Header list of 1ivt.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL PROTEIN 29-MAR-02 1IVT
TITLE NMR STRUCTURES OF THE C-TERMINAL GLOBULAR DOMAIN OF HUMAN LAMIN A/C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LAMIN A/C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA BARREL, ALL SHEET, IG-FOLD, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR I.KRIMM,C.OSTLUND,B.GILQUIN,J.COUPRIE,P.HOSSENLOPP,J.P.MORNON,G.BONN,
AUTHOR 2 J.C.COURVALIN,H.J.WORMAN,S.ZINN-JUSTIN
REVDAT 4 23-FEB-22 1IVT 1 REMARK
REVDAT 3 24-FEB-09 1IVT 1 VERSN
REVDAT 2 01-APR-03 1IVT 1 JRNL
REVDAT 1 21-AUG-02 1IVT 0
JRNL AUTH I.KRIMM,C.OSTLUND,B.GILQUIN,J.COUPRIE,P.HOSSENLOPP,
JRNL AUTH 2 J.P.MORNON,G.BONNE,J.C.COURVALIN,H.J.WORMAN,S.ZINN-JUSTIN
JRNL TITL THE IG-LIKE STRUCTURE OF THE C-TERMINAL DOMAIN OF LAMIN A/C,
JRNL TITL 2 MUTATED IN MUSCULAR DYSTROPHIES, CARDIOMYOPATHY, AND PARTIAL
JRNL TITL 3 LIPODYSTROPHY.
JRNL REF STRUCTURE V. 10 811 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 12057196
JRNL DOI 10.1016/S0969-2126(02)00777-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IVT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000005318.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM U-15N,13C; 20MM PHOSPHATE
REMARK 210 BUFFER K; 1MM U-15N; 20MM
REMARK 210 PHOSPHATE BUFFER K; 1MM U-15N,
REMARK 210 13C; 20MM PHOSPHATE BUFFER K
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 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 : 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 SER A 458 N - CA - CB ANGL. DEV. = 10.4 DEGREES
REMARK 500 2 PHE A 451 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 2 SER A 458 N - CA - CB ANGL. DEV. = 10.0 DEGREES
REMARK 500 4 PHE A 487 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 4 PHE A 487 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 4 MET A 540 CA - CB - CG ANGL. DEV. = 10.4 DEGREES
REMARK 500 5 SER A 458 N - CA - CB ANGL. DEV. = 10.4 DEGREES
REMARK 500 5 LEU A 479 N - CA - CB ANGL. DEV. = -12.1 DEGREES
REMARK 500 5 TYR A 481 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 5 TYR A 481 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 SER A 458 N - CA - CB ANGL. DEV. = 9.4 DEGREES
REMARK 500 6 GLN A 468 N - CA - CB ANGL. DEV. = 11.5 DEGREES
REMARK 500 6 TYR A 481 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 6 TYR A 481 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 7 LEU A 454 CB - CG - CD1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 7 SER A 458 N - CA - CB ANGL. DEV. = 10.3 DEGREES
REMARK 500 8 SER A 458 N - CA - CB ANGL. DEV. = 10.9 DEGREES
REMARK 500 8 TYR A 481 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 8 TYR A 481 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 9 TYR A 481 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 9 TYR A 481 CB - CG - CD1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 9 SER A 546 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 10 SER A 458 N - CA - CB ANGL. DEV. = 9.1 DEGREES
REMARK 500 10 GLN A 468 N - CA - CB ANGL. DEV. = 11.6 DEGREES
REMARK 500 10 TYR A 481 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 10 TYR A 481 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 12 SER A 458 N - CA - CB ANGL. DEV. = 9.5 DEGREES
REMARK 500 12 TYR A 481 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 12 TYR A 481 CB - CG - CD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 13 PHE A 451 N - CA - CB ANGL. DEV. = 11.1 DEGREES
REMARK 500 13 SER A 458 N - CA - CB ANGL. DEV. = 9.7 DEGREES
REMARK 500 14 TYR A 481 CB - CG - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 14 TYR A 481 CB - CG - CD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 14 GLN A 493 N - CA - CB ANGL. DEV. = 11.2 DEGREES
REMARK 500 14 TRP A 520 CA - CB - CG ANGL. DEV. = 12.6 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 ARG A 439 6.05 -60.79
REMARK 500 1 GLU A 447 152.73 -25.41
REMARK 500 1 ASN A 459 51.49 -92.81
REMARK 500 1 SER A 463 93.71 -67.19
REMARK 500 1 ASP A 476 -153.94 -100.58
REMARK 500 1 PRO A 485 19.53 -64.30
REMARK 500 1 ALA A 491 84.42 -35.87
REMARK 500 1 TRP A 498 -163.30 -173.46
REMARK 500 1 ALA A 500 -30.01 -31.39
REMARK 500 1 SER A 507 62.97 -150.18
REMARK 500 1 PRO A 509 35.77 -94.38
REMARK 500 1 THR A 519 -163.85 164.77
REMARK 500 1 ASN A 532 -170.66 -55.82
REMARK 500 1 ARG A 545 -112.99 -112.35
REMARK 500 1 VAL A 547 68.81 82.51
REMARK 500 2 SER A 429 44.50 -102.61
REMARK 500 2 ARG A 439 7.01 -61.89
REMARK 500 2 GLU A 447 166.47 -45.92
REMARK 500 2 GLU A 448 -6.31 81.98
REMARK 500 2 ASN A 459 41.68 -88.81
REMARK 500 2 ASP A 461 102.57 -55.44
REMARK 500 2 PRO A 485 40.15 -66.74
REMARK 500 2 ALA A 491 82.19 -42.54
REMARK 500 2 TRP A 498 -157.92 -178.79
REMARK 500 2 ALA A 502 25.45 -74.66
REMARK 500 2 SER A 507 64.72 -150.67
REMARK 500 2 THR A 519 -156.97 170.89
REMARK 500 2 TRP A 520 -74.22 -133.27
REMARK 500 2 ASN A 532 -171.61 -53.31
REMARK 500 2 VAL A 538 -75.84 -114.05
REMARK 500 2 VAL A 547 43.83 -98.52
REMARK 500 2 THR A 548 -170.56 -178.46
REMARK 500 3 SER A 429 150.33 77.43
REMARK 500 3 ARG A 439 12.18 -65.24
REMARK 500 3 GLU A 447 -169.29 -65.82
REMARK 500 3 LYS A 450 -80.75 -91.57
REMARK 500 3 ASN A 459 49.98 -93.34
REMARK 500 3 MET A 464 21.64 -77.90
REMARK 500 3 ASP A 475 0.84 95.50
REMARK 500 3 PRO A 485 2.88 -51.78
REMARK 500 3 ALA A 491 86.04 -35.13
REMARK 500 3 TRP A 498 -156.84 -171.92
REMARK 500 3 PRO A 509 40.47 -92.92
REMARK 500 3 THR A 519 -160.21 180.00
REMARK 500 3 ASN A 532 -174.11 -59.49
REMARK 500 3 THR A 548 147.83 -176.38
REMARK 500 4 ARG A 439 13.37 -67.39
REMARK 500 4 GLU A 447 162.18 -37.13
REMARK 500 4 LYS A 450 -70.35 -83.33
REMARK 500 4 ASP A 461 102.11 -55.64
REMARK 500
REMARK 500 THIS ENTRY HAS 227 RAMACHANDRAN 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 PHE A 451 0.08 SIDE CHAIN
REMARK 500 3 PHE A 451 0.08 SIDE CHAIN
REMARK 500 3 PHE A 487 0.09 SIDE CHAIN
REMARK 500 4 TYR A 481 0.07 SIDE CHAIN
REMARK 500 5 PHE A 430 0.08 SIDE CHAIN
REMARK 500 5 PHE A 451 0.09 SIDE CHAIN
REMARK 500 5 PHE A 483 0.09 SIDE CHAIN
REMARK 500 6 TYR A 481 0.09 SIDE CHAIN
REMARK 500 8 ARG A 541 0.09 SIDE CHAIN
REMARK 500 9 PHE A 430 0.09 SIDE CHAIN
REMARK 500 9 TYR A 481 0.09 SIDE CHAIN
REMARK 500 10 TYR A 481 0.09 SIDE CHAIN
REMARK 500 12 PHE A 451 0.11 SIDE CHAIN
REMARK 500 12 ARG A 541 0.12 SIDE CHAIN
REMARK 500 13 TYR A 481 0.09 SIDE CHAIN
REMARK 500 14 PHE A 451 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IVT A 428 549 UNP P02545 LAMA_HUMAN 428 549
SEQRES 1 A 122 SER SER PHE SER GLN HIS ALA ARG THR SER GLY ARG VAL
SEQRES 2 A 122 ALA VAL GLU GLU VAL ASP GLU GLU GLY LYS PHE VAL ARG
SEQRES 3 A 122 LEU ARG ASN LYS SER ASN GLU ASP GLN SER MET GLY ASN
SEQRES 4 A 122 TRP GLN ILE LYS ARG GLN ASN GLY ASP ASP PRO LEU LEU
SEQRES 5 A 122 THR TYR ARG PHE PRO PRO LYS PHE THR LEU LYS ALA GLY
SEQRES 6 A 122 GLN VAL VAL THR ILE TRP ALA ALA GLY ALA GLY ALA THR
SEQRES 7 A 122 HIS SER PRO PRO THR ASP LEU VAL TRP LYS ALA GLN ASN
SEQRES 8 A 122 THR TRP GLY CYS GLY ASN SER LEU ARG THR ALA LEU ILE
SEQRES 9 A 122 ASN SER THR GLY GLU GLU VAL ALA MET ARG LYS LEU VAL
SEQRES 10 A 122 ARG SER VAL THR VAL
HELIX 1 1 SER A 463 ASN A 466 5 4
SHEET 1 A 5 SER A 431 THR A 436 0
SHEET 2 A 5 GLU A 537 VAL A 544 -1 O MET A 540 N ARG A 435
SHEET 3 A 5 SER A 525 ILE A 531 -1 N THR A 528 O ARG A 541
SHEET 4 A 5 GLN A 468 ASN A 473 -1 N GLN A 468 O ILE A 531
SHEET 5 A 5 LEU A 478 ARG A 482 -1 O TYR A 481 N ILE A 469
SHEET 1 B 4 ALA A 441 ASP A 446 0
SHEET 2 B 4 PHE A 451 ARG A 455 -1 O ARG A 455 N ALA A 441
SHEET 3 B 4 VAL A 494 ALA A 499 -1 O VAL A 495 N LEU A 454
SHEET 4 B 4 ASP A 511 TRP A 514 1 O LEU A 512 N TRP A 498
CISPEP 1 PRO A 508 PRO A 509 1 0.40
CISPEP 2 PRO A 508 PRO A 509 2 1.37
CISPEP 3 PRO A 508 PRO A 509 3 0.32
CISPEP 4 PRO A 508 PRO A 509 4 1.35
CISPEP 5 PRO A 508 PRO A 509 5 3.27
CISPEP 6 PRO A 508 PRO A 509 6 3.08
CISPEP 7 PRO A 508 PRO A 509 7 4.32
CISPEP 8 PRO A 508 PRO A 509 8 1.78
CISPEP 9 PRO A 508 PRO A 509 9 4.12
CISPEP 10 PRO A 508 PRO A 509 10 2.53
CISPEP 11 PRO A 508 PRO A 509 11 0.61
CISPEP 12 PRO A 508 PRO A 509 12 0.90
CISPEP 13 PRO A 508 PRO A 509 13 2.30
CISPEP 14 PRO A 508 PRO A 509 14 1.16
CISPEP 15 PRO A 508 PRO A 509 15 3.69
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