Header list of 1sop.pdb file
Complete list - 2 20 Bytes
HEADER STRUCTURAL PROTEIN 15-MAR-04 1SOP
TITLE C-TERMINAL CYSTINE-RICH DOMAIN OF MINICOLLAGEN-I FROM HYDRA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MINI-COLLAGEN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL CYSTINE-RICH DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: FMOC SOLID PHASE SYNTHESIS + OXIDATION. THE SEQUENCE
SOURCE 4 IS NATURALLY FOUND IN HYDRA SP.
KEYWDS COLLAGEN OXIDATIVE REFOLDING, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR A.G.MILBRADT,L.MORODER,C.RENNER
REVDAT 4 02-MAR-22 1SOP 1 REMARK LINK
REVDAT 3 24-FEB-09 1SOP 1 VERSN
REVDAT 2 05-APR-05 1SOP 1 JRNL
REVDAT 1 27-APR-04 1SOP 0
JRNL AUTH E.POKIDYSHEVA,A.G.MILBRADT,S.MEIER,C.RENNER,D.HAUSSINGER,
JRNL AUTH 2 H.P.BACHINGER,L.MORODER,S.GRZESIEK,T.W.HOLSTEIN,S.OZBEK,
JRNL AUTH 3 J.ENGEL
JRNL TITL THE STRUCTURE OF THE CYS-RICH TERMINAL DOMAIN OF HYDRA
JRNL TITL 2 MINICOLLAGEN, WHICH IS INVOLVED IN DISULFIDE NETWORKS OF THE
JRNL TITL 3 NEMATOCYST WALL.
JRNL REF J.BIOL.CHEM. V. 279 30395 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15123641
JRNL DOI 10.1074/JBC.M403734200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, DISCOVER 2.98
REMARK 3 AUTHORS : BRUKER (XWINNMR), MSI (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 INDEPENDENT DG STRUCTURES SUBSEQUENTLY REFINED BY MDSA
REMARK 3 EXPERIMENTAL RESTRAINTS APPLIED THROUGHOUT
REMARK 4
REMARK 4 1SOP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021879.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : 10 MM
REMARK 210 PRESSURE : 1 BAR
REMARK 210 SAMPLE CONTENTS : 3 MM PEPTIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 ROESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DGII INSIGHT 2000
REMARK 210 METHOD USED : DISTANCE GEOMETRY MD REFINEMENT
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 : 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: 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: 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
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 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 6 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 7 CYS A 14 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 7 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 8 ALA A 21 N - CA - CB ANGL. DEV. = 10.1 DEGREES
REMARK 500 8 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 9 CYS A 14 CB - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 9 CYS A 14 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 9 PRO A 20 N - CA - C ANGL. DEV. = 16.8 DEGREES
REMARK 500 9 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 10 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 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 PRO A 20 -155.31 -72.65
REMARK 500 1 LYS A 22 87.08 -154.97
REMARK 500 1 ARG A 23 104.44 62.19
REMARK 500 2 PRO A 20 -167.55 -51.96
REMARK 500 2 LYS A 22 84.74 71.21
REMARK 500 2 ARG A 23 113.97 -161.87
REMARK 500 3 PRO A 20 -169.84 -49.21
REMARK 500 3 LYS A 22 121.09 83.73
REMARK 500 3 ARG A 23 104.71 82.03
REMARK 500 5 PRO A 20 -152.91 -48.65
REMARK 500 5 ALA A 21 88.62 65.90
REMARK 500 5 ARG A 23 88.37 69.70
REMARK 500 6 PRO A 20 -168.19 -50.27
REMARK 500 7 GLN A 9 77.53 -110.32
REMARK 500 7 PRO A 20 -157.23 -74.69
REMARK 500 8 GLN A 9 79.09 -111.54
REMARK 500 8 PRO A 20 -172.44 -48.01
REMARK 500 8 ALA A 21 87.13 146.62
REMARK 500 8 ARG A 23 102.63 60.29
REMARK 500 9 PRO A 20 9.79 -54.63
REMARK 500 9 LYS A 22 153.16 75.83
REMARK 500 10 GLN A 9 79.07 -113.23
REMARK 500 10 PRO A 20 -168.00 -47.04
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 PRO A 20 ALA A 21 1 149.02
REMARK 500 PRO A 20 ALA A 21 2 145.10
REMARK 500 PRO A 20 ALA A 21 4 111.21
REMARK 500 PRO A 20 ALA A 21 5 -145.64
REMARK 500 PRO A 20 ALA A 21 7 141.35
REMARK 500 PRO A 20 ALA A 21 9 -126.71
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1SOP A 1 24 UNP Q00484 Q00484_9CNID 126 149
SEQRES 1 A 26 ACE PRO CYS PRO PRO VAL CYS VAL ALA GLN CYS VAL PRO
SEQRES 2 A 26 THR CYS PRO GLN TYR CYS CYS PRO ALA LYS ARG LYS NH2
HET ACE A 0 6
HET NH2 A 25 3
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 1 ACE C2 H4 O
FORMUL 1 NH2 H2 N
SSBOND 1 CYS A 2 CYS A 18 1555 1555 1.99
SSBOND 2 CYS A 6 CYS A 14 1555 1555 1.99
SSBOND 3 CYS A 10 CYS A 19 1555 1555 2.00
LINK C ACE A 0 N PRO A 1 1555 1555 1.37
LINK C LYS A 24 N NH2 A 25 1555 1555 1.33
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