Header list of 1ozo.pdb file
Complete list - b 23 2 Bytes
HEADER METAL BINDING PROTEIN 09-APR-03 1OZO
TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF APO-S100P PROTEIN DETERMINED
TITLE 2 BY NMR SPECTROSCOPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-100P PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 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: S100P OR S100E;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EF-HAND, S100 PROTEIN, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR Y.-C.LEE,D.E.VOLK,V.THIVIYANATHAN,Q.KLEEREKOPER,A.V.GRIBENKO,S.ZHANG,
AUTHOR 2 D.G.GORENSTEIN,G.I.MAKHATADZE,B.A.LUXON
REVDAT 4 23-FEB-22 1OZO 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1OZO 1 VERSN
REVDAT 2 10-AUG-04 1OZO 1 JRNL
REVDAT 1 20-APR-04 1OZO 0
JRNL AUTH Y.-C.LEE,D.E.VOLK,V.THIVIYANATHAN,Q.KLEEREKOPER,
JRNL AUTH 2 A.V.GRIBENKO,S.ZHANG,D.G.GORENSTEIN,G.I.MAKHATADZE,B.A.LUXON
JRNL TITL NMR STRUCTURE OF THE APO-S100P PROTEIN.
JRNL REF J.BIOMOL.NMR V. 29 399 2004
JRNL REFN ISSN 0925-2738
JRNL PMID 15213440
JRNL DOI 10.1023/B:JNMR.0000032617.88899.4B
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 98, DIAMD
REMARK 3 AUTHORS : MSI (FELIX), XU, BRAUN (DIAMD)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 3344 RESTRAINTS, 3104 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 122 CSI-BASED TORSIONAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1OZO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018844.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.5-3 MM S100P 15N/13C; 20 MM
REMARK 210 TRIS-D6 BUFFER, 100MM KCL, 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AMBER 6/7, DIAMD
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 15
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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 HG SER B 72 OE2 GLU B 73 1.30
REMARK 500 HG SER A 85 OE2 GLU B 5 1.30
REMARK 500 HG SER A 47 OD2 ASP A 52 1.36
REMARK 500 OD2 ASP A 70 HG SER A 72 1.37
REMARK 500 HG SER B 47 OD2 ASP B 50 1.37
REMARK 500 OD1 ASP B 13 HG SER B 16 1.38
REMARK 500 HG1 THR A 2 OE1 GLU B 40 1.38
REMARK 500 HG1 THR B 92 OXT LYS B 95 1.41
REMARK 500 HH TYR A 18 OE2 GLU A 40 1.43
REMARK 500 HG SER A 24 OE1 GLN A 68 1.49
REMARK 500 O GLU A 40 HG1 THR B 2 1.51
REMARK 500 O PHE A 15 HG SER A 19 1.53
REMARK 500 O ALA A 80 HG SER A 83 1.55
REMARK 500 O ILE A 12 HG SER A 16 1.56
REMARK 500 O GLY A 20 HG SER A 21 1.56
REMARK 500 O GLY B 20 HG SER B 21 1.57
REMARK 500 HH TYR A 88 O GLU A 90 1.57
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 ILE B 11 CA - CB - CG1 ANGL. DEV. = 11.7 DEGREES
REMARK 500 1 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 1 LYS B 91 CB - CA - C ANGL. DEV. = 12.6 DEGREES
REMARK 500 2 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 3 PRO B 42 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 4 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 4 TYR B 18 C - N - CA ANGL. DEV. = 16.0 DEGREES
REMARK 500 4 TYR B 18 N - CA - CB ANGL. DEV. = -11.0 DEGREES
REMARK 500 4 TYR B 18 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 4 LYS B 51 C - N - CA ANGL. DEV. = 15.7 DEGREES
REMARK 500 5 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 5 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 6 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 6 SER A 24 C - N - CA ANGL. DEV. = 15.1 DEGREES
REMARK 500 7 GLN A 26 O - C - N ANGL. DEV. = -10.7 DEGREES
REMARK 500 7 THR A 27 C - N - CA ANGL. DEV. = 18.0 DEGREES
REMARK 500 7 GLN B 26 O - C - N ANGL. DEV. = -9.6 DEGREES
REMARK 500 7 THR B 27 C - N - CA ANGL. DEV. = 20.4 DEGREES
REMARK 500 7 LYS B 91 C - N - CA ANGL. DEV. = 15.0 DEGREES
REMARK 500 7 GLY B 93 C - N - CA ANGL. DEV. = 13.2 DEGREES
REMARK 500 8 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 8 THR B 27 C - N - CA ANGL. DEV. = 17.3 DEGREES
REMARK 500 9 THR A 27 C - N - CA ANGL. DEV. = 16.0 DEGREES
REMARK 500 9 THR B 27 C - N - CA ANGL. DEV. = 16.5 DEGREES
REMARK 500 10 GLN A 26 O - C - N ANGL. DEV. = -9.9 DEGREES
REMARK 500 10 THR A 27 C - N - CA ANGL. DEV. = 18.4 DEGREES
REMARK 500 10 THR B 27 C - N - CA ANGL. DEV. = 17.1 DEGREES
REMARK 500 11 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 11 TYR B 88 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 12 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 12 THR A 25 C - N - CA ANGL. DEV. = 15.7 DEGREES
REMARK 500 13 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 13 ARG A 17 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 13 SER A 24 C - N - CA ANGL. DEV. = 17.0 DEGREES
REMARK 500 13 LEU A 94 C - N - CA ANGL. DEV. = 15.1 DEGREES
REMARK 500 13 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 13 ARG B 17 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 13 THR B 92 CA - CB - CG2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 14 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 14 SER A 24 C - N - CA ANGL. DEV. = 18.8 DEGREES
REMARK 500 14 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 14 ARG B 17 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 14 THR B 27 C - N - CA ANGL. DEV. = 16.6 DEGREES
REMARK 500 15 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 15 ARG B 17 CD - NE - CZ ANGL. DEV. = 11.1 DEGREES
REMARK 500 15 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 15 ARG B 17 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 16 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 16 ARG B 17 CD - NE - CZ ANGL. DEV. = 10.2 DEGREES
REMARK 500 16 ARG B 17 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 51 ANGLE DEVIATIONS.
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 THR A 2 -170.02 -69.27
REMARK 500 1 SER A 21 -66.03 131.26
REMARK 500 1 SER A 24 -20.86 179.62
REMARK 500 1 THR A 25 172.95 95.20
REMARK 500 1 LEU A 33 -39.81 -35.74
REMARK 500 1 PRO A 42 144.48 -39.94
REMARK 500 1 LYS A 49 -57.74 179.78
REMARK 500 1 ASP A 50 44.69 -7.13
REMARK 500 1 LYS A 51 17.61 54.89
REMARK 500 1 LEU A 58 -73.34 -93.52
REMARK 500 1 ASP A 62 -33.72 -29.25
REMARK 500 1 ASP A 66 -38.78 -159.64
REMARK 500 1 ALA A 67 -8.51 153.90
REMARK 500 1 TYR A 88 109.84 -178.54
REMARK 500 1 PHE A 89 -87.14 -96.25
REMARK 500 1 LYS A 91 -32.94 -133.95
REMARK 500 1 THR A 92 71.51 128.71
REMARK 500 1 ARG B 17 -62.18 -94.27
REMARK 500 1 TYR B 18 -72.89 -73.76
REMARK 500 1 SER B 19 19.98 -63.59
REMARK 500 1 SER B 21 -57.39 -167.48
REMARK 500 1 SER B 24 -15.29 -163.79
REMARK 500 1 THR B 25 -163.40 83.18
REMARK 500 1 GLN B 26 61.51 -111.97
REMARK 500 1 SER B 47 -66.22 -90.72
REMARK 500 1 LYS B 49 -75.01 -170.54
REMARK 500 1 LYS B 51 -0.21 42.59
REMARK 500 1 LEU B 58 -67.27 -104.84
REMARK 500 1 ASP B 62 -14.72 -43.84
REMARK 500 1 ASP B 66 -5.75 52.73
REMARK 500 1 ALA B 67 -4.27 -177.35
REMARK 500 1 SER B 72 3.28 -65.18
REMARK 500 1 GLU B 73 -50.99 -120.27
REMARK 500 1 HIS B 86 -80.38 -19.49
REMARK 500 1 LYS B 87 -36.98 68.72
REMARK 500 1 TYR B 88 -27.41 -148.63
REMARK 500 1 PHE B 89 -119.63 -153.46
REMARK 500 1 LYS B 91 -101.21 -124.83
REMARK 500 2 SER A 21 -50.55 69.54
REMARK 500 2 SER A 24 -0.18 -149.15
REMARK 500 2 THR A 25 -161.16 81.65
REMARK 500 2 GLN A 26 49.15 -104.40
REMARK 500 2 PRO A 42 154.15 -39.43
REMARK 500 2 LYS A 49 -118.72 172.12
REMARK 500 2 LYS A 51 -6.09 49.54
REMARK 500 2 VAL A 54 -61.53 62.34
REMARK 500 2 ASP A 62 -35.45 -28.74
REMARK 500 2 ASP A 66 -62.94 -147.04
REMARK 500 2 ALA A 67 -50.81 144.47
REMARK 500 2 GLN A 68 97.26 -61.57
REMARK 500
REMARK 500 THIS ENTRY HAS 573 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 24 THR A 25 1 -112.40
REMARK 500 LEU A 28 THR A 29 1 149.50
REMARK 500 SER B 19 GLY B 20 1 -149.79
REMARK 500 SER B 24 THR B 25 1 -102.29
REMARK 500 LEU B 28 THR B 29 1 149.25
REMARK 500 TYR A 18 SER A 19 2 148.39
REMARK 500 SER A 24 THR A 25 2 -117.76
REMARK 500 SER B 19 GLY B 20 2 138.65
REMARK 500 LEU B 28 THR B 29 2 143.55
REMARK 500 PHE B 89 GLU B 90 2 130.40
REMARK 500 SER A 24 THR A 25 3 -142.49
REMARK 500 GLN A 26 THR A 27 3 -148.66
REMARK 500 SER B 24 THR B 25 3 148.67
REMARK 500 TYR A 18 SER A 19 4 148.56
REMARK 500 SER A 24 THR A 25 4 -110.51
REMARK 500 GLU A 38 LYS A 39 4 -148.68
REMARK 500 PHE A 89 GLU A 90 4 -140.24
REMARK 500 ILE B 11 ILE B 12 4 145.59
REMARK 500 ASP B 13 VAL B 14 4 147.72
REMARK 500 SER B 24 THR B 25 4 -146.41
REMARK 500 PHE B 89 GLU B 90 4 147.52
REMARK 500 SER A 24 THR A 25 5 -111.17
REMARK 500 SER B 19 GLY B 20 5 -149.87
REMARK 500 SER B 21 GLU B 22 5 147.83
REMARK 500 LEU B 28 THR B 29 5 148.71
REMARK 500 LYS B 87 TYR B 88 5 -148.23
REMARK 500 PHE B 89 GLU B 90 5 -134.34
REMARK 500 SER A 24 THR A 25 6 123.10
REMARK 500 GLN A 26 THR A 27 6 141.90
REMARK 500 LYS A 49 ASP A 50 6 -144.97
REMARK 500 PHE A 89 GLU A 90 6 144.10
REMARK 500 LYS A 91 THR A 92 6 130.53
REMARK 500 SER B 19 GLY B 20 6 142.18
REMARK 500 GLY B 20 SER B 21 6 149.05
REMARK 500 GLU B 22 GLY B 23 6 142.88
REMARK 500 SER B 24 THR B 25 6 144.00
REMARK 500 GLN B 26 THR B 27 6 143.67
REMARK 500 ASP B 50 LYS B 51 6 -146.95
REMARK 500 SER A 24 THR A 25 7 111.83
REMARK 500 GLN A 26 THR A 27 7 60.43
REMARK 500 LEU A 28 THR A 29 7 145.17
REMARK 500 GLU A 38 LYS A 39 7 -146.72
REMARK 500 GLY A 48 LYS A 49 7 149.62
REMARK 500 ASP A 52 ALA A 53 7 143.96
REMARK 500 SER B 24 THR B 25 7 118.31
REMARK 500 LEU B 28 THR B 29 7 139.63
REMARK 500 GLU B 38 LYS B 39 7 -149.63
REMARK 500 GLU B 90 LYS B 91 7 -148.90
REMARK 500 GLY A 23 SER A 24 8 -134.54
REMARK 500 GLN A 26 THR A 27 8 37.20
REMARK 500
REMARK 500 THIS ENTRY HAS 117 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 2 TYR B 18 0.08 SIDE CHAIN
REMARK 500 3 TYR A 88 0.10 SIDE CHAIN
REMARK 500 4 ARG B 17 0.11 SIDE CHAIN
REMARK 500 4 TYR B 18 0.14 SIDE CHAIN
REMARK 500 4 PHE B 44 0.08 SIDE CHAIN
REMARK 500 5 ARG B 17 0.17 SIDE CHAIN
REMARK 500 7 TYR A 88 0.07 SIDE CHAIN
REMARK 500 7 ARG B 17 0.26 SIDE CHAIN
REMARK 500 8 TYR A 18 0.08 SIDE CHAIN
REMARK 500 8 TYR A 88 0.08 SIDE CHAIN
REMARK 500 8 ARG B 17 0.12 SIDE CHAIN
REMARK 500 9 TYR B 88 0.08 SIDE CHAIN
REMARK 500 11 ARG B 17 0.10 SIDE CHAIN
REMARK 500 12 ARG A 17 0.09 SIDE CHAIN
REMARK 500 13 ARG A 17 0.11 SIDE CHAIN
REMARK 500 13 ASP A 62 0.07 SIDE CHAIN
REMARK 500 13 TYR A 88 0.14 SIDE CHAIN
REMARK 500 14 ARG B 17 0.19 SIDE CHAIN
REMARK 500 15 ARG A 17 0.08 SIDE CHAIN
REMARK 500 15 TYR A 18 0.09 SIDE CHAIN
REMARK 500 16 TYR A 88 0.09 SIDE CHAIN
REMARK 500 16 TYR B 88 0.09 SIDE CHAIN
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 7 GLN A 26 10.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J55 RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF CA+-BOUND HUMAN S100P
DBREF 1OZO A 1 95 UNP P25815 S100P_HUMAN 1 95
DBREF 1OZO B 1 95 UNP P25815 S100P_HUMAN 1 95
SEQADV 1OZO ALA A 6 UNP P25815 THR 6 CONFLICT
SEQADV 1OZO SER A 85 UNP P25815 CYS 85 CONFLICT
SEQADV 1OZO THR A 92 UNP P25815 ALA 92 CONFLICT
SEQADV 1OZO ALA B 6 UNP P25815 THR 6 CONFLICT
SEQADV 1OZO SER B 85 UNP P25815 CYS 85 CONFLICT
SEQADV 1OZO THR B 92 UNP P25815 ALA 92 CONFLICT
SEQRES 1 A 95 MET THR GLU LEU GLU ALA ALA MET GLY MET ILE ILE ASP
SEQRES 2 A 95 VAL PHE SER ARG TYR SER GLY SER GLU GLY SER THR GLN
SEQRES 3 A 95 THR LEU THR LYS GLY GLU LEU LYS VAL LEU MET GLU LYS
SEQRES 4 A 95 GLU LEU PRO GLY PHE LEU GLN SER GLY LYS ASP LYS ASP
SEQRES 5 A 95 ALA VAL ASP LYS LEU LEU LYS ASP LEU ASP ALA ASN GLY
SEQRES 6 A 95 ASP ALA GLN VAL ASP PHE SER GLU PHE ILE VAL PHE VAL
SEQRES 7 A 95 ALA ALA ILE THR SER ALA SER HIS LYS TYR PHE GLU LYS
SEQRES 8 A 95 THR GLY LEU LYS
SEQRES 1 B 95 MET THR GLU LEU GLU ALA ALA MET GLY MET ILE ILE ASP
SEQRES 2 B 95 VAL PHE SER ARG TYR SER GLY SER GLU GLY SER THR GLN
SEQRES 3 B 95 THR LEU THR LYS GLY GLU LEU LYS VAL LEU MET GLU LYS
SEQRES 4 B 95 GLU LEU PRO GLY PHE LEU GLN SER GLY LYS ASP LYS ASP
SEQRES 5 B 95 ALA VAL ASP LYS LEU LEU LYS ASP LEU ASP ALA ASN GLY
SEQRES 6 B 95 ASP ALA GLN VAL ASP PHE SER GLU PHE ILE VAL PHE VAL
SEQRES 7 B 95 ALA ALA ILE THR SER ALA SER HIS LYS TYR PHE GLU LYS
SEQRES 8 B 95 THR GLY LEU LYS
HELIX 1 1 THR A 2 SER A 19 1 18
HELIX 2 2 LYS A 30 LEU A 41 1 12
HELIX 3 3 GLY A 43 SER A 47 5 5
HELIX 4 4 ASP A 55 ALA A 63 1 9
HELIX 5 5 PHE A 71 HIS A 86 1 16
HELIX 6 6 THR B 2 TYR B 18 1 17
HELIX 7 7 LYS B 30 LYS B 34 1 5
HELIX 8 8 LEU B 36 LEU B 41 1 6
HELIX 9 9 GLY B 43 SER B 47 5 5
HELIX 10 10 ASP B 55 ASP B 60 1 6
HELIX 11 11 LEU B 61 GLY B 65 5 5
HELIX 12 12 ASP B 70 HIS B 86 1 17
SHEET 1 A 2 THR A 27 THR A 29 0
SHEET 2 A 2 GLN A 68 ASP A 70 -1 O VAL A 69 N LEU A 28
SHEET 1 B 2 LEU B 28 THR B 29 0
SHEET 2 B 2 GLN B 68 VAL B 69 -1 O VAL B 69 N LEU B 28
CISPEP 1 GLN B 26 THR B 27 7 18.74
CISPEP 2 GLN B 26 THR B 27 8 -7.12
CISPEP 3 GLN A 26 THR A 27 9 17.57
CISPEP 4 GLN B 26 THR B 27 9 3.29
CISPEP 5 GLN A 26 THR A 27 10 15.05
CISPEP 6 GLN B 26 THR B 27 10 21.11
CISPEP 7 GLN B 26 THR B 27 14 7.28
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
Complete list - b 23 2 Bytes