Header list of 1zpx.pdb file
Complete list - 2 20 Bytes
HEADER STRUCTURAL PROTEIN 18-MAY-05 1ZPX
TITLE NMR STRUCTURE OF MCOL1-[13-33] FROM HYDRA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MINI-COLLAGEN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HYDRA SP.
KEYWDS CYSTEINE-RICH PEPTIDE, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR A.G.MILBRADT,C.BOULEGUE,L.MORODER,C.RENNER
REVDAT 4 02-MAR-22 1ZPX 1 REMARK LINK
REVDAT 3 24-FEB-09 1ZPX 1 VERSN
REVDAT 2 06-DEC-05 1ZPX 1 JRNL
REVDAT 1 15-NOV-05 1ZPX 0
JRNL AUTH A.G.MILBRADT,C.BOULEGUE,L.MORODER,C.RENNER
JRNL TITL THE TWO CYSTEINE-RICH HEAD DOMAINS OF MINICOLLAGEN FROM
JRNL TITL 2 HYDRA NEMATOCYSTS DIFFER IN THEIR CYSTINE FRAMEWORK AND
JRNL TITL 3 OVERALL FOLD DESPITE AN IDENTICAL CYSTEINE SEQUENCE PATTERN.
JRNL REF J.MOL.BIOL. V. 354 591 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16257007
JRNL DOI 10.1016/J.JMB.2005.09.080
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.POKIDYSHEVA,A.G.MILBRADT,S.MEIER,C.RENNER,D.HAUSSINGER,
REMARK 1 AUTH 2 H.P.BACHINGER,L.MORODER,S.GRZESIEK,T.W.HOLSTEIN,S.OZBEK,
REMARK 1 AUTH 3 J.ENGEL
REMARK 1 TITL THE STRUCTURE OF THE CYS-RICH TERMINAL DOMAIN OF HYDRA
REMARK 1 TITL 2 MINICOLLAGEN, WHICH IS INVOLVED IN DISULFIDE NETWORKS OF THE
REMARK 1 TITL 3 NEMATOCYST WALL.
REMARK 1 REF J.BIOL.CHEM. V. 279 30395 2004
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3, DISCOVER 2.98
REMARK 3 AUTHORS : BRUKER (XWINNMR), ACCELRYS (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZPX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000033004.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283; 293; 303
REMARK 210 PH : 3.8; 3.8; 3.8
REMARK 210 IONIC STRENGTH : NULL; NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM MINICOLLAGEN [13-33] PH
REMARK 210 3.8; 2 MM MINICOLLAGEN [13-33]
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DGII 98.0, DISCOVER 2.98
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: 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 5 CYS A 26 CB - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 7 ALA A 23 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 10 ALA A 23 N - CA - CB ANGL. DEV. = -8.6 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 SER A 16 -33.72 -134.47
REMARK 500 1 PRO A 19 108.34 -56.91
REMARK 500 2 SER A 16 -34.17 -139.08
REMARK 500 2 SER A 20 20.57 -79.13
REMARK 500 2 PRO A 28 -16.79 -45.89
REMARK 500 3 PRO A 19 102.80 -51.62
REMARK 500 3 CYS A 22 4.69 -68.07
REMARK 500 3 PRO A 28 -13.69 -45.68
REMARK 500 4 PRO A 19 108.79 -52.39
REMARK 500 5 PRO A 19 88.99 -57.90
REMARK 500 5 SER A 20 32.59 -85.45
REMARK 500 5 CYS A 22 8.22 -68.30
REMARK 500 5 ALA A 23 156.57 -44.44
REMARK 500 5 PRO A 28 -12.54 -48.49
REMARK 500 6 SER A 16 -50.07 -162.43
REMARK 500 6 PRO A 19 100.75 -53.34
REMARK 500 6 CYS A 22 25.04 -79.46
REMARK 500 6 PRO A 28 -31.86 -36.72
REMARK 500 7 PRO A 19 93.75 -55.35
REMARK 500 7 SER A 20 35.25 -94.10
REMARK 500 7 CYS A 22 14.13 -69.33
REMARK 500 7 ALA A 23 165.85 -41.18
REMARK 500 7 PRO A 28 2.89 -61.69
REMARK 500 8 PRO A 19 107.58 -51.81
REMARK 500 8 SER A 20 36.72 -90.97
REMARK 500 8 CYS A 26 36.74 27.24
REMARK 500 8 PRO A 28 -19.03 -45.66
REMARK 500 9 CYS A 14 -71.36 -134.67
REMARK 500 9 SER A 16 90.44 -160.07
REMARK 500 9 TYR A 17 11.69 55.01
REMARK 500 9 PRO A 19 99.91 -55.15
REMARK 500 9 CYS A 22 58.00 -108.37
REMARK 500 10 PRO A 19 99.00 -54.84
REMARK 500 10 ALA A 23 165.75 -47.58
REMARK 500 10 PRO A 28 -14.22 -46.55
REMARK 500 10 TYR A 32 73.38 51.41
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 20 VAL A 21 1 148.58
REMARK 500 CYS A 26 ALA A 27 1 -148.64
REMARK 500 CYS A 18 PRO A 19 2 144.41
REMARK 500 CYS A 26 ALA A 27 2 -146.65
REMARK 500 CYS A 18 PRO A 19 3 148.27
REMARK 500 SER A 20 VAL A 21 3 148.66
REMARK 500 CYS A 26 ALA A 27 3 -146.20
REMARK 500 CYS A 18 PRO A 19 4 148.07
REMARK 500 CYS A 26 ALA A 27 4 -144.59
REMARK 500 CYS A 18 PRO A 19 5 148.63
REMARK 500 SER A 20 VAL A 21 5 148.16
REMARK 500 CYS A 18 PRO A 19 6 148.57
REMARK 500 SER A 20 VAL A 21 6 144.48
REMARK 500 CYS A 26 ALA A 27 6 -149.75
REMARK 500 CYS A 18 PRO A 19 7 148.68
REMARK 500 SER A 20 VAL A 21 7 142.20
REMARK 500 ALA A 25 CYS A 26 8 71.01
REMARK 500 CYS A 18 PRO A 19 9 142.36
REMARK 500 CYS A 22 ALA A 23 9 145.75
REMARK 500 CYS A 26 ALA A 27 9 -146.10
REMARK 500 CYS A 18 PRO A 19 10 149.43
REMARK 500 SER A 20 VAL A 21 10 147.28
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 9 TYR A 17 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 34
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SOP RELATED DB: PDB
REMARK 900 C-TERMINAL CYSTEINE-RICH DOMAIN
REMARK 900 RELATED ID: 1SP7 RELATED DB: PDB
REMARK 900 C-TERMINAL CYSTEINE-RICH DOMAIN
DBREF 1ZPX A 13 33 UNP Q00484 Q00484_9CNID 32 52
SEQRES 1 A 23 ACE PRO CYS GLY SER TYR CYS PRO SER VAL CYS ALA PRO
SEQRES 2 A 23 ALA CYS ALA PRO VAL CYS CYS TYR PRO NH2
HET ACE A 12 6
HET NH2 A 34 3
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 1 ACE C2 H4 O
FORMUL 1 NH2 H2 N
HELIX 1 1 ALA A 27 TYR A 32 1 6
SSBOND 1 CYS A 14 CYS A 26 1555 1555 1.98
SSBOND 2 CYS A 18 CYS A 31 1555 1555 1.98
SSBOND 3 CYS A 22 CYS A 30 1555 1555 1.99
LINK C ACE A 12 N PRO A 13 1555 1555 1.37
LINK C PRO A 33 N NH2 A 34 1555 1555 1.33
CISPEP 1 ALA A 23 PRO A 24 1 10.62
CISPEP 2 ALA A 23 PRO A 24 2 9.51
CISPEP 3 ALA A 23 PRO A 24 3 7.18
CISPEP 4 ALA A 23 PRO A 24 4 8.12
CISPEP 5 ALA A 23 PRO A 24 5 11.62
CISPEP 6 ALA A 23 PRO A 24 6 6.15
CISPEP 7 CYS A 31 TYR A 32 6 11.58
CISPEP 8 ALA A 23 PRO A 24 7 7.58
CISPEP 9 ALA A 23 PRO A 24 8 3.73
CISPEP 10 ALA A 23 PRO A 24 9 8.96
CISPEP 11 ALA A 23 PRO A 24 10 7.68
SITE 1 AC2 1 PRO A 33
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 - 2 20 Bytes