Header list of 2acm.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL PROTEIN 19-JUL-05 2ACM
TITLE SOLUTION STRUCTURE OF THE SEA DOMAIN OF HUMAN MUCIN 1 (MUC1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MUCIN-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEA DOMAIN (RESIDUES 1041-1097);
COMPND 5 SYNONYM: MUC1 MUCUS PROTEIN, MUC-1, POLYMORPHIC EPITHELIAL MUCIN,
COMPND 6 PEM, PEMT, EPISIALIN, TUMOR-ASSOCIATED MUCIN, CARCINOMA-ASSOCIATED
COMPND 7 MUCIN, TUMOR-ASSOCIATED EPITHELIAL MEMBRANE ANTIGEN, EMA, H23AG,
COMPND 8 PEANUT- REACTIVE URINARY MUCIN, PUM, BREAST CARCINOMA-ASSOCIATED
COMPND 9 ANTIGEN DF3, CD227 ANTIGEN;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: MUCIN-1;
COMPND 13 CHAIN: B;
COMPND 14 FRAGMENT: SEA DOMAIN (RESIDUES 1098-1152);
COMPND 15 SYNONYM: MUC1 MUCUS PROTEIN, MUC-1, POLYMORPHIC EPITHELIAL MUCIN,
COMPND 16 PEM, PEMT, EPISIALIN, TUMOR-ASSOCIATED MUCIN, CARCINOMA-ASSOCIATED
COMPND 17 MUCIN, TUMOR-ASSOCIATED EPITHELIAL MEMBRANE ANTIGEN, EMA, H23AG,
COMPND 18 PEANUT- REACTIVE URINARY MUCIN, PUM, BREAST CARCINOMA-ASSOCIATED
COMPND 19 ANTIGEN DF3, CD227 ANTIGEN;
COMPND 20 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: MUC1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: MUC1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: ROSETTA PLYSS;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS AUTO-CATALYTIC PROTEOLYSIS, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR B.MACAO,D.G.A.JOHANSSON,G.C.HANSSON,T.HARD
REVDAT 3 09-MAR-22 2ACM 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2ACM 1 VERSN
REVDAT 1 17-JAN-06 2ACM 0
JRNL AUTH B.MACAO,D.G.A.JOHANSSON,G.C.HANSSON,T.HARD
JRNL TITL AUTOPROTEOLYSIS COUPLED TO PROTEIN FOLDING IN THE SEA DOMAIN
JRNL TITL 2 OF THE MEMBRANE-BOUND MUC1 MUCIN
JRNL REF NAT.STRUCT.MOL.BIOL. V. 13 71 2006
JRNL REFN ISSN 1545-9993
JRNL PMID 16369486
JRNL DOI 10.1038/NSMB1035
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.10
REMARK 3 AUTHORS : C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DEPOSITED COORDINATES ARE BASED ON 1238
REMARK 3 NON-REDUNDANT NOE DISTANCE RESTRAINTS, 180 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS AND 42 DISTANCE RESTRAINTS FOR (21) HYDROGEN BONDS
REMARK 4
REMARK 4 2ACM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033744.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : 20MM KPI, 20MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM SEA DOMAIN U-15N,13C; 20MM
REMARK 210 POTASSIUM PHOSPHATE, 20MM SODIUM
REMARK 210 CHLORIDE; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; CBCA(CO)NH;
REMARK 210 HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 1032
REMARK 465 SER A 1033
REMARK 465 SER A 1034
REMARK 465 HIS A 1035
REMARK 465 HIS A 1036
REMARK 465 HIS A 1037
REMARK 465 HIS A 1038
REMARK 465 HIS A 1039
REMARK 465 HIS A 1040
REMARK 465 PRO B 1145
REMARK 465 PHE B 1146
REMARK 465 PRO B 1147
REMARK 465 PHE B 1148
REMARK 465 SER B 1149
REMARK 465 ALA B 1150
REMARK 465 GLN B 1151
REMARK 465 SER B 1152
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 TYR B 1124 H ALA B 1128 1.57
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 ASP A1060 122.81 -172.75
REMARK 500 1 LYS A1082 -15.11 -38.86
REMARK 500 2 ASP A1060 123.21 -170.29
REMARK 500 2 THR B1111 -64.71 -123.00
REMARK 500 2 SER B1137 -110.51 -97.66
REMARK 500 2 ASP B1143 -73.60 -79.74
REMARK 500 3 ASP A1060 123.46 -172.15
REMARK 500 3 LYS A1082 -25.33 -36.40
REMARK 500 3 GLN A1083 -29.99 -38.53
REMARK 500 3 THR B1111 -68.60 -123.93
REMARK 500 4 ASP A1060 118.42 -168.07
REMARK 500 4 THR B1111 -68.64 -101.51
REMARK 500 4 SER B1137 -72.32 -88.37
REMARK 500 4 ASP B1143 -88.27 -89.53
REMARK 500 5 ASP A1060 118.10 -164.16
REMARK 500 5 LYS A1082 -10.92 -40.72
REMARK 500 5 THR B1111 -65.21 -123.57
REMARK 500 6 ASP A1060 122.81 -172.75
REMARK 500 6 LYS A1082 -15.11 -38.86
REMARK 500 7 ASP A1060 123.46 -172.15
REMARK 500 7 LYS A1082 -25.33 -36.40
REMARK 500 7 GLN A1083 -29.99 -38.53
REMARK 500 7 THR B1111 -68.60 -123.93
REMARK 500 8 ASP A1060 123.55 -170.99
REMARK 500 8 THR B1111 -66.15 -124.79
REMARK 500 8 SER B1137 -74.29 -80.90
REMARK 500 9 ASP A1060 117.14 -162.20
REMARK 500 9 LYS A1082 -11.92 -41.34
REMARK 500 9 THR B1111 -70.22 -120.59
REMARK 500 10 ASP A1060 118.42 -168.07
REMARK 500 10 THR B1111 -68.64 -101.51
REMARK 500 10 SER B1137 -72.32 -88.37
REMARK 500 10 ASP B1143 -88.27 -89.53
REMARK 500 11 ASP A1060 119.15 -163.91
REMARK 500 11 LYS A1082 -8.49 -41.62
REMARK 500 11 SER B1137 -75.59 -90.39
REMARK 500 12 SER B1137 -75.90 -82.47
REMARK 500 13 ASP A1060 118.10 -164.16
REMARK 500 13 LYS A1082 -10.92 -40.72
REMARK 500 13 THR B1111 -65.21 -123.57
REMARK 500 14 ASP A1060 123.55 -170.99
REMARK 500 14 THR B1111 -66.15 -124.79
REMARK 500 14 SER B1137 -74.29 -80.90
REMARK 500 15 ASP A1060 117.14 -162.20
REMARK 500 15 LYS A1082 -11.92 -41.34
REMARK 500 15 THR B1111 -70.22 -120.59
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2ACM A 1041 1097 UNP Q16615 MUC1_HUMAN 1041 1097
DBREF 2ACM B 1098 1152 UNP Q16615 MUC1_HUMAN 1098 1152
SEQADV 2ACM GLY A 1032 UNP Q16615 EXPRESSION TAG
SEQADV 2ACM SER A 1033 UNP Q16615 EXPRESSION TAG
SEQADV 2ACM SER A 1034 UNP Q16615 EXPRESSION TAG
SEQADV 2ACM HIS A 1035 UNP Q16615 EXPRESSION TAG
SEQADV 2ACM HIS A 1036 UNP Q16615 EXPRESSION TAG
SEQADV 2ACM HIS A 1037 UNP Q16615 EXPRESSION TAG
SEQADV 2ACM HIS A 1038 UNP Q16615 EXPRESSION TAG
SEQADV 2ACM HIS A 1039 UNP Q16615 EXPRESSION TAG
SEQADV 2ACM HIS A 1040 UNP Q16615 EXPRESSION TAG
SEQRES 1 A 66 GLY SER SER HIS HIS HIS HIS HIS HIS SER PHE PHE PHE
SEQRES 2 A 66 LEU SER PHE HIS ILE SER ASN LEU GLN PHE ASN SER SER
SEQRES 3 A 66 LEU GLU ASP PRO SER THR ASP TYR TYR GLN GLU LEU GLN
SEQRES 4 A 66 ARG ASP ILE SER GLU MET PHE LEU GLN ILE TYR LYS GLN
SEQRES 5 A 66 GLY GLY PHE LEU GLY LEU SER ASN ILE LYS PHE ARG PRO
SEQRES 6 A 66 GLY
SEQRES 1 B 55 SER VAL VAL VAL GLN LEU THR LEU ALA PHE ARG GLU GLY
SEQRES 2 B 55 THR ILE ASN VAL HIS ASP VAL GLU THR GLN PHE ASN GLN
SEQRES 3 B 55 TYR LYS THR GLU ALA ALA SER ARG TYR ASN LEU THR ILE
SEQRES 4 B 55 SER ASP VAL SER VAL SER ASP VAL PRO PHE PRO PHE SER
SEQRES 5 B 55 ALA GLN SER
HELIX 1 1 ASN A 1055 ASP A 1060 5 6
HELIX 2 2 THR A 1063 TYR A 1081 1 19
HELIX 3 3 ASN B 1113 ASN B 1133 1 21
SHEET 1 A 4 PHE A1086 PRO A1096 0
SHEET 2 A 4 VAL B1099 PHE B1107 -1 O VAL B1100 N ARG A1095
SHEET 3 A 4 PHE A1042 ILE A1049 -1 N PHE A1043 O LEU B1105
SHEET 4 A 4 ILE B1136 SER B1142 -1 O SER B1137 N HIS A1048
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
Complete list - r 9 2 Bytes