Header list of 1pbz.pdb file
Complete list - 23 20 Bytes
HEADER DE NOVO PROTEIN 15-MAY-03 1PBZ
TITLE DE NOVO DESIGNED PEPTIDE-METALLOPORPHYRIN COMPLEX, SOLUTION STRUCTURE
CAVEAT 1PBZ INCORRECT CHIRALITY AT SOME CA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DE NOVO DESIGNED CYCLIC PEPTIDE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: COMPLEXED WITH METALLOPORPHYRIN
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHESIZED BY SOLID STATE METHODS
KEYWDS PEPTIDE; METALLOPORPHYRIN; HEME; DE NOVO DESIGN, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR J.WANG,M.M.ROSENBLATT,K.S.SUSLICK
REVDAT 3 23-FEB-22 1PBZ 1 REMARK LINK
REVDAT 2 24-FEB-09 1PBZ 1 VERSN
REVDAT 1 09-DEC-03 1PBZ 0
JRNL AUTH M.M.ROSENBLATT,J.WANG,K.S.SUSLICK
JRNL TITL DE NOVO DESIGNED CYCLIC-PEPTIDE HEME COMPLEXES
JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 13140 2003
JRNL REFN ISSN 0027-8424
JRNL PMID 14595023
JRNL DOI 10.1073/PNAS.2231273100
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 98
REMARK 3 AUTHORS : ACCELRYS, INC
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PBZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019221.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 277
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 50 MM POTASSIUM PHOSPHATE, 10 MM
REMARK 210 POTASSIUM CHLORIDE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3MM CYCLIC PEPTIDE
REMARK 210 METALLOPORPHYRIN COMPLEX
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO RESTRAINT VIOLATIONS GREATER
REMARK 210 THAN 0.3 ANGSTROMS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 IONIC_STRENGTH: 50MM PRESSURE: 1 ATM SOLVENT SYSTEM: AQUEOUS THE
REMARK 210 STRUCTURE WAS DETERMINED USING 2D HOMONUCLEAR METHODS (WUTHRICH,
REMARK 210 1986)
REMARK 210 FOR RESONANCE ASSIGNMENTS GENERATION OF DISTANCE RESTRAINTS.
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 N NH2 A 18 O4 PC3 A 20 2.19
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 GLY B 16 CA - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500 2 CYS A 17 N - CA - CB ANGL. DEV. = -12.7 DEGREES
REMARK 500 2 ALA B 15 CB - CA - C ANGL. DEV. = 11.2 DEGREES
REMARK 500 7 HIS B 9 CB - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 8 CYS A 17 N - CA - CB ANGL. DEV. = -13.9 DEGREES
REMARK 500 8 ALA B 15 N - CA - CB ANGL. DEV. = -8.4 DEGREES
REMARK 500 9 HIS B 9 CB - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 9 ALA B 13 N - CA - CB ANGL. DEV. = -8.6 DEGREES
REMARK 500 10 HIS B 9 CB - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 10 ALA B 10 N - CA - CB ANGL. DEV. = -9.0 DEGREES
REMARK 500 11 CYS A 1 N - CA - CB ANGL. DEV. = -14.7 DEGREES
REMARK 500 11 ALA A 13 N - CA - CB ANGL. DEV. = -9.0 DEGREES
REMARK 500 11 CYS A 17 N - CA - CB ANGL. DEV. = -13.9 DEGREES
REMARK 500 11 HIS B 9 CB - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 11 ALA B 13 N - CA - CB ANGL. DEV. = -9.1 DEGREES
REMARK 500 11 ALA B 15 N - CA - CB ANGL. DEV. = -13.3 DEGREES
REMARK 500 13 GLY A 16 CA - C - N ANGL. DEV. = -14.2 DEGREES
REMARK 500 13 CYS B 1 N - CA - CB ANGL. DEV. = -13.9 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 ALA A 12 -73.09 -63.29
REMARK 500 1 ALA A 13 -30.44 -31.94
REMARK 500 1 GLU A 14 -70.77 -74.21
REMARK 500 1 ALA B 12 -71.89 -56.35
REMARK 500 1 ALA B 13 -9.59 -45.72
REMARK 500 1 ALA B 15 56.07 -91.53
REMARK 500 2 ALA A 12 -79.42 -60.81
REMARK 500 2 ALA A 13 -39.07 -22.29
REMARK 500 2 GLU A 14 -70.40 -80.62
REMARK 500 2 ALA B 12 -70.07 -46.22
REMARK 500 2 ALA B 15 -122.13 -85.21
REMARK 500 3 ALA A 12 -78.11 -56.99
REMARK 500 3 ALA A 13 -24.84 -35.17
REMARK 500 3 GLU A 14 -71.26 -80.48
REMARK 500 3 ALA B 13 -30.81 -33.71
REMARK 500 3 GLU B 14 -92.46 -84.38
REMARK 500 4 ALA A 12 -78.11 -56.99
REMARK 500 4 ALA A 13 -24.84 -35.17
REMARK 500 4 GLU A 14 -71.26 -80.48
REMARK 500 4 ALA B 13 -30.81 -33.71
REMARK 500 4 GLU B 14 -92.46 -84.38
REMARK 500 5 ALA A 12 -70.05 -66.25
REMARK 500 5 ALA A 13 -30.09 -33.76
REMARK 500 5 GLU A 14 -75.43 -73.44
REMARK 500 5 ALA B 12 -75.27 -52.90
REMARK 500 5 ALA B 13 0.32 -49.30
REMARK 500 5 GLU B 14 -63.17 -97.07
REMARK 500 5 ALA B 15 56.19 -100.17
REMARK 500 6 ALA A 12 -75.07 -56.89
REMARK 500 6 ALA A 13 -41.21 -24.93
REMARK 500 6 ALA B 13 -34.99 -32.39
REMARK 500 6 GLU B 14 -73.65 -69.26
REMARK 500 7 ALA A 13 -31.54 -32.37
REMARK 500 7 ALA B 12 -73.54 -49.82
REMARK 500 7 ALA B 13 -26.71 -36.88
REMARK 500 7 GLU B 14 -77.67 -79.26
REMARK 500 8 ALA A 13 -30.63 -33.83
REMARK 500 8 GLU A 14 -74.21 -74.86
REMARK 500 8 ALA B 12 -77.07 -48.91
REMARK 500 8 ALA B 13 -6.60 -47.45
REMARK 500 8 GLU B 14 -63.86 -90.13
REMARK 500 8 ALA B 15 59.50 -101.05
REMARK 500 9 ALA A 12 -74.16 -63.15
REMARK 500 9 ALA A 13 -33.42 -27.65
REMARK 500 9 ALA B 12 -79.66 -53.46
REMARK 500 9 ALA B 13 -1.75 -46.96
REMARK 500 9 GLU B 14 -60.92 -100.17
REMARK 500 9 ALA B 15 56.67 -100.22
REMARK 500 10 ALA A 12 -74.02 -55.46
REMARK 500 10 ALA A 13 -14.25 -42.18
REMARK 500
REMARK 500 THIS ENTRY HAS 73 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PC3 A 20
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 PC3 A 20 CO3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 9 NE2
REMARK 620 2 PC3 A 20 N2B 87.7
REMARK 620 3 PC3 A 20 N4B 87.7 91.0
REMARK 620 4 PC3 A 20 N6B 90.0 177.7 88.7
REMARK 620 5 PC3 A 20 N8B 93.4 90.9 177.9 89.5
REMARK 620 6 HIS B 9 NE2 177.1 92.5 89.4 89.8 89.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PC3 A 20
DBREF 1PBZ A 0 18 PDB 1PBZ 1PBZ 0 18
DBREF 1PBZ B 0 18 PDB 1PBZ 1PBZ 0 18
SEQRES 1 A 19 ACE CYS GLY ALA GLU ALA ALA LYS ALA HIS ALA LYS ALA
SEQRES 2 A 19 ALA GLU ALA GLY CYS NH2
SEQRES 1 B 19 ACE CYS GLY ALA GLU ALA ALA LYS ALA HIS ALA LYS ALA
SEQRES 2 B 19 ALA GLU ALA GLY CYS NH2
HET ACE A 0 6
HET NH2 A 18 3
HET ACE B 0 6
HET NH2 B 18 3
HET PC3 A 20 81
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
HETNAM PC3 COPROPORPHYRIN I CONTAINING CO(III)
FORMUL 1 ACE 2(C2 H4 O)
FORMUL 1 NH2 2(H2 N)
FORMUL 3 PC3 C36 H36 CO N4 O8
HELIX 1 1 GLY A 2 GLY A 16 1 15
HELIX 2 2 GLY B 2 ALA B 15 1 14
SSBOND 1 CYS A 1 CYS B 1 1555 1555 2.00
SSBOND 2 CYS A 17 CYS B 17 1555 1555 2.01
LINK C ACE A 0 N CYS A 1 1555 1555 1.33
LINK C CYS A 17 N NH2 A 18 1555 1555 1.32
LINK C ACE B 0 N CYS B 1 1555 1555 1.33
LINK C CYS B 17 N NH2 B 18 1555 1555 1.32
LINK NE2 HIS A 9 CO3 PC3 A 20 1555 1555 2.24
LINK CO3 PC3 A 20 NE2 HIS B 9 1555 1555 2.27
SITE 1 AC1 10 CYS A 1 ALA A 5 HIS A 9 ALA A 12
SITE 2 AC1 10 CYS A 17 NH2 A 18 CYS B 1 ALA B 8
SITE 3 AC1 10 HIS B 9 CYS B 17
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 - 23 20 Bytes