Header list of 1h4b.pdb file
Complete list - r 25 2 Bytes
HEADER ALLERGEN 26-FEB-03 1H4B
TITLE SOLUTION STRUCTURE OF THE BIRCH POLLEN ALLERGEN BET V 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLCALCIN BET V 4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CALCIUM-BINDING POLLEN ALLERGEN BET V 4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BETULA VERRUCOSA;
SOURCE 3 ORGANISM_COMMON: WHITE BIRCH;
SOURCE 4 ORGANISM_TAXID: 3505;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMW175
KEYWDS ALLERGEN, BIRCH POLLEN ALLERGEN, CALCIUM-BINDING POLCALCIN,
KEYWDS 2 HETERONUCLEAR NMR, STRUCTURE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR P.NEUDECKER,J.NERKAMP,A.EISENMANN,T.LAUBER,K.LEHMANN,
AUTHOR 2 K.SCHWEIMER,P.ROESCH
REVDAT 5 24-FEB-09 1H4B 1 VERSN
REVDAT 4 18-MAR-04 1H4B 1 ATOM
REVDAT 3 10-MAR-04 1H4B 1 ATOM
REVDAT 2 04-MAR-04 1H4B 1 JRNL
REVDAT 1 26-FEB-04 1H4B 0
JRNL AUTH P.NEUDECKER,J.NERKAMP,A.EISENMANN,A.NOURSE,
JRNL AUTH 2 T.LAUBER,K.SCHWEIMER,K.LEHMANN,S.SCHWARZINGER,
JRNL AUTH 3 F.FERREIRA,P.ROESCH
JRNL TITL SOLUTION STRUCTURE, DYNAMICS, AND HYDRODYNAMICS OF
JRNL TITL 2 THE CALCIUM-BOUND CROSS-REACTIVE BIRCH POLLEN
JRNL TITL 3 ALLERGEN BET V 4 REVEAL A CANONICAL MONOMERIC TWO
JRNL TITL 4 EF-HAND ASSEMBLY WITH A REGULATORY FUNCTION
JRNL REF J.MOL.BIOL. V. 336 1141 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15037075
JRNL DOI 10.1016/J.JMB.2003.12.070
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851 NIH 1.2.1
REMARK 3 AUTHORS : BRUNGER, CLORE, KUSZEWSKI, SCHWIETERS, TJ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H4B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-FEB-03.
REMARK 100 THE PDBE ID CODE IS EBI-12240.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 45 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-TOCSY,2D-NOESY,
REMARK 210 1H,15N-HSQC,1H,15N-IPAP,
REMARK 210 HNHA,3D-1H,15N-TOCSY-HSQC,
REMARK 210 3D-1H,15N/1H,15N-
REMARK 210 HMQC-NOESY-HSQC,
REMARK 210 3D-1H,13C/1H,15N-
REMARK 210 HMQC-NOESY-HSQC,
REMARK 210 13C-CTHSQC, HNCO,
REMARK 210 LONG-RANGE H(N)CO,
REMARK 210 C(CO)NH, HNCA,
REMARK 210 H(C)CH-COSY, (H)CCH-COSY,
REMARK 210 3D-1H,13C-NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600; 750
REMARK 210 SPECTROMETER MODEL : DRX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NDEE, NMRVIEW 5.0.4,
REMARK 210 X-PLOR 3.851 NIH 1.2.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 90
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 LYS A 8 - H GLU A 12 1.56
REMARK 500 O ALA A 28 - H GLY A 32 1.55
REMARK 500 O MET A 50 - H ASP A 54 1.52
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 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 A 19 103.08 -57.75
REMARK 500 1 SER A 40 52.37 -153.76
REMARK 500 1 ASN A 73 54.95 -149.38
REMARK 500 2 ASP A 3 179.59 -51.08
REMARK 500 2 ASP A 19 103.66 -55.71
REMARK 500 2 SER A 40 51.78 -155.63
REMARK 500 2 ASP A 54 101.31 -58.62
REMARK 500 2 ASN A 73 51.46 -148.03
REMARK 500 3 ASP A 19 103.37 -58.64
REMARK 500 3 SER A 40 57.40 -155.49
REMARK 500 3 ASP A 54 101.52 -59.51
REMARK 500 3 ASN A 73 56.06 -152.10
REMARK 500 4 SER A 40 58.62 -156.07
REMARK 500 4 ASN A 73 56.43 -152.24
REMARK 500 5 ASP A 19 103.48 -56.48
REMARK 500 5 SER A 40 66.45 -155.25
REMARK 500 5 ASP A 54 101.23 -59.52
REMARK 500 5 ASN A 73 58.37 -146.24
REMARK 500 6 ASP A 19 103.28 -59.22
REMARK 500 6 SER A 40 64.64 -154.72
REMARK 500 6 ASN A 73 55.28 -148.33
REMARK 500 7 SER A 40 51.35 -156.54
REMARK 500 7 ASP A 54 101.37 -59.11
REMARK 500 7 ASN A 73 57.01 -150.58
REMARK 500 8 ASP A 19 103.52 -57.88
REMARK 500 8 SER A 40 55.63 -154.75
REMARK 500 8 ASP A 54 101.41 -59.74
REMARK 500 8 ASN A 73 56.73 -149.70
REMARK 500 9 SER A 40 67.69 -155.74
REMARK 500 9 ASP A 54 100.69 -58.40
REMARK 500 9 ASN A 73 58.69 -150.24
REMARK 500 10 ASP A 19 103.66 -59.18
REMARK 500 10 SER A 40 60.58 -153.82
REMARK 500 10 ASN A 73 48.42 -151.69
REMARK 500 11 SER A 40 56.63 -155.18
REMARK 500 11 ASN A 73 58.17 -148.83
REMARK 500 12 ASP A 19 103.48 -57.36
REMARK 500 12 SER A 40 65.04 -155.76
REMARK 500 12 ASN A 73 57.68 -145.22
REMARK 500 13 ASP A 19 103.33 -54.66
REMARK 500 13 SER A 40 61.57 -155.44
REMARK 500 13 ASP A 54 101.47 -59.97
REMARK 500 13 ASN A 73 53.29 -145.94
REMARK 500 14 ASP A 19 103.43 -57.58
REMARK 500 14 SER A 40 52.53 -155.15
REMARK 500 14 ASN A 73 46.31 -150.00
REMARK 500 15 ASP A 19 103.11 -56.02
REMARK 500 15 SER A 40 52.23 -116.79
REMARK 500 16 ASP A 19 103.51 -56.12
REMARK 500 16 SER A 40 50.77 -154.30
REMARK 500 16 ASP A 54 101.52 -58.77
REMARK 500 16 ASN A 73 46.88 -149.22
REMARK 500 17 SER A 40 49.15 -156.07
REMARK 500 17 ASP A 54 101.35 -59.67
REMARK 500 18 SER A 40 49.60 -155.50
REMARK 500 18 ASN A 73 59.83 -144.49
REMARK 500 19 ASP A 19 103.46 -59.79
REMARK 500 19 SER A 40 55.15 -155.24
REMARK 500 19 ASN A 73 55.23 -145.81
REMARK 500 20 ASP A 19 103.56 -58.65
REMARK 500 20 SER A 40 56.41 -155.99
REMARK 500 20 ASN A 73 56.74 -149.93
REMARK 500 21 ASP A 19 103.14 -54.08
REMARK 500 21 SER A 40 57.48 -156.15
REMARK 500 21 ASP A 54 101.63 -59.19
REMARK 500 21 ASN A 73 55.89 -152.12
REMARK 500 22 ASP A 19 103.43 -55.32
REMARK 500 22 SER A 40 59.77 -152.00
REMARK 500 22 ASN A 73 58.30 -140.48
REMARK 500 23 ASP A 19 103.36 -59.09
REMARK 500 23 SER A 40 58.67 -154.58
REMARK 500 23 ASN A 73 56.74 -144.40
REMARK 500 24 ASP A 19 103.09 -58.74
REMARK 500 24 SER A 40 50.02 -155.33
REMARK 500 24 ASP A 54 101.69 -59.82
REMARK 500 24 ASN A 73 54.98 -149.56
REMARK 500 25 ASP A 19 103.05 -55.47
REMARK 500 25 SER A 40 56.20 -155.09
REMARK 500 25 ASN A 73 58.54 -150.11
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 11 0.19 SIDE CHAIN
REMARK 500 1 ARG A 13 0.25 SIDE CHAIN
REMARK 500 1 ARG A 17 0.32 SIDE CHAIN
REMARK 500 1 ARG A 71 0.28 SIDE CHAIN
REMARK 500 1 ARG A 74 0.14 SIDE CHAIN
REMARK 500 2 ARG A 11 0.18 SIDE CHAIN
REMARK 500 2 ARG A 13 0.29 SIDE CHAIN
REMARK 500 2 ARG A 17 0.30 SIDE CHAIN
REMARK 500 2 ARG A 71 0.30 SIDE CHAIN
REMARK 500 2 ARG A 74 0.30 SIDE CHAIN
REMARK 500 3 ARG A 11 0.30 SIDE CHAIN
REMARK 500 3 ARG A 13 0.31 SIDE CHAIN
REMARK 500 3 ARG A 17 0.23 SIDE CHAIN
REMARK 500 3 ARG A 71 0.32 SIDE CHAIN
REMARK 500 4 ARG A 11 0.19 SIDE CHAIN
REMARK 500 4 ARG A 17 0.32 SIDE CHAIN
REMARK 500 4 ARG A 74 0.23 SIDE CHAIN
REMARK 500 5 ARG A 11 0.22 SIDE CHAIN
REMARK 500 5 ARG A 13 0.20 SIDE CHAIN
REMARK 500 5 ARG A 17 0.29 SIDE CHAIN
REMARK 500 5 ARG A 71 0.15 SIDE CHAIN
REMARK 500 5 ARG A 74 0.32 SIDE CHAIN
REMARK 500 6 ARG A 11 0.11 SIDE CHAIN
REMARK 500 6 ARG A 17 0.22 SIDE CHAIN
REMARK 500 6 ARG A 71 0.08 SIDE CHAIN
REMARK 500 6 ARG A 74 0.24 SIDE CHAIN
REMARK 500 7 ARG A 11 0.25 SIDE CHAIN
REMARK 500 7 ARG A 13 0.31 SIDE CHAIN
REMARK 500 7 ARG A 17 0.15 SIDE CHAIN
REMARK 500 7 ARG A 71 0.28 SIDE CHAIN
REMARK 500 7 ARG A 74 0.29 SIDE CHAIN
REMARK 500 8 ARG A 11 0.28 SIDE CHAIN
REMARK 500 8 ARG A 13 0.22 SIDE CHAIN
REMARK 500 8 ARG A 17 0.22 SIDE CHAIN
REMARK 500 8 ARG A 74 0.29 SIDE CHAIN
REMARK 500 9 ARG A 11 0.23 SIDE CHAIN
REMARK 500 9 ARG A 13 0.28 SIDE CHAIN
REMARK 500 9 ARG A 17 0.22 SIDE CHAIN
REMARK 500 9 ARG A 71 0.32 SIDE CHAIN
REMARK 500 9 ARG A 74 0.20 SIDE CHAIN
REMARK 500 10 ARG A 11 0.31 SIDE CHAIN
REMARK 500 10 ARG A 13 0.32 SIDE CHAIN
REMARK 500 10 ARG A 17 0.23 SIDE CHAIN
REMARK 500 10 ARG A 71 0.09 SIDE CHAIN
REMARK 500 10 ARG A 74 0.30 SIDE CHAIN
REMARK 500 11 ARG A 11 0.31 SIDE CHAIN
REMARK 500 11 ARG A 13 0.25 SIDE CHAIN
REMARK 500 11 ARG A 17 0.28 SIDE CHAIN
REMARK 500 11 ARG A 74 0.12 SIDE CHAIN
REMARK 500 12 ARG A 11 0.32 SIDE CHAIN
REMARK 500 12 ARG A 13 0.25 SIDE CHAIN
REMARK 500 12 ARG A 17 0.30 SIDE CHAIN
REMARK 500 12 ARG A 71 0.23 SIDE CHAIN
REMARK 500 12 ARG A 74 0.27 SIDE CHAIN
REMARK 500 13 ARG A 13 0.29 SIDE CHAIN
REMARK 500 13 ARG A 17 0.19 SIDE CHAIN
REMARK 500 13 ARG A 71 0.16 SIDE CHAIN
REMARK 500 13 ARG A 74 0.21 SIDE CHAIN
REMARK 500 14 ARG A 11 0.30 SIDE CHAIN
REMARK 500 14 ARG A 13 0.15 SIDE CHAIN
REMARK 500 14 ARG A 17 0.29 SIDE CHAIN
REMARK 500 14 ARG A 71 0.29 SIDE CHAIN
REMARK 500 14 ARG A 74 0.20 SIDE CHAIN
REMARK 500 15 ARG A 11 0.18 SIDE CHAIN
REMARK 500 15 ARG A 13 0.17 SIDE CHAIN
REMARK 500 15 ARG A 17 0.24 SIDE CHAIN
REMARK 500 15 ARG A 71 0.23 SIDE CHAIN
REMARK 500 15 ARG A 74 0.15 SIDE CHAIN
REMARK 500 16 ARG A 11 0.31 SIDE CHAIN
REMARK 500 16 ARG A 13 0.26 SIDE CHAIN
REMARK 500 16 ARG A 17 0.25 SIDE CHAIN
REMARK 500 16 ARG A 71 0.30 SIDE CHAIN
REMARK 500 16 ARG A 74 0.17 SIDE CHAIN
REMARK 500 17 ARG A 11 0.31 SIDE CHAIN
REMARK 500 17 ARG A 13 0.31 SIDE CHAIN
REMARK 500 17 ARG A 17 0.28 SIDE CHAIN
REMARK 500 17 ARG A 74 0.11 SIDE CHAIN
REMARK 500 18 ARG A 11 0.31 SIDE CHAIN
REMARK 500 18 ARG A 13 0.24 SIDE CHAIN
REMARK 500 18 ARG A 17 0.32 SIDE CHAIN
REMARK 500 18 ARG A 71 0.21 SIDE CHAIN
REMARK 500 19 ARG A 13 0.31 SIDE CHAIN
REMARK 500 19 ARG A 17 0.31 SIDE CHAIN
REMARK 500 19 ARG A 71 0.12 SIDE CHAIN
REMARK 500 19 ARG A 74 0.26 SIDE CHAIN
REMARK 500 20 ARG A 11 0.19 SIDE CHAIN
REMARK 500 20 ARG A 13 0.26 SIDE CHAIN
REMARK 500 20 ARG A 17 0.23 SIDE CHAIN
REMARK 500 20 ARG A 71 0.23 SIDE CHAIN
REMARK 500 20 ARG A 74 0.24 SIDE CHAIN
REMARK 500 21 ARG A 11 0.30 SIDE CHAIN
REMARK 500 21 ARG A 13 0.27 SIDE CHAIN
REMARK 500 21 ARG A 17 0.15 SIDE CHAIN
REMARK 500 21 ARG A 71 0.32 SIDE CHAIN
REMARK 500 21 ARG A 74 0.17 SIDE CHAIN
REMARK 500 22 ARG A 11 0.19 SIDE CHAIN
REMARK 500 22 ARG A 13 0.29 SIDE CHAIN
REMARK 500 22 ARG A 17 0.16 SIDE CHAIN
REMARK 500 22 ARG A 71 0.24 SIDE CHAIN
REMARK 500 22 ARG A 74 0.31 SIDE CHAIN
REMARK 500 23 ARG A 11 0.18 SIDE CHAIN
REMARK 500 23 ARG A 13 0.08 SIDE CHAIN
REMARK 500 23 ARG A 17 0.31 SIDE CHAIN
REMARK 500 23 ARG A 71 0.32 SIDE CHAIN
REMARK 500 23 ARG A 74 0.28 SIDE CHAIN
REMARK 500 24 ARG A 11 0.31 SIDE CHAIN
REMARK 500 24 ARG A 17 0.18 SIDE CHAIN
REMARK 500 24 ARG A 71 0.20 SIDE CHAIN
REMARK 500 24 ARG A 74 0.26 SIDE CHAIN
REMARK 500 25 ARG A 11 0.29 SIDE CHAIN
REMARK 500 25 ARG A 13 0.12 SIDE CHAIN
REMARK 500 25 ARG A 17 0.26 SIDE CHAIN
REMARK 500 25 ARG A 71 0.13 SIDE CHAIN
REMARK 500 25 ARG A 74 0.11 SIDE CHAIN
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 A1085 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 30 OE1
REMARK 620 2 GLU A 30 OE2 51.4
REMARK 620 3 ASN A 21 OD1 126.8 76.0
REMARK 620 4 LYS A 25 O 77.9 125.9 153.9
REMARK 620 5 ASP A 19 OD1 106.7 94.0 81.7 82.6
REMARK 620 6 ASP A 23 OD1 153.0 154.2 78.3 79.6 84.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1086 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 54 OD1
REMARK 620 2 PHE A 60 O 82.8
REMARK 620 3 GLU A 65 OE2 94.0 126.3
REMARK 620 4 ASP A 56 OD1 81.9 153.8 76.0
REMARK 620 5 ASP A 58 OD1 84.8 79.5 154.0 78.1
REMARK 620 6 GLU A 65 OE1 106.7 78.3 51.3 126.7 153.3
REMARK 620 N 1 2 3 4 5
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1085
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1086
DBREF 1H4B A 1 84 UNP Q39419 POC4_BETVE 2 85
SEQRES 1 A 84 ALA ASP ASP HIS PRO GLN ASP LYS ALA GLU ARG GLU ARG
SEQRES 2 A 84 ILE PHE LYS ARG PHE ASP ALA ASN GLY ASP GLY LYS ILE
SEQRES 3 A 84 SER ALA ALA GLU LEU GLY GLU ALA LEU LYS THR LEU GLY
SEQRES 4 A 84 SER ILE THR PRO ASP GLU VAL LYS HIS MET MET ALA GLU
SEQRES 5 A 84 ILE ASP THR ASP GLY ASP GLY PHE ILE SER PHE GLN GLU
SEQRES 6 A 84 PHE THR ASP PHE GLY ARG ALA ASN ARG GLY LEU LEU LYS
SEQRES 7 A 84 ASP VAL ALA LYS ILE PHE
HET CA A1085 1
HET CA A1086 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
HELIX 1 1 PRO A 5 PHE A 18 1 14
HELIX 2 2 ALA A 28 LEU A 35 1 8
HELIX 3 3 LYS A 36 LEU A 38 5 3
HELIX 4 4 PRO A 43 ILE A 53 1 11
HELIX 5 5 PHE A 63 ALA A 72 1 10
HELIX 6 6 ARG A 74 PHE A 84 1 11
SHEET 1 AA 2 LYS A 25 SER A 27 0
SHEET 2 AA 2 PHE A 60 SER A 62 -1 O ILE A 61 N ILE A 26
LINK CA CA A1085 OE1 GLU A 30 1555 1555 2.46
LINK CA CA A1085 OE2 GLU A 30 1555 1555 2.46
LINK CA CA A1085 OD1 ASN A 21 1555 1555 2.37
LINK CA CA A1085 O LYS A 25 1555 1555 2.11
LINK CA CA A1085 OD1 ASP A 19 1555 1555 2.32
LINK CA CA A1085 OD1 ASP A 23 1555 1555 2.27
LINK CA CA A1086 O PHE A 60 1555 1555 2.12
LINK CA CA A1086 OE2 GLU A 65 1555 1555 2.46
LINK CA CA A1086 OD1 ASP A 56 1555 1555 2.37
LINK CA CA A1086 OD1 ASP A 58 1555 1555 2.27
LINK CA CA A1086 OE1 GLU A 65 1555 1555 2.46
LINK CA CA A1086 OD1 ASP A 54 1555 1555 2.32
SITE 1 AC1 5 ASP A 19 ASN A 21 ASP A 23 LYS A 25
SITE 2 AC1 5 GLU A 30
SITE 1 AC2 5 ASP A 54 ASP A 56 ASP A 58 PHE A 60
SITE 2 AC2 5 GLU A 65
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 25 2 Bytes