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HEADER HYDROLASE 11-JUN-24 8ZVQ
TITLE CRYO-EM STRUCTURE OF HUMAN HORMONE-SENSITIVE LIPASE (HSL)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HORMONE-SENSITIVE LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HSL,MONOACYLGLYCEROL LIPASE LIPE,RETINYL ESTER HYDROLASE,
COMPND 5 REH;
COMPND 6 EC: 3.1.1.79,3.1.1.23;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LIPE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS LIPID DROPLETS, LIPOLYSIS, HUMAN HORMONE-SENSITIVE LIPASE, HYDROLYSIS
KEYWDS 2 OF DIACYLGLYCEROL (DAG), HYDROLASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR H.PENG,Q.XU,J.WU,Q.HU
REVDAT 1 23-APR-25 8ZVQ 0
JRNL AUTH H.PENG,Q.XU,T.ZHANG,J.ZHU,J.PAN,X.GUAN,S.FENG,J.WU,Q.HU
JRNL TITL MOLECULAR DETERMINANTS FOR THE ASSOCIATION OF HUMAN
JRNL TITL 2 HORMONE-SENSITIVE LIPASE WITH LIPID DROPLETS.
JRNL REF NAT COMMUN V. 16 3497 2025
JRNL REFN ESSN 2041-1723
JRNL PMID 40221426
JRNL DOI 10.1038/S41467-025-58887-Z
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.400
REMARK 3 NUMBER OF PARTICLES : 384309
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 8ZVQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 14-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1300048633.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : HUMAN HORMONE-SENSITIVE LIPASE
REMARK 245 (HSL)
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : TFS KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 LEU A 3
REMARK 465 GLU A 199
REMARK 465 THR A 200
REMARK 465 GLY A 201
REMARK 465 LEU A 202
REMARK 465 SER A 203
REMARK 465 VAL A 204
REMARK 465 ALA A 205
REMARK 465 ALA A 206
REMARK 465 SER A 207
REMARK 465 SER A 208
REMARK 465 LEU A 209
REMARK 465 PHE A 210
REMARK 465 THR A 211
REMARK 465 SER A 212
REMARK 465 GLY A 213
REMARK 465 ASN A 325
REMARK 465 GLY A 326
REMARK 465 GLN A 327
REMARK 465 ARG A 328
REMARK 465 SER A 329
REMARK 465 LEU A 330
REMARK 465 GLU A 331
REMARK 465 LEU A 332
REMARK 465 TRP A 333
REMARK 465 PRO A 334
REMARK 465 ARG A 335
REMARK 465 PRO A 336
REMARK 465 GLU A 492
REMARK 465 ASP A 493
REMARK 465 HIS A 494
REMARK 465 SER A 495
REMARK 465 ASN A 496
REMARK 465 SER A 497
REMARK 465 ASP A 498
REMARK 465 GLN A 499
REMARK 465 LYS A 500
REMARK 465 ALA A 501
REMARK 465 LEU A 502
REMARK 465 GLY A 503
REMARK 465 MET A 504
REMARK 465 MET A 505
REMARK 465 GLY A 506
REMARK 465 LEU A 507
REMARK 465 VAL A 508
REMARK 465 ARG A 509
REMARK 465 ARG A 510
REMARK 465 ASP A 511
REMARK 465 THR A 512
REMARK 465 ALA A 513
REMARK 465 LEU A 514
REMARK 465 LEU A 515
REMARK 465 LEU A 516
REMARK 465 ARG A 517
REMARK 465 ASP A 518
REMARK 465 PHE A 519
REMARK 465 ARG A 520
REMARK 465 LEU A 521
REMARK 465 GLY A 522
REMARK 465 ALA A 523
REMARK 465 SER A 524
REMARK 465 SER A 525
REMARK 465 TRP A 526
REMARK 465 LEU A 527
REMARK 465 ASN A 528
REMARK 465 SER A 529
REMARK 465 PHE A 530
REMARK 465 LEU A 531
REMARK 465 GLU A 532
REMARK 465 LEU A 533
REMARK 465 SER A 534
REMARK 465 GLY A 535
REMARK 465 ARG A 536
REMARK 465 LYS A 537
REMARK 465 SER A 538
REMARK 465 GLN A 539
REMARK 465 LYS A 540
REMARK 465 MET A 541
REMARK 465 SER A 542
REMARK 465 GLU A 543
REMARK 465 PRO A 544
REMARK 465 ILE A 545
REMARK 465 ALA A 546
REMARK 465 GLU A 547
REMARK 465 PRO A 548
REMARK 465 MET A 549
REMARK 465 ARG A 550
REMARK 465 ARG A 551
REMARK 465 SER A 552
REMARK 465 VAL A 553
REMARK 465 SER A 554
REMARK 465 GLU A 555
REMARK 465 ALA A 556
REMARK 465 ALA A 557
REMARK 465 LEU A 558
REMARK 465 ALA A 559
REMARK 465 GLN A 560
REMARK 465 PRO A 561
REMARK 465 GLN A 562
REMARK 465 GLY A 563
REMARK 465 PRO A 564
REMARK 465 LEU A 565
REMARK 465 GLY A 566
REMARK 465 THR A 567
REMARK 465 ASP A 568
REMARK 465 SER A 569
REMARK 465 LEU A 570
REMARK 465 LYS A 571
REMARK 465 ASN A 572
REMARK 465 LEU A 573
REMARK 465 THR A 574
REMARK 465 LEU A 575
REMARK 465 ARG A 576
REMARK 465 ASP A 577
REMARK 465 LEU A 578
REMARK 465 SER A 579
REMARK 465 LEU A 580
REMARK 465 ARG A 581
REMARK 465 GLY A 582
REMARK 465 ASN A 583
REMARK 465 SER A 584
REMARK 465 GLU A 585
REMARK 465 THR A 586
REMARK 465 SER A 587
REMARK 465 SER A 588
REMARK 465 ASP A 589
REMARK 465 THR A 590
REMARK 465 PRO A 591
REMARK 465 GLU A 592
REMARK 465 MET A 593
REMARK 465 SER A 594
REMARK 465 LEU A 595
REMARK 465 SER A 596
REMARK 465 ALA A 597
REMARK 465 GLU A 598
REMARK 465 THR A 599
REMARK 465 LEU A 600
REMARK 465 SER A 601
REMARK 465 PRO A 602
REMARK 465 SER A 603
REMARK 465 THR A 604
REMARK 465 PRO A 605
REMARK 465 SER A 606
REMARK 465 ASP A 607
REMARK 465 VAL A 608
REMARK 465 ASN A 609
REMARK 465 PHE A 610
REMARK 465 LEU A 611
REMARK 465 LEU A 612
REMARK 465 PRO A 613
REMARK 465 PRO A 614
REMARK 465 GLU A 615
REMARK 465 ASP A 616
REMARK 465 ALA A 617
REMARK 465 GLY A 618
REMARK 465 GLU A 619
REMARK 465 GLU A 620
REMARK 465 ALA A 621
REMARK 465 GLU A 622
REMARK 465 ALA A 623
REMARK 465 LYS A 624
REMARK 465 ASN A 625
REMARK 465 GLU A 626
REMARK 465 LEU A 627
REMARK 465 SER A 628
REMARK 465 PRO A 629
REMARK 465 MET A 630
REMARK 465 ASP A 631
REMARK 465 ARG A 632
REMARK 465 GLY A 633
REMARK 465 LEU A 634
REMARK 465 GLY A 635
REMARK 465 VAL A 636
REMARK 465 ARG A 637
REMARK 465 PRO A 753
REMARK 465 ALA A 754
REMARK 465 GLY A 755
REMARK 465 ALA A 756
REMARK 465 GLY A 757
REMARK 465 PRO A 758
REMARK 465 SER A 759
REMARK 465 GLY A 760
REMARK 465 GLU A 761
REMARK 465 THR A 762
REMARK 465 GLY A 763
REMARK 465 ALA A 764
REMARK 465 ALA A 765
REMARK 465 GLY A 766
REMARK 465 VAL A 767
REMARK 465 ASP A 768
REMARK 465 GLY A 769
REMARK 465 GLY A 770
REMARK 465 CYS A 771
REMARK 465 GLY A 772
REMARK 465 GLY A 773
REMARK 465 ARG A 774
REMARK 465 HIS A 775
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 LEU B 3
REMARK 465 GLU B 199
REMARK 465 THR B 200
REMARK 465 GLY B 201
REMARK 465 LEU B 202
REMARK 465 SER B 203
REMARK 465 VAL B 204
REMARK 465 ALA B 205
REMARK 465 ALA B 206
REMARK 465 SER B 207
REMARK 465 SER B 208
REMARK 465 LEU B 209
REMARK 465 PHE B 210
REMARK 465 THR B 211
REMARK 465 SER B 212
REMARK 465 GLY B 213
REMARK 465 ASN B 325
REMARK 465 GLY B 326
REMARK 465 GLN B 327
REMARK 465 ARG B 328
REMARK 465 SER B 329
REMARK 465 LEU B 330
REMARK 465 GLU B 331
REMARK 465 LEU B 332
REMARK 465 TRP B 333
REMARK 465 PRO B 334
REMARK 465 ARG B 335
REMARK 465 PRO B 336
REMARK 465 GLU B 492
REMARK 465 ASP B 493
REMARK 465 HIS B 494
REMARK 465 SER B 495
REMARK 465 ASN B 496
REMARK 465 SER B 497
REMARK 465 ASP B 498
REMARK 465 GLN B 499
REMARK 465 LYS B 500
REMARK 465 ALA B 501
REMARK 465 LEU B 502
REMARK 465 GLY B 503
REMARK 465 MET B 504
REMARK 465 MET B 505
REMARK 465 GLY B 506
REMARK 465 LEU B 507
REMARK 465 VAL B 508
REMARK 465 ARG B 509
REMARK 465 ARG B 510
REMARK 465 ASP B 511
REMARK 465 THR B 512
REMARK 465 ALA B 513
REMARK 465 LEU B 514
REMARK 465 LEU B 515
REMARK 465 LEU B 516
REMARK 465 ARG B 517
REMARK 465 ASP B 518
REMARK 465 PHE B 519
REMARK 465 ARG B 520
REMARK 465 LEU B 521
REMARK 465 GLY B 522
REMARK 465 ALA B 523
REMARK 465 SER B 524
REMARK 465 SER B 525
REMARK 465 TRP B 526
REMARK 465 LEU B 527
REMARK 465 ASN B 528
REMARK 465 SER B 529
REMARK 465 PHE B 530
REMARK 465 LEU B 531
REMARK 465 GLU B 532
REMARK 465 LEU B 533
REMARK 465 SER B 534
REMARK 465 GLY B 535
REMARK 465 ARG B 536
REMARK 465 LYS B 537
REMARK 465 SER B 538
REMARK 465 GLN B 539
REMARK 465 LYS B 540
REMARK 465 MET B 541
REMARK 465 SER B 542
REMARK 465 GLU B 543
REMARK 465 PRO B 544
REMARK 465 ILE B 545
REMARK 465 ALA B 546
REMARK 465 GLU B 547
REMARK 465 PRO B 548
REMARK 465 MET B 549
REMARK 465 ARG B 550
REMARK 465 ARG B 551
REMARK 465 SER B 552
REMARK 465 VAL B 553
REMARK 465 SER B 554
REMARK 465 GLU B 555
REMARK 465 ALA B 556
REMARK 465 ALA B 557
REMARK 465 LEU B 558
REMARK 465 ALA B 559
REMARK 465 GLN B 560
REMARK 465 PRO B 561
REMARK 465 GLN B 562
REMARK 465 GLY B 563
REMARK 465 PRO B 564
REMARK 465 LEU B 565
REMARK 465 GLY B 566
REMARK 465 THR B 567
REMARK 465 ASP B 568
REMARK 465 SER B 569
REMARK 465 LEU B 570
REMARK 465 LYS B 571
REMARK 465 ASN B 572
REMARK 465 LEU B 573
REMARK 465 THR B 574
REMARK 465 LEU B 575
REMARK 465 ARG B 576
REMARK 465 ASP B 577
REMARK 465 LEU B 578
REMARK 465 SER B 579
REMARK 465 LEU B 580
REMARK 465 ARG B 581
REMARK 465 GLY B 582
REMARK 465 ASN B 583
REMARK 465 SER B 584
REMARK 465 GLU B 585
REMARK 465 THR B 586
REMARK 465 SER B 587
REMARK 465 SER B 588
REMARK 465 ASP B 589
REMARK 465 THR B 590
REMARK 465 PRO B 591
REMARK 465 GLU B 592
REMARK 465 MET B 593
REMARK 465 SER B 594
REMARK 465 LEU B 595
REMARK 465 SER B 596
REMARK 465 ALA B 597
REMARK 465 GLU B 598
REMARK 465 THR B 599
REMARK 465 LEU B 600
REMARK 465 SER B 601
REMARK 465 PRO B 602
REMARK 465 SER B 603
REMARK 465 THR B 604
REMARK 465 PRO B 605
REMARK 465 SER B 606
REMARK 465 ASP B 607
REMARK 465 VAL B 608
REMARK 465 ASN B 609
REMARK 465 PHE B 610
REMARK 465 LEU B 611
REMARK 465 LEU B 612
REMARK 465 PRO B 613
REMARK 465 PRO B 614
REMARK 465 GLU B 615
REMARK 465 ASP B 616
REMARK 465 ALA B 617
REMARK 465 GLY B 618
REMARK 465 GLU B 619
REMARK 465 GLU B 620
REMARK 465 ALA B 621
REMARK 465 GLU B 622
REMARK 465 ALA B 623
REMARK 465 LYS B 624
REMARK 465 ASN B 625
REMARK 465 GLU B 626
REMARK 465 LEU B 627
REMARK 465 SER B 628
REMARK 465 PRO B 629
REMARK 465 MET B 630
REMARK 465 ASP B 631
REMARK 465 ARG B 632
REMARK 465 GLY B 633
REMARK 465 LEU B 634
REMARK 465 GLY B 635
REMARK 465 VAL B 636
REMARK 465 ARG B 637
REMARK 465 PRO B 753
REMARK 465 ALA B 754
REMARK 465 GLY B 755
REMARK 465 ALA B 756
REMARK 465 GLY B 757
REMARK 465 PRO B 758
REMARK 465 SER B 759
REMARK 465 GLY B 760
REMARK 465 GLU B 761
REMARK 465 THR B 762
REMARK 465 GLY B 763
REMARK 465 ALA B 764
REMARK 465 ALA B 765
REMARK 465 GLY B 766
REMARK 465 VAL B 767
REMARK 465 ASP B 768
REMARK 465 GLY B 769
REMARK 465 GLY B 770
REMARK 465 CYS B 771
REMARK 465 GLY B 772
REMARK 465 GLY B 773
REMARK 465 ARG B 774
REMARK 465 HIS B 775
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 ARG A 178 NE2 GLN A 182 1.53
REMARK 500 NH1 ARG A 262 O TYR A 307 1.60
REMARK 500 O ARG A 178 CD GLN A 182 1.70
REMARK 500 CA PRO A 179 OE1 GLN A 182 1.78
REMARK 500 C ARG A 178 NE2 GLN A 182 1.81
REMARK 500 O ARG A 178 OE1 GLN A 182 1.87
REMARK 500 C PRO A 179 OE1 GLN A 182 2.01
REMARK 500 O PRO A 179 OE1 GLN A 182 2.17
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 LEU A 728 CA - CB - CG ANGL. DEV. = 17.2 DEGREES
REMARK 500 PRO A 752 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO A 752 N - CD - CG ANGL. DEV. = -10.3 DEGREES
REMARK 500 LEU B 140 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 LEU B 140 CB - CG - CD2 ANGL. DEV. = -10.3 DEGREES
REMARK 500 LEU B 188 CA - CB - CG ANGL. DEV. = 18.7 DEGREES
REMARK 500 LEU B 474 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 LEU B 728 CA - CB - CG ANGL. DEV. = 21.5 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 CYS A 168 30.52 -89.80
REMARK 500 ARG A 262 -37.40 -130.92
REMARK 500 PRO A 340 -167.45 -77.25
REMARK 500 PHE A 354 13.74 56.55
REMARK 500 HIS A 407 54.11 -93.07
REMARK 500 TYR A 452 68.72 37.41
REMARK 500 LEU A 467 47.12 -91.36
REMARK 500 PRO A 662 -5.01 -58.10
REMARK 500 LEU A 728 27.86 -140.98
REMARK 500 LEU A 731 -36.26 -130.49
REMARK 500 ARG B 262 -32.29 -130.50
REMARK 500 HIS B 294 40.08 39.59
REMARK 500 TYR B 452 70.64 39.54
REMARK 500 LEU B 467 44.56 -89.01
REMARK 500 MET B 695 48.51 -86.73
REMARK 500 ALA B 730 34.74 -95.73
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 ARG A 417 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-60512 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF HUMAN HORMONE-SENSITIVE LIPASE (HSL)
DBREF 8ZVQ A 1 775 UNP Q05469 LIPS_HUMAN 302 1076
DBREF 8ZVQ B 1 775 UNP Q05469 LIPS_HUMAN 302 1076
SEQRES 1 A 775 MET ASP LEU ARG THR MET THR GLN SER LEU VAL THR LEU
SEQRES 2 A 775 ALA GLU ASP ASN ILE ALA PHE PHE SER SER GLN GLY PRO
SEQRES 3 A 775 GLY GLU THR ALA GLN ARG LEU SER GLY VAL PHE ALA GLY
SEQRES 4 A 775 VAL ARG GLU GLN ALA LEU GLY LEU GLU PRO ALA LEU GLY
SEQRES 5 A 775 ARG LEU LEU GLY VAL ALA HIS LEU PHE ASP LEU ASP PRO
SEQRES 6 A 775 GLU THR PRO ALA ASN GLY TYR ARG SER LEU VAL HIS THR
SEQRES 7 A 775 ALA ARG CYS CYS LEU ALA HIS LEU LEU HIS LYS SER ARG
SEQRES 8 A 775 TYR VAL ALA SER ASN ARG ARG SER ILE PHE PHE ARG THR
SEQRES 9 A 775 SER HIS ASN LEU ALA GLU LEU GLU ALA TYR LEU ALA ALA
SEQRES 10 A 775 LEU THR GLN LEU ARG ALA LEU VAL TYR TYR ALA GLN ARG
SEQRES 11 A 775 LEU LEU VAL THR ASN ARG PRO GLY VAL LEU PHE PHE GLU
SEQRES 12 A 775 GLY ASP GLU GLY LEU THR ALA ASP PHE LEU ARG GLU TYR
SEQRES 13 A 775 VAL THR LEU HIS LYS GLY CYS PHE TYR GLY ARG CYS LEU
SEQRES 14 A 775 GLY PHE GLN PHE THR PRO ALA ILE ARG PRO PHE LEU GLN
SEQRES 15 A 775 THR ILE SER ILE GLY LEU VAL SER PHE GLY GLU HIS TYR
SEQRES 16 A 775 LYS ARG ASN GLU THR GLY LEU SER VAL ALA ALA SER SER
SEQRES 17 A 775 LEU PHE THR SER GLY ARG PHE ALA ILE ASP PRO GLU LEU
SEQRES 18 A 775 ARG GLY ALA GLU PHE GLU ARG ILE THR GLN ASN LEU ASP
SEQRES 19 A 775 VAL HIS PHE TRP LYS ALA PHE TRP ASN ILE THR GLU MET
SEQRES 20 A 775 GLU VAL LEU SER SER LEU ALA ASN MET ALA SER ALA THR
SEQRES 21 A 775 VAL ARG VAL SER ARG LEU LEU SER LEU PRO PRO GLU ALA
SEQRES 22 A 775 PHE GLU MET PRO LEU THR ALA ASP PRO THR LEU THR VAL
SEQRES 23 A 775 THR ILE SER PRO PRO LEU ALA HIS THR GLY PRO GLY PRO
SEQRES 24 A 775 VAL LEU VAL ARG LEU ILE SER TYR ASP LEU ARG GLU GLY
SEQRES 25 A 775 GLN ASP SER GLU GLU LEU SER SER LEU ILE LYS SER ASN
SEQRES 26 A 775 GLY GLN ARG SER LEU GLU LEU TRP PRO ARG PRO GLN GLN
SEQRES 27 A 775 ALA PRO ARG SER ARG SER LEU ILE VAL HIS PHE HIS GLY
SEQRES 28 A 775 GLY GLY PHE VAL ALA GLN THR SER ARG SER HIS GLU PRO
SEQRES 29 A 775 TYR LEU LYS SER TRP ALA GLN GLU LEU GLY ALA PRO ILE
SEQRES 30 A 775 ILE SER ILE ASP TYR SER LEU ALA PRO GLU ALA PRO PHE
SEQRES 31 A 775 PRO ARG ALA LEU GLU GLU CYS PHE PHE ALA TYR CYS TRP
SEQRES 32 A 775 ALA ILE LYS HIS CYS ALA LEU LEU GLY SER THR GLY GLU
SEQRES 33 A 775 ARG ILE CYS LEU ALA GLY ASP SER ALA GLY GLY ASN LEU
SEQRES 34 A 775 CYS PHE THR VAL ALA LEU ARG ALA ALA ALA TYR GLY VAL
SEQRES 35 A 775 ARG VAL PRO ASP GLY ILE MET ALA ALA TYR PRO ALA THR
SEQRES 36 A 775 MET LEU GLN PRO ALA ALA SER PRO SER ARG LEU LEU SER
SEQRES 37 A 775 LEU MET ASP PRO LEU LEU PRO LEU SER VAL LEU SER LYS
SEQRES 38 A 775 CYS VAL SER ALA TYR ALA GLY ALA LYS THR GLU ASP HIS
SEQRES 39 A 775 SER ASN SER ASP GLN LYS ALA LEU GLY MET MET GLY LEU
SEQRES 40 A 775 VAL ARG ARG ASP THR ALA LEU LEU LEU ARG ASP PHE ARG
SEQRES 41 A 775 LEU GLY ALA SER SER TRP LEU ASN SER PHE LEU GLU LEU
SEQRES 42 A 775 SER GLY ARG LYS SER GLN LYS MET SER GLU PRO ILE ALA
SEQRES 43 A 775 GLU PRO MET ARG ARG SER VAL SER GLU ALA ALA LEU ALA
SEQRES 44 A 775 GLN PRO GLN GLY PRO LEU GLY THR ASP SER LEU LYS ASN
SEQRES 45 A 775 LEU THR LEU ARG ASP LEU SER LEU ARG GLY ASN SER GLU
SEQRES 46 A 775 THR SER SER ASP THR PRO GLU MET SER LEU SER ALA GLU
SEQRES 47 A 775 THR LEU SER PRO SER THR PRO SER ASP VAL ASN PHE LEU
SEQRES 48 A 775 LEU PRO PRO GLU ASP ALA GLY GLU GLU ALA GLU ALA LYS
SEQRES 49 A 775 ASN GLU LEU SER PRO MET ASP ARG GLY LEU GLY VAL ARG
SEQRES 50 A 775 ALA ALA PHE PRO GLU GLY PHE HIS PRO ARG ARG SER SER
SEQRES 51 A 775 GLN GLY ALA THR GLN MET PRO LEU TYR SER SER PRO ILE
SEQRES 52 A 775 VAL LYS ASN PRO PHE MET SER PRO LEU LEU ALA PRO ASP
SEQRES 53 A 775 SER MET LEU LYS SER LEU PRO PRO VAL HIS ILE VAL ALA
SEQRES 54 A 775 CYS ALA LEU ASP PRO MET LEU ASP ASP SER VAL MET LEU
SEQRES 55 A 775 ALA ARG ARG LEU ARG ASN LEU GLY GLN PRO VAL THR LEU
SEQRES 56 A 775 ARG VAL VAL GLU ASP LEU PRO HIS GLY PHE LEU THR LEU
SEQRES 57 A 775 ALA ALA LEU CYS ARG GLU THR ARG GLN ALA ALA GLU LEU
SEQRES 58 A 775 CYS VAL GLU ARG ILE ARG LEU VAL LEU THR PRO PRO ALA
SEQRES 59 A 775 GLY ALA GLY PRO SER GLY GLU THR GLY ALA ALA GLY VAL
SEQRES 60 A 775 ASP GLY GLY CYS GLY GLY ARG HIS
SEQRES 1 B 775 MET ASP LEU ARG THR MET THR GLN SER LEU VAL THR LEU
SEQRES 2 B 775 ALA GLU ASP ASN ILE ALA PHE PHE SER SER GLN GLY PRO
SEQRES 3 B 775 GLY GLU THR ALA GLN ARG LEU SER GLY VAL PHE ALA GLY
SEQRES 4 B 775 VAL ARG GLU GLN ALA LEU GLY LEU GLU PRO ALA LEU GLY
SEQRES 5 B 775 ARG LEU LEU GLY VAL ALA HIS LEU PHE ASP LEU ASP PRO
SEQRES 6 B 775 GLU THR PRO ALA ASN GLY TYR ARG SER LEU VAL HIS THR
SEQRES 7 B 775 ALA ARG CYS CYS LEU ALA HIS LEU LEU HIS LYS SER ARG
SEQRES 8 B 775 TYR VAL ALA SER ASN ARG ARG SER ILE PHE PHE ARG THR
SEQRES 9 B 775 SER HIS ASN LEU ALA GLU LEU GLU ALA TYR LEU ALA ALA
SEQRES 10 B 775 LEU THR GLN LEU ARG ALA LEU VAL TYR TYR ALA GLN ARG
SEQRES 11 B 775 LEU LEU VAL THR ASN ARG PRO GLY VAL LEU PHE PHE GLU
SEQRES 12 B 775 GLY ASP GLU GLY LEU THR ALA ASP PHE LEU ARG GLU TYR
SEQRES 13 B 775 VAL THR LEU HIS LYS GLY CYS PHE TYR GLY ARG CYS LEU
SEQRES 14 B 775 GLY PHE GLN PHE THR PRO ALA ILE ARG PRO PHE LEU GLN
SEQRES 15 B 775 THR ILE SER ILE GLY LEU VAL SER PHE GLY GLU HIS TYR
SEQRES 16 B 775 LYS ARG ASN GLU THR GLY LEU SER VAL ALA ALA SER SER
SEQRES 17 B 775 LEU PHE THR SER GLY ARG PHE ALA ILE ASP PRO GLU LEU
SEQRES 18 B 775 ARG GLY ALA GLU PHE GLU ARG ILE THR GLN ASN LEU ASP
SEQRES 19 B 775 VAL HIS PHE TRP LYS ALA PHE TRP ASN ILE THR GLU MET
SEQRES 20 B 775 GLU VAL LEU SER SER LEU ALA ASN MET ALA SER ALA THR
SEQRES 21 B 775 VAL ARG VAL SER ARG LEU LEU SER LEU PRO PRO GLU ALA
SEQRES 22 B 775 PHE GLU MET PRO LEU THR ALA ASP PRO THR LEU THR VAL
SEQRES 23 B 775 THR ILE SER PRO PRO LEU ALA HIS THR GLY PRO GLY PRO
SEQRES 24 B 775 VAL LEU VAL ARG LEU ILE SER TYR ASP LEU ARG GLU GLY
SEQRES 25 B 775 GLN ASP SER GLU GLU LEU SER SER LEU ILE LYS SER ASN
SEQRES 26 B 775 GLY GLN ARG SER LEU GLU LEU TRP PRO ARG PRO GLN GLN
SEQRES 27 B 775 ALA PRO ARG SER ARG SER LEU ILE VAL HIS PHE HIS GLY
SEQRES 28 B 775 GLY GLY PHE VAL ALA GLN THR SER ARG SER HIS GLU PRO
SEQRES 29 B 775 TYR LEU LYS SER TRP ALA GLN GLU LEU GLY ALA PRO ILE
SEQRES 30 B 775 ILE SER ILE ASP TYR SER LEU ALA PRO GLU ALA PRO PHE
SEQRES 31 B 775 PRO ARG ALA LEU GLU GLU CYS PHE PHE ALA TYR CYS TRP
SEQRES 32 B 775 ALA ILE LYS HIS CYS ALA LEU LEU GLY SER THR GLY GLU
SEQRES 33 B 775 ARG ILE CYS LEU ALA GLY ASP SER ALA GLY GLY ASN LEU
SEQRES 34 B 775 CYS PHE THR VAL ALA LEU ARG ALA ALA ALA TYR GLY VAL
SEQRES 35 B 775 ARG VAL PRO ASP GLY ILE MET ALA ALA TYR PRO ALA THR
SEQRES 36 B 775 MET LEU GLN PRO ALA ALA SER PRO SER ARG LEU LEU SER
SEQRES 37 B 775 LEU MET ASP PRO LEU LEU PRO LEU SER VAL LEU SER LYS
SEQRES 38 B 775 CYS VAL SER ALA TYR ALA GLY ALA LYS THR GLU ASP HIS
SEQRES 39 B 775 SER ASN SER ASP GLN LYS ALA LEU GLY MET MET GLY LEU
SEQRES 40 B 775 VAL ARG ARG ASP THR ALA LEU LEU LEU ARG ASP PHE ARG
SEQRES 41 B 775 LEU GLY ALA SER SER TRP LEU ASN SER PHE LEU GLU LEU
SEQRES 42 B 775 SER GLY ARG LYS SER GLN LYS MET SER GLU PRO ILE ALA
SEQRES 43 B 775 GLU PRO MET ARG ARG SER VAL SER GLU ALA ALA LEU ALA
SEQRES 44 B 775 GLN PRO GLN GLY PRO LEU GLY THR ASP SER LEU LYS ASN
SEQRES 45 B 775 LEU THR LEU ARG ASP LEU SER LEU ARG GLY ASN SER GLU
SEQRES 46 B 775 THR SER SER ASP THR PRO GLU MET SER LEU SER ALA GLU
SEQRES 47 B 775 THR LEU SER PRO SER THR PRO SER ASP VAL ASN PHE LEU
SEQRES 48 B 775 LEU PRO PRO GLU ASP ALA GLY GLU GLU ALA GLU ALA LYS
SEQRES 49 B 775 ASN GLU LEU SER PRO MET ASP ARG GLY LEU GLY VAL ARG
SEQRES 50 B 775 ALA ALA PHE PRO GLU GLY PHE HIS PRO ARG ARG SER SER
SEQRES 51 B 775 GLN GLY ALA THR GLN MET PRO LEU TYR SER SER PRO ILE
SEQRES 52 B 775 VAL LYS ASN PRO PHE MET SER PRO LEU LEU ALA PRO ASP
SEQRES 53 B 775 SER MET LEU LYS SER LEU PRO PRO VAL HIS ILE VAL ALA
SEQRES 54 B 775 CYS ALA LEU ASP PRO MET LEU ASP ASP SER VAL MET LEU
SEQRES 55 B 775 ALA ARG ARG LEU ARG ASN LEU GLY GLN PRO VAL THR LEU
SEQRES 56 B 775 ARG VAL VAL GLU ASP LEU PRO HIS GLY PHE LEU THR LEU
SEQRES 57 B 775 ALA ALA LEU CYS ARG GLU THR ARG GLN ALA ALA GLU LEU
SEQRES 58 B 775 CYS VAL GLU ARG ILE ARG LEU VAL LEU THR PRO PRO ALA
SEQRES 59 B 775 GLY ALA GLY PRO SER GLY GLU THR GLY ALA ALA GLY VAL
SEQRES 60 B 775 ASP GLY GLY CYS GLY GLY ARG HIS
HELIX 1 1 THR A 5 SER A 23 1 19
HELIX 2 2 GLU A 28 PHE A 61 1 34
HELIX 3 3 GLY A 71 ASN A 96 1 26
HELIX 4 4 THR A 104 THR A 134 1 31
HELIX 5 5 GLU A 146 THR A 158 1 13
HELIX 6 6 GLY A 162 TYR A 165 1 4
HELIX 7 7 PRO A 175 ARG A 197 1 23
HELIX 8 9 PRO A 219 ASN A 232 1 14
HELIX 9 10 VAL A 235 GLU A 246 1 12
HELIX 10 11 GLU A 248 MET A 256 1 9
HELIX 11 12 GLU A 316 LEU A 321 1 6
HELIX 12 13 SER A 359 LEU A 373 1 15
HELIX 13 14 ARG A 392 LYS A 406 1 15
HELIX 14 15 SER A 424 ALA A 439 1 16
HELIX 15 16 SER A 464 LEU A 469 5 6
HELIX 16 17 LEU A 476 TYR A 486 1 11
HELIX 17 18 PRO A 662 LYS A 665 5 4
HELIX 18 19 PRO A 671 LEU A 673 5 3
HELIX 19 20 ASP A 676 SER A 681 1 6
HELIX 20 21 LEU A 696 ASN A 708 1 13
HELIX 21 22 PHE A 725 LEU A 728 5 4
HELIX 22 23 ARG A 733 LEU A 750 1 18
HELIX 23 24 THR B 5 SER B 23 1 19
HELIX 24 25 GLU B 28 PHE B 61 1 34
HELIX 25 26 GLY B 71 ASN B 96 1 26
HELIX 26 27 THR B 104 THR B 134 1 31
HELIX 27 28 GLU B 146 THR B 158 1 13
HELIX 28 29 GLY B 162 TYR B 165 1 4
HELIX 29 30 PRO B 175 ARG B 197 1 23
HELIX 30 32 PRO B 219 ASN B 232 1 14
HELIX 31 33 VAL B 235 GLU B 246 1 12
HELIX 32 34 GLU B 248 MET B 256 1 9
HELIX 33 35 GLU B 316 LEU B 321 1 6
HELIX 34 36 SER B 359 LEU B 373 1 15
HELIX 35 37 ARG B 392 LYS B 406 1 15
HELIX 36 38 SER B 424 ALA B 439 1 16
HELIX 37 39 SER B 464 LEU B 469 5 6
HELIX 38 40 LEU B 476 TYR B 486 1 11
HELIX 39 41 PRO B 662 LYS B 665 5 4
HELIX 40 42 PRO B 671 LEU B 673 5 3
HELIX 41 43 ASP B 676 SER B 681 1 6
HELIX 42 44 LEU B 696 ASN B 708 1 13
HELIX 43 45 PHE B 725 LEU B 728 5 4
HELIX 44 46 ARG B 733 LEU B 750 1 18
SHEET 1 A 2 VAL A 263 LEU A 269 0
SHEET 2 A 2 VAL A 300 SER A 306 -1 N SER A 306 O VAL A 263
SHEET 1 B 2 PHE A 274 PRO A 277 0
SHEET 2 B 2 THR A 285 ILE A 288 -1 N ILE A 288 O PHE A 274
SHEET 1 C 4 PRO A 376 ILE A 380 0
SHEET 2 C 4 SER A 344 PHE A 349 1 N ILE A 346 O PRO A 376
SHEET 3 C 4 ARG A 417 ASP A 423 1 N ARG A 417 O LEU A 345
SHEET 4 C 4 GLY A 447 ALA A 451 1 N GLY A 447 O LEU A 420
SHEET 1 D 2 VAL A 685 CYS A 690 0
SHEET 2 D 2 VAL A 713 VAL A 718 1 N THR A 714 O VAL A 685
SHEET 1 E 2 VAL B 263 LEU B 269 0
SHEET 2 E 2 VAL B 300 SER B 306 -1 N SER B 306 O VAL B 263
SHEET 1 F 2 PHE B 274 PRO B 277 0
SHEET 2 F 2 THR B 285 ILE B 288 -1 N ILE B 288 O PHE B 274
SHEET 1 G 4 PRO B 376 ILE B 380 0
SHEET 2 G 4 SER B 344 PHE B 349 1 N ILE B 346 O PRO B 376
SHEET 3 G 4 ARG B 417 ASP B 423 1 N ARG B 417 O LEU B 345
SHEET 4 G 4 GLY B 447 ALA B 451 1 N GLY B 447 O LEU B 420
SHEET 1 H 2 VAL B 685 CYS B 690 0
SHEET 2 H 2 VAL B 713 VAL B 718 1 N THR B 714 O VAL B 685
CISPEP 1 ALA A 385 PRO A 386 0 -0.38
CISPEP 2 PHE A 390 PRO A 391 0 2.80
CISPEP 3 ALA B 385 PRO B 386 0 2.30
CISPEP 4 PHE B 390 PRO B 391 0 2.75
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
TER 4449 PRO A 752
TER 8898 PRO B 752
MASTER 595 0 0 44 20 0 0 6 8896 2 0 120
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