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 0.05
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 10 % D2O-1, 10 MM CALCIUM ION-2,
REMARK 210 10 MM DTT-3, 10 MM TRIS-4, 25 MM
REMARK 210 SODIUM CHLORIDE-5, 500 UM [U-100%
REMARK 210 13C; U-100% 15N] ENTITY_1-6,
REMARK 210 1500 UM ENTITY_3-7, 90% H2O/10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D CBCA(CO)NH;
REMARK 210 3D HNCACB; 3D C(CO)NH; 3D H(CCO)
REMARK 210 NH; 3D HNCO; 3D HNHA; 3D HN(CO)
REMARK 210 CA; IPAP-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING, DGSA
REMARK 210 -DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, Y, 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 O TRP Y 7 H ILE Y 10 1.50
REMARK 500 O TRP X 7 H ILE X 10 1.54
REMARK 500 O ASP A 35 HG1 THR A 39 1.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 SER A 93 CB SER A 93 OG 0.119
REMARK 500 1 SER B 93 CB SER B 93 OG 0.120
REMARK 500 2 SER A 93 CB SER A 93 OG 0.112
REMARK 500 2 SER B 93 CB SER B 93 OG 0.113
REMARK 500 3 LYS X 4 N LYS X 4 CA 0.157
REMARK 500 3 LYS X 4 CA LYS X 4 CB -0.188
REMARK 500 3 SER A 93 CB SER A 93 OG 0.110
REMARK 500 3 SER B 93 CB SER B 93 OG 0.111
REMARK 500 4 SER A 93 CB SER A 93 OG 0.112
REMARK 500 4 SER B 93 CB SER B 93 OG 0.113
REMARK 500 5 SER A 93 CB SER A 93 OG 0.111
REMARK 500 5 SER B 93 CB SER B 93 OG 0.110
REMARK 500 6 SER A 93 CB SER A 93 OG 0.115
REMARK 500 6 SER B 93 CB SER B 93 OG 0.115
REMARK 500 7 SER A 93 CB SER A 93 OG 0.111
REMARK 500 7 SER B 93 CB SER B 93 OG 0.113
REMARK 500 8 SER A 93 CB SER A 93 OG 0.113
REMARK 500 8 SER B 93 CB SER B 93 OG 0.115
REMARK 500 9 ARG X 2 N ARG X 2 CA 0.196
REMARK 500 9 ARG X 2 CA ARG X 2 CB -0.152
REMARK 500 9 ARG X 2 CA ARG X 2 C -0.217
REMARK 500 9 SER A 93 CB SER A 93 OG 0.113
REMARK 500 9 SER B 93 CB SER B 93 OG 0.114
REMARK 500 10 SER A 93 CB SER A 93 OG 0.111
REMARK 500 10 SER B 93 CB SER B 93 OG 0.113
REMARK 500 11 SER A 93 CB SER A 93 OG 0.111
REMARK 500 11 SER B 93 CB SER B 93 OG 0.112
REMARK 500 12 SER A 93 CB SER A 93 OG 0.113
REMARK 500 12 SER B 93 CB SER B 93 OG 0.111
REMARK 500 13 SER A 93 CB SER A 93 OG 0.114
REMARK 500 13 SER B 93 CB SER B 93 OG 0.113
REMARK 500 14 SER A 93 CB SER A 93 OG 0.114
REMARK 500 14 SER B 93 CB SER B 93 OG 0.113
REMARK 500 15 SER A 93 CB SER A 93 OG 0.113
REMARK 500 15 SER B 93 CB SER B 93 OG 0.114
REMARK 500 16 SER A 93 CB SER A 93 OG 0.113
REMARK 500 16 SER B 93 CB SER B 93 OG 0.114
REMARK 500 17 SER A 93 CB SER A 93 OG 0.117
REMARK 500 17 SER B 93 CB SER B 93 OG 0.119
REMARK 500 18 SER A 93 CB SER A 93 OG 0.118
REMARK 500 18 SER B 93 CB SER B 93 OG 0.114
REMARK 500 19 SER A 93 CB SER A 93 OG 0.112
REMARK 500 19 SER B 93 CB SER B 93 OG 0.113
REMARK 500 20 SER A 93 CB SER A 93 OG 0.111
REMARK 500 20 SER B 93 CB SER B 93 OG 0.111
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 3 LYS X 4 CB - CA - C ANGL. DEV. = 21.5 DEGREES
REMARK 500 9 ARG X 2 C - N - CA ANGL. DEV. = -18.9 DEGREES
REMARK 500 9 ARG X 2 CB - CA - C ANGL. DEV. = 27.4 DEGREES
REMARK 500 9 ARG X 2 CA - C - O ANGL. DEV. = -14.2 DEGREES
REMARK 500 9 ARG X 2 CA - C - N ANGL. DEV. = 14.4 DEGREES
REMARK 500 16 ARG X 2 O - C - N ANGL. DEV. = -10.8 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 PHE A 44 -103.87 -87.91
REMARK 500 1 LEU A 45 153.52 -15.42
REMARK 500 1 VAL A 47 -79.69 -128.39
REMARK 500 1 ASP A 62 42.92 -77.49
REMARK 500 1 PHE B 44 -89.70 -89.71
REMARK 500 1 LEU B 45 160.04 -39.68
REMARK 500 1 VAL B 47 -79.11 -128.45
REMARK 500 1 ASP B 62 42.73 -77.28
REMARK 500 2 THR X 3 112.41 -174.08
REMARK 500 2 LYS X 4 106.04 51.91
REMARK 500 2 ASP X 6 19.71 43.44
REMARK 500 2 LYS A 21 -65.15 -124.22
REMARK 500 2 GLU A 22 20.70 -69.90
REMARK 500 2 ASP A 24 152.34 -39.29
REMARK 500 2 PHE A 44 -106.18 -83.83
REMARK 500 2 LEU A 45 127.65 -9.69
REMARK 500 2 VAL A 47 -40.19 -148.76
REMARK 500 2 ASP A 66 -117.36 -93.71
REMARK 500 2 LYS B 21 -65.54 -124.05
REMARK 500 2 GLU B 22 20.72 -69.94
REMARK 500 2 ASP B 24 152.31 -39.57
REMARK 500 2 PHE B 44 -92.29 -84.53
REMARK 500 2 LEU B 45 134.86 -33.52
REMARK 500 2 VAL B 47 -39.97 -148.66
REMARK 500 2 ASP B 66 -117.31 -93.97
REMARK 500 3 THR X 3 -160.45 54.03
REMARK 500 3 LYS X 4 109.45 78.61
REMARK 500 3 ASP X 6 18.37 47.35
REMARK 500 3 THR Y 3 43.20 -143.76
REMARK 500 3 ILE Y 5 97.08 34.69
REMARK 500 3 PHE A 44 -105.15 -95.14
REMARK 500 3 LEU A 45 154.07 -13.54
REMARK 500 3 VAL A 47 -83.74 -145.00
REMARK 500 3 ASP A 62 43.54 -73.12
REMARK 500 3 PHE B 44 -92.11 -96.42
REMARK 500 3 LEU B 45 160.03 -37.84
REMARK 500 3 VAL B 47 -83.45 -144.91
REMARK 500 3 ASP B 62 43.56 -73.30
REMARK 500 4 ARG X 2 -143.19 50.03
REMARK 500 4 ILE X 5 115.16 -161.26
REMARK 500 4 PHE A 44 -105.86 -84.07
REMARK 500 4 LEU A 45 153.50 -16.33
REMARK 500 4 VAL A 47 -61.82 -148.18
REMARK 500 4 ASP A 62 43.35 -77.96
REMARK 500 4 PHE B 44 -92.37 -85.64
REMARK 500 4 LEU B 45 160.08 -39.93
REMARK 500 4 VAL B 47 -61.54 -148.14
REMARK 500 4 ASP B 62 43.11 -77.98
REMARK 500 5 THR X 3 -142.19 -166.31
REMARK 500 5 LYS X 4 -165.14 38.98
REMARK 500
REMARK 500 THIS ENTRY HAS 296 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 16 ARG X 2 -17.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 100 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 19 O
REMARK 620 2 ASP A 24 N 102.2
REMARK 620 3 ASP A 24 O 52.3 64.0
REMARK 620 4 LYS A 27 O 102.4 95.4 72.3
REMARK 620 5 GLU A 32 OE2 82.1 116.5 130.1 146.4
REMARK 620 6 GLU A 32 OE1 104.8 145.1 150.8 99.9 47.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 102 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 62 OD2
REMARK 620 2 ASP A 66 OD1 93.4
REMARK 620 3 GLU A 68 O 97.8 67.3
REMARK 620 4 GLU A 73 OE2 157.8 100.0 103.7
REMARK 620 5 ASP A 62 OD1 9.1 95.6 90.5 162.1
REMARK 620 6 GLU A 73 OE1 128.3 136.1 91.3 46.5 123.6
REMARK 620 7 LEU A 61 O 92.4 142.0 148.4 66.2 96.0 59.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 101 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 19 O
REMARK 620 2 ASP B 24 N 100.6
REMARK 620 3 ASP B 24 O 50.7 67.9
REMARK 620 4 LYS B 27 O 101.7 109.2 77.4
REMARK 620 5 GLU B 32 OE2 72.5 111.1 119.7 139.7
REMARK 620 6 GLU B 32 OE1 92.1 144.0 140.1 100.9 41.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 103 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 62 OD2
REMARK 620 2 ASP B 66 OD1 93.0
REMARK 620 3 GLU B 68 O 96.4 63.9
REMARK 620 4 GLU B 73 OE2 162.6 97.9 100.5
REMARK 620 5 ASP B 62 OD1 9.9 93.6 87.8 167.9
REMARK 620 6 GLU B 73 OE1 130.8 131.5 88.2 46.7 125.8
REMARK 620 7 LEU B 61 O 95.3 144.8 148.1 68.1 100.2 61.9
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2K2F RELATED DB: PDB
REMARK 900 RELATED ID: 1ZFS RELATED DB: PDB
REMARK 900 RELATED ID: 16050 RELATED DB: BMRB
DBREF 2KBM X 1 12 UNP Q3T1K5 CAZA2_RAT 265 276
DBREF 2KBM Y 1 12 UNP Q3T1K5 CAZA2_RAT 265 276
DBREF 2KBM A 1 93 UNP P35467 S10A1_RAT 2 94
DBREF 2KBM B 1 93 UNP P35467 S10A1_RAT 2 94
SEQRES 1 X 12 THR ARG THR LYS ILE ASP TRP ASN LYS ILE LEU SER
SEQRES 1 Y 12 THR ARG THR LYS ILE ASP TRP ASN LYS ILE LEU SER
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 ASP LEU LEU GLN THR
SEQRES 4 A 93 GLU LEU SER SER PHE LEU ASP VAL GLN LYS ASP ALA ASP
SEQRES 5 A 93 ALA VAL ASP LYS ILE MET LYS GLU LEU ASP GLU ASN GLY
SEQRES 6 A 93 ASP GLY GLU VAL ASP PHE GLN GLU PHE VAL VAL LEU VAL
SEQRES 7 A 93 ALA ALA LEU THR VAL ALA CYS 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 ASP LEU LEU GLN THR
SEQRES 4 B 93 GLU LEU SER SER PHE LEU ASP VAL GLN LYS ASP ALA ASP
SEQRES 5 B 93 ALA VAL ASP LYS ILE MET LYS GLU LEU ASP GLU ASN GLY
SEQRES 6 B 93 ASP GLY GLU VAL ASP PHE GLN GLU PHE VAL VAL LEU VAL
SEQRES 7 B 93 ALA ALA LEU THR VAL ALA CYS ASN ASN PHE PHE TRP GLU
SEQRES 8 B 93 ASN SER
HET CA A 100 1
HET CA A 102 1
HET CA B 101 1
HET CA B 103 1
HETNAM CA CALCIUM ION
FORMUL 5 CA 4(CA 2+)
HELIX 1 1 ASP X 6 SER X 12 1 7
HELIX 2 2 ASP Y 6 SER Y 12 1 7
HELIX 3 3 SER A 2 GLY A 20 1 19
HELIX 4 4 LYS A 30 SER A 42 1 13
HELIX 5 5 VAL A 47 LYS A 49 5 3
HELIX 6 6 ASP A 50 ASP A 62 1 13
HELIX 7 7 ASP A 70 TRP A 90 1 21
HELIX 8 8 SER B 2 GLY B 20 1 19
HELIX 9 9 LYS B 30 SER B 42 1 13
HELIX 10 10 VAL B 47 LYS B 49 5 3
HELIX 11 11 ASP B 50 ASP B 62 1 13
HELIX 12 12 ASP B 70 TRP B 90 1 21
SHEET 1 A 2 LEU A 28 SER A 29 0
SHEET 2 A 2 GLU A 68 VAL A 69 -1 O VAL A 69 N LEU A 28
SHEET 1 B 2 LEU B 28 SER B 29 0
SHEET 2 B 2 GLU B 68 VAL B 69 -1 O VAL B 69 N LEU B 28
LINK O SER A 19 CA CA A 100 1555 1555 2.55
LINK N ASP A 24 CA CA A 100 1555 1555 2.44
LINK O ASP A 24 CA CA A 100 1555 1555 2.80
LINK O LYS A 27 CA CA A 100 1555 1555 2.43
LINK OE2 GLU A 32 CA CA A 100 1555 1555 2.90
LINK OD2 ASP A 62 CA CA A 102 1555 1555 4.97
LINK OD1 ASP A 66 CA CA A 102 1555 1555 2.77
LINK O GLU A 68 CA CA A 102 1555 1555 2.39
LINK OE2 GLU A 73 CA CA A 102 1555 1555 2.89
LINK O SER B 19 CA CA B 101 1555 1555 2.80
LINK N ASP B 24 CA CA B 101 1555 1555 2.23
LINK O ASP B 24 CA CA B 101 1555 1555 2.72
LINK O LYS B 27 CA CA B 101 1555 1555 2.19
LINK OE2 GLU B 32 CA CA B 101 1555 1555 3.25
LINK OD2 ASP B 62 CA CA B 103 1555 1555 4.94
LINK OD1 ASP B 66 CA CA B 103 1555 1555 2.88
LINK O GLU B 68 CA CA B 103 1555 1555 2.55
LINK OE2 GLU B 73 CA CA B 103 1555 1555 2.88
LINK OE1 GLU A 32 CA CA A 100 1555 1555 2.15
LINK OD1 ASP A 62 CA CA A 102 1555 1555 2.90
LINK OE1 GLU A 73 CA CA A 102 1555 1555 2.48
LINK OE1 GLU B 32 CA CA B 101 1555 1555 2.37
LINK OD1 ASP B 62 CA CA B 103 1555 1555 2.88
LINK OE1 GLU B 73 CA CA B 103 1555 1555 2.46
LINK O LEU A 61 CA CA A 102 1555 1555 2.58
LINK O LEU B 61 CA CA B 103 1555 1555 2.43
SITE 1 AC1 6 HIS A 18 SER A 19 GLU A 22 GLY A 23
SITE 2 AC1 6 ASP A 24 LEU A 28
SITE 1 AC2 3 SER B 19 GLU B 22 LYS B 27
SITE 1 AC3 4 LYS A 27 LEU A 61 ASP A 62 GLU A 63
SITE 1 AC4 3 ASP B 62 GLU B 63 ASN B 64
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
